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n3:pmcid
PMC0
bibo:doi
10.1186%2Fs13046-014-0062-0
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n2:Section
dc:title
introduction
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The Snail superfamily of transcription factors includes Snail1, Slug, and Scratch proteins, all of which share a SNAG domain and at least four functional zinc fingers [>>1<<]. Snail1 has four zinc fingers, located from amino acids 154 to 259, whereas Scratch and Slug each have five [2],[3].
n3:mentions
n4:11994736
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Snail1 has four zinc fingers, located from amino acids 154 to 259, whereas Scratch and Slug each have five [>>2<<],[3]. The comparison of these zinc-finger sequences has further subdivided the superfamily into Snail and Scratch families, with Slug acting as a subfamily within the Snail grouping. The Snail superfamily has been implicated in various
n3:mentions
n4:3683556
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_:vb33215957
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Snail1 has four zinc fingers, located from amino acids 154 to 259, whereas Scratch and Slug each have five [2],[>>3<<]. The comparison of these zinc-finger sequences has further subdivided the superfamily into Snail and Scratch families, with Slug acting as a subfamily within the Snail grouping. The Snail superfamily has been implicated in various
n3:mentions
n4:11275308
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The Snail superfamily has been implicated in various processes relating to cell differentiation and survival [>>1<<].
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n4:11994736
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First characterized in Drosophila melanogaster in 1984, Snail1 also has well-documented homologs in Xenopus, C. elegans, mice, chicks, and humans [>>4<<],[5]. In humans, Snail1 is expressed in the kidney, thyroid, adrenal gland, lungs, placenta, lymph nodes, heart, brain, liver, and skeletal muscle tissues [6],[7].
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In humans, Snail1 is expressed in the kidney, thyroid, adrenal gland, lungs, placenta, lymph nodes, heart, brain, liver, and skeletal muscle tissues [>>6<<],[7]. Snail1 is a C2H2 zinc-finger protein composed of 264 amino acids, with a molecular weight of 29.1 kDa [7] (Figure 1). The SNAI1 gene, which is 2.0 kb and contains 3 exons, has been mapped to chromosome 20q.13.2 between markers
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n3:Context
rdf:value
In humans, Snail1 is expressed in the kidney, thyroid, adrenal gland, lungs, placenta, lymph nodes, heart, brain, liver, and skeletal muscle tissues [6],[>>7<<]. Snail1 is a C2H2 zinc-finger protein composed of 264 amino acids, with a molecular weight of 29.1 kDa [7] (Figure 1). The SNAI1 gene, which is 2.0 kb and contains 3 exons, has been mapped to chromosome 20q.13.2 between markers D20S886
n3:mentions
n4:10585766
Subject Item
_:vb33215962
rdf:type
n3:Context
rdf:value
Snail1 is a C2H2 zinc-finger protein composed of 264 amino acids, with a molecular weight of 29.1 kDa [>>7<<] (Figure 1).
n3:mentions
n4:10585766
Subject Item
_:vb33215963
rdf:type
n3:Context
rdf:value
13.2 between markers D20S886 and D20S109 [>>7<<]. A Snail1 retrogene (SNAI1P) exists on human chromosome 2 [8].
n3:mentions
n4:10585766
Subject Item
_:vb33215964
rdf:type
n3:Context
rdf:value
13.2 between markers D20S886 and D20S109 [7]. A Snail1 retrogene (SNAI1P) exists on human chromosome 2 [>>8<<].
n3:mentions
n4:19427053
Subject Item
_:vb33215965
rdf:type
n3:Context
rdf:value
The expression of mesenchymal markers, like vimentin and fibronectin, replaces that of the usual epithelial markers, including E-cadherin, cytokeratins and Mucin-1 [>>10<<]. EMT is fundamental to both normal developmental processes and metastatic cancer. The induction of epithelial-to-mesenchymal transition (EMT) is Snail1’s most studied function, as this process is crucial for the formation of the mesoderm
n3:mentions
n4:19487818
Subject Item
_:vb33215966
rdf:type
n3:Context
rdf:value
The induction of epithelial-to-mesenchymal transition (EMT) is Snail1’s most studied function, as this process is crucial for the formation of the mesoderm and the neural crest [>>1<<]. Snail1 knockout in mice is lethal because gastrulation does not occur [11]. The primary mechanism of Snail1-induced EMT is the repression of E-cadherin, which causes reduced cell adhesion and promotes migratory capacity [12]. The
n3:mentions
n4:11994736
Subject Item
_:vb33215967
rdf:type
n3:Context
rdf:value
Snail1 knockout in mice is lethal because gastrulation does not occur [>>11<<]. The primary mechanism of Snail1-induced EMT is the repression of E-cadherin, which causes reduced cell adhesion and promotes migratory capacity [12].
n3:mentions
n4:11689706
Subject Item
_:vb33215968
rdf:type
n3:Context
rdf:value
The primary mechanism of Snail1-induced EMT is the repression of E-cadherin, which causes reduced cell adhesion and promotes migratory capacity [>>12<<]. The further elucidation of Snail1’s role in EMT provides a critical insight into the development of metastatic cancer. In addition, Snail1 has been recently implicated in the regulation of drug/immune resistance and the cancer stem cell
n3:mentions
n4:15983400
Subject Item
_:vb33215969
rdf:type
n3:Context
rdf:value
In addition, Snail1 has been recently implicated in the regulation of drug/immune resistance and the cancer stem cell (CSC) phenotype [>>13<<]–[16].
n3:mentions
n4:15314165
Subject Item
_:vb33215970
rdf:type
n3:Context
rdf:value
In addition, Snail1 has been recently implicated in the regulation of drug/immune resistance and the cancer stem cell (CSC) phenotype [13]–[>>16<<].
n3:mentions
n4:24333218
Subject Item
_:vb33215971
rdf:type
n2:Section
dc:title
conclusions and future directions
n2:contains
_:vb33215972
Subject Item
_:vb33215972
rdf:type
n3:Context
rdf:value
To that end, the development of chemical inhibitors for both Snail1 and targets further upstream has begun [>>183<<]–[187]. PI3K, MEK, and mTOR inhibitors are making great strides, and combinations of these prove even more effective.
n3:mentions
n4:18039463
Subject Item
_:vb33215973
rdf:type
n2:Section
dc:title
regulation of snail1 expression
n2:contains
_:vb33215984 _:vb33215985 _:vb33215986 _:vb33215987 _:vb33215988 _:vb33215989 _:vb33215990 _:vb33215991 _:vb33215992 _:vb33215993 _:vb33215994 _:vb33215995 _:vb33215996 _:vb33215997 _:vb33215998 _:vb33215999 _:vb33215974 _:vb33215975 _:vb33215976 _:vb33215977 _:vb33215978 _:vb33215979 _:vb33215980 _:vb33215981 _:vb33215982 _:vb33215983 _:vb33216032 _:vb33216033 _:vb33216016 _:vb33216017 _:vb33216018 _:vb33216019 _:vb33216020 _:vb33216021 _:vb33216022 _:vb33216023 _:vb33216024 _:vb33216025 _:vb33216026 _:vb33216027 _:vb33216028 _:vb33216029 _:vb33216030 _:vb33216031 _:vb33216000 _:vb33216001 _:vb33216002 _:vb33216003 _:vb33216004 _:vb33216005 _:vb33216006 _:vb33216007 _:vb33216008 _:vb33216009 _:vb33216010 _:vb33216011 _:vb33216012 _:vb33216013 _:vb33216014 _:vb33216015
Subject Item
_:vb33215974
rdf:type
n3:Context
rdf:value
The Notch intracellular domain, LOXL2, NF-κB, HIF-1α, IKKα, SMAD, HMGA2, Egr-1, PARP-1, STAT3, MTA3, and Gli1 all interact directly with the Snail1 promoter to regulate Snail1 at the transcriptional level [>>17<<]–[29]. Hypoxic stress, caused by insufficient oxygen, prompts a transcriptional response mediated by hypoxia-inducible factors (HIFs) [17].
n3:mentions
n4:20965423
Subject Item
_:vb33215975
rdf:type
n3:Context
rdf:value
The Notch intracellular domain, LOXL2, NF-κB, HIF-1α, IKKα, SMAD, HMGA2, Egr-1, PARP-1, STAT3, MTA3, and Gli1 all interact directly with the Snail1 promoter to regulate Snail1 at the transcriptional level [17]–[>>29<<]. Hypoxic stress, caused by insufficient oxygen, prompts a transcriptional response mediated by hypoxia-inducible factors (HIFs) [17].
n3:mentions
n4:16858414
Subject Item
_:vb33215976
rdf:type
n3:Context
rdf:value
Hypoxic stress, caused by insufficient oxygen, prompts a transcriptional response mediated by hypoxia-inducible factors (HIFs) [>>17<<]. Notch increases HIF-1α recruitment to the LOX promoter, and LOXL2 oxidizes K98 and/or K127 on the Snail1 promoter, leading to a conformational change in shape [18]. Under hypoxic conditions, HIF-1α binds to HRE2, contained within -750
n3:mentions
n4:20965423
Subject Item
_:vb33215977
rdf:type
n3:Context
rdf:value
Notch increases HIF-1α recruitment to the LOX promoter, and LOXL2 oxidizes K98 and/or K127 on the Snail1 promoter, leading to a conformational change in shape [>>18<<]. Under hypoxic conditions, HIF-1α binds to HRE2, contained within -750 to -643 bp of the Snail1 promoter, and increases Snail1 transcription. Knockdown of HIF-1α results in the repression of both Snail1 and EMT [19]. NF-κB also binds to
n3:mentions
n4:16096638
Subject Item
_:vb33215978
rdf:type
n3:Context
rdf:value
Knockdown of HIF-1α results in the repression of both Snail1 and EMT [>>19<<]. NF-κB also binds to the Snail1 promoter, between -194 and -78 bp, and increases its transcription [20].
n3:mentions
n4:23979441
Subject Item
_:vb33215979
rdf:type
n3:Context
rdf:value
NF-κB also binds to the Snail1 promoter, between -194 and -78 bp, and increases its transcription [>>20<<]. SMAD2 and IKKα bind concurrently to the Snail1 promoter between -631 and -506 bp, resulting in Snail1’s upregulation [21]. HMGA2 cooperates in this complex as well, as the binding of HMGA2 to the Snail1 promoter increases SMAD binding
n3:mentions
n4:15286702
Subject Item
_:vb33215980
rdf:type
n3:Context
rdf:value
SMAD2 and IKKα bind concurrently to the Snail1 promoter between -631 and -506 bp, resulting in Snail1’s upregulation [>>21<<]. HMGA2 cooperates in this complex as well, as the binding of HMGA2 to the Snail1 promoter increases SMAD binding [22].
n3:mentions
n4:21081648
Subject Item
_:vb33215981
rdf:type
n3:Context
rdf:value
HMGA2 cooperates in this complex as well, as the binding of HMGA2 to the Snail1 promoter increases SMAD binding [>>22<<].
n3:mentions
n4:18832382
Subject Item
_:vb33215982
rdf:type
n3:Context
rdf:value
In addition, ILK promotes PARP-1 binding, and STAT3 binds as a final result of an IL-6/JAK/STAT pathway [>>23<<],[24]. In mice, a pathway beginning with HB-EGF and progressing through the MEK/ERK pathway has also induced STAT3 binding to the Snail1 promoter [25].
n3:mentions
n4:18773488
Subject Item
_:vb33215983
rdf:type
n3:Context
rdf:value
In addition, ILK promotes PARP-1 binding, and STAT3 binds as a final result of an IL-6/JAK/STAT pathway [23],[>>24<<]. In mice, a pathway beginning with HB-EGF and progressing through the MEK/ERK pathway has also induced STAT3 binding to the Snail1 promoter [25].
n3:mentions
n4:21976712
Subject Item
_:vb33215984
rdf:type
n3:Context
rdf:value
In mice, a pathway beginning with HB-EGF and progressing through the MEK/ERK pathway has also induced STAT3 binding to the Snail1 promoter [>>25<<]. Gli1 and Snail1 interact through a positive feedback loop: Shh and Wnt crosstalk results in the upregulation of both [26]. MTA3, a subunit of the Mi-2/NuRD complex, transcriptionally represses Snail1 in an ER-dependent manner. Snail1,
n3:mentions
n4:23994020
Subject Item
_:vb33215985
rdf:type
n3:Context
rdf:value
Gli1 and Snail1 interact through a positive feedback loop: Shh and Wnt crosstalk results in the upregulation of both [>>26<<]. MTA3, a subunit of the Mi-2/NuRD complex, transcriptionally represses Snail1 in an ER-dependent manner. Snail1, in turn, binds to the ER promoter to complete the negative feedback loop [27],[28]. In a similar fashion, Egr-1 and Snail1
n3:mentions
n4:17297467
Subject Item
_:vb33215986
rdf:type
n3:Context
rdf:value
Snail1, in turn, binds to the ER promoter to complete the negative feedback loop [>>27<<],[28]. In a similar fashion, Egr-1 and Snail1 relate via a negative feedback loop. Egr-1, another zinc-finger transcription factor, binds to the Snail1 promoter at four sites between -450 and -50 bp. This process necessitates the presence
n3:mentions
n4:12705869
Subject Item
_:vb33215987
rdf:type
n3:Context
rdf:value
Snail1, in turn, binds to the ER promoter to complete the negative feedback loop [27],[>>28<<]. In a similar fashion, Egr-1 and Snail1 relate via a negative feedback loop. Egr-1, another zinc-finger transcription factor, binds to the Snail1 promoter at four sites between -450 and -50 bp. This process necessitates the presence of
n3:mentions
n4:17761946
Subject Item
_:vb33215988
rdf:type
n3:Context
rdf:value
This process necessitates the presence of HGF and is mediated by the MAPK pathway, and it ultimately results in Snail1 upregulation. Snail1, in turn, represses Egr-1 [>>29<<].
n3:mentions
n4:16858414
Subject Item
_:vb33215989
rdf:type
n3:Context
rdf:value
YY1 binds to the 3’ enhancer, rather than the promoter, and knockdown of YY1 has been shown to decrease Snail1 expression [>>30<<]. Furthermore, Snail1 is capable of binding to its own promoter and upregulating itself [31]. Snail1 binds to the E box region within the Snail ILK Responsive Element (SIRE); PARP-1 also binds to the SIRE, which is located between -134
n3:mentions
n4:19208738
Subject Item
_:vb33215990
rdf:type
n3:Context
rdf:value
Furthermore, Snail1 is capable of binding to its own promoter and upregulating itself [>>31<<]. Snail1 binds to the E box region within the Snail ILK Responsive Element (SIRE); PARP-1 also binds to the SIRE, which is located between -134 and -69 bp, when induced by ILK [23] (Figure 2).
n3:mentions
n4:16617148
Subject Item
_:vb33215991
rdf:type
n3:Context
rdf:value
Snail1 binds to the E box region within the Snail ILK Responsive Element (SIRE); PARP-1 also binds to the SIRE, which is located between -134 and -69 bp, when induced by ILK [>>23<<] (Figure 2).
n3:mentions
n4:18773488
Subject Item
_:vb33215992
rdf:type
n3:Context
rdf:value
Consequently, when p53 is repressed, the repression of Snail1 is lifted, and the expression of Snail1 rises [>>32<<].
n3:mentions
n4:22024162
Subject Item
_:vb33215993
rdf:type
n3:Context
rdf:value
Consequential proteasomal degradation follows [>>33<<],[34]. In conditions that prevent GSK-3β from phosphorylating Snail1, the F-box E3 ubiquitin ligase FBXL14 appears to cause proteasomal degradation by ubiquitinating the same lysine residues as β-Trcp [35].
n3:mentions
n4:15448698
Subject Item
_:vb33215994
rdf:type
n3:Context
rdf:value
Consequential proteasomal degradation follows [33],[>>34<<]. In conditions that prevent GSK-3β from phosphorylating Snail1, the F-box E3 ubiquitin ligase FBXL14 appears to cause proteasomal degradation by ubiquitinating the same lysine residues as β-Trcp [35].
n3:mentions
n4:16940750
Subject Item
_:vb33215995
rdf:type
n3:Context
rdf:value
In conditions that prevent GSK-3β from phosphorylating Snail1, the F-box E3 ubiquitin ligase FBXL14 appears to cause proteasomal degradation by ubiquitinating the same lysine residues as β-Trcp [>>35<<]. P21-activated kinase 1 (PAK1) also phosphorylates Snail1 at S246[36]. Phosphorylation determines Snail1’s subcellular location, as GSK-3β -mediated phosphorylation induces Snail1’s export to the cytoplasm through exportins such as
n3:mentions
n4:19955572
Subject Item
_:vb33215996
rdf:type
n3:Context
rdf:value
P21-activated kinase 1 (PAK1) also phosphorylates Snail1 at S246[>>36<<]. Phosphorylation determines Snail1’s subcellular location, as GSK-3β -mediated phosphorylation induces Snail1’s export to the cytoplasm through exportins such as chromosome region maintenance 1 (CRM1) [33],[37].
n3:mentions
n4:15833848
Subject Item
_:vb33215997
rdf:type
n3:Context
rdf:value
Phosphorylation determines Snail1’s subcellular location, as GSK-3β -mediated phosphorylation induces Snail1’s export to the cytoplasm through exportins such as chromosome region maintenance 1 (CRM1) [>>33<<],[37]. By contrast, PAK1 phosphorylation promotes Snail1’s presence in the nucleus and, therefore, increases its activity [36]. In the cytoplasm, Snail1 is quickly degraded; it has a half-life of only twenty-five minutes [33]. To protect
n3:mentions
n4:15448698
Subject Item
_:vb33215998
rdf:type
n3:Context
rdf:value
Phosphorylation determines Snail1’s subcellular location, as GSK-3β -mediated phosphorylation induces Snail1’s export to the cytoplasm through exportins such as chromosome region maintenance 1 (CRM1) [33],[>>37<<]. By contrast, PAK1 phosphorylation promotes Snail1’s presence in the nucleus and, therefore, increases its activity [36]. In the cytoplasm, Snail1 is quickly degraded; it has a half-life of only twenty-five minutes [33]. To protect from
n3:mentions
n4:12832491
Subject Item
_:vb33215999
rdf:type
n3:Context
rdf:value
By contrast, PAK1 phosphorylation promotes Snail1’s presence in the nucleus and, therefore, increases its activity [>>36<<]. In the cytoplasm, Snail1 is quickly degraded; it has a half-life of only twenty-five minutes [33]. To protect from this degradation, Snail1 has nuclear localization signals (NLS): one monopartite from amino acids 151-152 and one
n3:mentions
n4:15833848
Subject Item
_:vb33216000
rdf:type
n3:Context
rdf:value
In the cytoplasm, Snail1 is quickly degraded; it has a half-life of only twenty-five minutes [>>33<<]. To protect from this degradation, Snail1 has nuclear localization signals (NLS): one monopartite from amino acids 151-152 and one bipartite overlapping the SNAG domain between amino acids 8 and 16 [38]. These signals are responsible for
n3:mentions
n4:15448698
Subject Item
_:vb33216001
rdf:type
n3:Context
rdf:value
To protect from this degradation, Snail1 has nuclear localization signals (NLS): one monopartite from amino acids 151-152 and one bipartite overlapping the SNAG domain between amino acids 8 and 16 [>>38<<]. These signals are responsible for the nuclear transport of Snail1, which in turn is required for proper expression. β-catenin, Lef-1, and IκB employ similar systems [38] (Figure 3, Table 1).
n3:mentions
n4:17587810
Subject Item
_:vb33216002
rdf:type
n3:Context
rdf:value
These signals are responsible for the nuclear transport of Snail1, which in turn is required for proper expression. β-catenin, Lef-1, and IκB employ similar systems [>>38<<] (Figure 3, Table 1).
n3:mentions
n4:17587810
Subject Item
_:vb33216003
rdf:type
n3:Context
rdf:value
Direct regulatorsInteraction locationUpstream pathway(s)Reference(s)LOXL2/3SNAG domain; K98 and K127Notch/Lox[>>17<<]NF-κBPromoter: -194 to -78 bpTNFα, RANKL, PI3K/Akt[20],[43],[44]HIF-1αPromoter: -750 to -643 bpHypoxic conditions[19]SMADsPromoter:
n3:mentions
n4:20965423
Subject Item
_:vb33216004
rdf:type
n3:Context
rdf:value
Direct regulatorsInteraction locationUpstream pathway(s)Reference(s)LOXL2/3SNAG domain; K98 and K127Notch/Lox[17]NF-κBPromoter: -194 to -78 bpTNFα, RANKL, PI3K/Akt[>>20<<],[43],[44]HIF-1αPromoter: -750 to -643 bpHypoxic conditions[19]SMADsPromoter: -631 to -506 bpTGF-β1, Ras[45],[46]IKKαPromoter:
n3:mentions
n4:15286702
Subject Item
_:vb33216005
rdf:type
n3:Context
rdf:value
Direct regulatorsInteraction locationUpstream pathway(s)Reference(s)LOXL2/3SNAG domain; K98 and K127Notch/Lox[17]NF-κBPromoter: -194 to -78 bpTNFα, RANKL, PI3K/Akt[20],[>>43<<],[44]HIF-1αPromoter: -750 to -643 bpHypoxic conditions[19]SMADsPromoter: -631 to -506 bpTGF-β1, Ras[45],[46]IKKαPromoter:
n3:mentions
n4:24011086
Subject Item
_:vb33216006
rdf:type
n3:Context
rdf:value
Direct regulatorsInteraction locationUpstream pathway(s)Reference(s)LOXL2/3SNAG domain; K98 and K127Notch/Lox[17]NF-κBPromoter: -194 to -78 bpTNFα, RANKL, PI3K/Akt[20],[43],[>>44<<]HIF-1αPromoter: -750 to -643 bpHypoxic conditions[19]SMADsPromoter: -631 to -506 bpTGF-β1, Ras[45],[46]IKKαPromoter:
n3:mentions
n4:17563753
Subject Item
_:vb33216007
rdf:type
n3:Context
rdf:value
Direct regulatorsInteraction locationUpstream pathway(s)Reference(s)LOXL2/3SNAG domain; K98 and K127Notch/Lox[17]NF-κBPromoter: -194 to -78 bpTNFα, RANKL, PI3K/Akt[20],[43],[44]HIF-1αPromoter: -750 to -643 bpHypoxic conditions[>>19<<]SMADsPromoter: -631 to -506 bpTGF-β1, Ras[45],[46]IKKαPromoter: -631 to -506 bp (concurrent with SMADs)TGF-β1, Ras, PI3K/Akt[21],[44],[46]HMGA2Promoter:
n3:mentions
n4:23979441
Subject Item
_:vb33216008
rdf:type
n3:Context
rdf:value
pathway(s)Reference(s)LOXL2/3SNAG domain; K98 and K127Notch/Lox[17]NF-κBPromoter: -194 to -78 bpTNFα, RANKL, PI3K/Akt[20],[43],[44]HIF-1αPromoter: -750 to -643 bpHypoxic conditions[19]SMADsPromoter: -631 to -506 bpTGF-β1, Ras[>>45<<],[46]IKKαPromoter: -631 to -506 bp (concurrent with SMADs)TGF-β1, Ras, PI3K/Akt[21],[44],[46]HMGA2Promoter:
n3:mentions
n4:24106276
Subject Item
_:vb33216009
rdf:type
n3:Context
rdf:value
pathway(s)Reference(s)LOXL2/3SNAG domain; K98 and K127Notch/Lox[17]NF-κBPromoter: -194 to -78 bpTNFα, RANKL, PI3K/Akt[20],[43],[44]HIF-1αPromoter: -750 to -643 bpHypoxic conditions[19]SMADsPromoter: -631 to -506 bpTGF-β1, Ras[45],[>>46<<]IKKαPromoter: -631 to -506 bp (concurrent with SMADs)TGF-β1, Ras, PI3K/Akt[21],[44],[46]HMGA2Promoter:
n3:mentions
n4:19010789
Subject Item
_:vb33216010
rdf:type
n3:Context
rdf:value
-194 to -78 bpTNFα, RANKL, PI3K/Akt[20],[43],[44]HIF-1αPromoter: -750 to -643 bpHypoxic conditions[19]SMADsPromoter: -631 to -506 bpTGF-β1, Ras[45],[46]IKKαPromoter: -631 to -506 bp (concurrent with SMADs)TGF-β1, Ras, PI3K/Akt[>>21<<],[44],[46]HMGA2Promoter: 2 regions within -131 to -92 bpTGF-β1[22]YY13’ EnhancerNF-κB[30]Egr-1Promoter:
n3:mentions
n4:21081648
Subject Item
_:vb33216011
rdf:type
n3:Context
rdf:value
-194 to -78 bpTNFα, RANKL, PI3K/Akt[20],[43],[44]HIF-1αPromoter: -750 to -643 bpHypoxic conditions[19]SMADsPromoter: -631 to -506 bpTGF-β1, Ras[45],[46]IKKαPromoter: -631 to -506 bp (concurrent with SMADs)TGF-β1, Ras, PI3K/Akt[21],[>>44<<],[46]HMGA2Promoter: 2 regions within -131 to -92 bpTGF-β1[22]YY13’ EnhancerNF-κB[30]Egr-1Promoter:
n3:mentions
n4:17563753
Subject Item
_:vb33216012
rdf:type
n3:Context
rdf:value
-194 to -78 bpTNFα, RANKL, PI3K/Akt[20],[43],[44]HIF-1αPromoter: -750 to -643 bpHypoxic conditions[19]SMADsPromoter: -631 to -506 bpTGF-β1, Ras[45],[46]IKKαPromoter: -631 to -506 bp (concurrent with SMADs)TGF-β1, Ras, PI3K/Akt[21],[44],[>>46<<]HMGA2Promoter: 2 regions within -131 to -92 bpTGF-β1[22]YY13’ EnhancerNF-κB[30]Egr-1Promoter:
n3:mentions
n4:19010789
Subject Item
_:vb33216013
rdf:type
n3:Context
rdf:value
-750 to -643 bpHypoxic conditions[19]SMADsPromoter: -631 to -506 bpTGF-β1, Ras[45],[46]IKKαPromoter: -631 to -506 bp (concurrent with SMADs)TGF-β1, Ras, PI3K/Akt[21],[44],[46]HMGA2Promoter: 2 regions within -131 to -92 bpTGF-β1[>>22<<]YY13’ EnhancerNF-κB[30]Egr-1Promoter: 4 sites between -450 and -50 bpHGF, MAPK[29]PARP-1Promoter:
n3:mentions
n4:18832382
Subject Item
_:vb33216014
rdf:type
n3:Context
rdf:value
conditions[19]SMADsPromoter: -631 to -506 bpTGF-β1, Ras[45],[46]IKKαPromoter: -631 to -506 bp (concurrent with SMADs)TGF-β1, Ras, PI3K/Akt[21],[44],[46]HMGA2Promoter: 2 regions within -131 to -92 bpTGF-β1[22]YY13’ EnhancerNF-κB[>>30<<]Egr-1Promoter: 4 sites between -450 and -50 bpHGF, MAPK[29]PARP-1Promoter: SIREILK[23]Gli1There are 4 candidate GLI binding sites (consensus sequence for binding:
n3:mentions
n4:19208738
Subject Item
_:vb33216015
rdf:type
n3:Context
rdf:value
Ras[45],[46]IKKαPromoter: -631 to -506 bp (concurrent with SMADs)TGF-β1, Ras, PI3K/Akt[21],[44],[46]HMGA2Promoter: 2 regions within -131 to -92 bpTGF-β1[22]YY13’ EnhancerNF-κB[30]Egr-1Promoter: 4 sites between -450 and -50 bpHGF, MAPK[>>29<<]PARP-1Promoter: SIREILK[23]Gli1There are 4 candidate GLI binding sites (consensus sequence for binding:
n3:mentions
n4:16858414
Subject Item
_:vb33216016
rdf:type
n3:Context
rdf:value
-631 to -506 bp (concurrent with SMADs)TGF-β1, Ras, PI3K/Akt[21],[44],[46]HMGA2Promoter: 2 regions within -131 to -92 bpTGF-β1[22]YY13’ EnhancerNF-κB[30]Egr-1Promoter: 4 sites between -450 and -50 bpHGF, MAPK[29]PARP-1Promoter: SIREILK[>>23<<]Gli1There are 4 candidate GLI binding sites (consensus sequence for binding:
n3:mentions
n4:18773488
Subject Item
_:vb33216017
rdf:type
n3:Context
rdf:value
-131 to -92 bpTGF-β1[22]YY13’ EnhancerNF-κB[30]Egr-1Promoter: 4 sites between -450 and -50 bpHGF, MAPK[29]PARP-1Promoter: SIREILK[23]Gli1There are 4 candidate GLI binding sites (consensus sequence for binding: 5'-GACCACCCA-3')Shh, Wnt[>>26<<]STAT3PromoterIL-6/JAK, HB-EGF/EGFR/MEK/ERK (mice)[24],[25]MTA3PromoterER[27],[28]PAK1S246 [36]GSK-3βMotif 1 (S96, S100, S104) and Motif 2 (S107, S111, S115, S119)Wnt, PI3K/Akt, FGF[33],[34]Snail1Promoter:
n3:mentions
n4:17297467
Subject Item
_:vb33216018
rdf:type
n3:Context
rdf:value
4 sites between -450 and -50 bpHGF, MAPK[29]PARP-1Promoter: SIREILK[23]Gli1There are 4 candidate GLI binding sites (consensus sequence for binding: 5'-GACCACCCA-3')Shh, Wnt[26]STAT3PromoterIL-6/JAK, HB-EGF/EGFR/MEK/ERK (mice)[>>24<<],[25]MTA3PromoterER[27],[28]PAK1S246 [36]GSK-3βMotif 1 (S96, S100, S104) and Motif 2 (S107, S111, S115, S119)Wnt, PI3K/Akt, FGF[33],[34]Snail1Promoter:
n3:mentions
n4:21976712
Subject Item
_:vb33216019
rdf:type
n3:Context
rdf:value
4 sites between -450 and -50 bpHGF, MAPK[29]PARP-1Promoter: SIREILK[23]Gli1There are 4 candidate GLI binding sites (consensus sequence for binding: 5'-GACCACCCA-3')Shh, Wnt[26]STAT3PromoterIL-6/JAK, HB-EGF/EGFR/MEK/ERK (mice)[24],[>>25<<]MTA3PromoterER[27],[28]PAK1S246 [36]GSK-3βMotif 1 (S96, S100, S104) and Motif 2 (S107, S111, S115, S119)Wnt, PI3K/Akt, FGF[33],[34]Snail1Promoter:
n3:mentions
n4:23994020
Subject Item
_:vb33216020
rdf:type
n3:Context
rdf:value
-450 and -50 bpHGF, MAPK[29]PARP-1Promoter: SIREILK[23]Gli1There are 4 candidate GLI binding sites (consensus sequence for binding: 5'-GACCACCCA-3')Shh, Wnt[26]STAT3PromoterIL-6/JAK, HB-EGF/EGFR/MEK/ERK (mice)[24],[25]MTA3PromoterER[>>27<<],[28]PAK1S246 [36]GSK-3βMotif 1 (S96, S100, S104) and Motif 2 (S107, S111, S115, S119)Wnt, PI3K/Akt, FGF[33],[34]Snail1Promoter:
n3:mentions
n4:12705869
Subject Item
_:vb33216021
rdf:type
n3:Context
rdf:value
and -50 bpHGF, MAPK[29]PARP-1Promoter: SIREILK[23]Gli1There are 4 candidate GLI binding sites (consensus sequence for binding: 5'-GACCACCCA-3')Shh, Wnt[26]STAT3PromoterIL-6/JAK, HB-EGF/EGFR/MEK/ERK (mice)[24],[25]MTA3PromoterER[27],[>>28<<]PAK1S246 [36]GSK-3βMotif 1 (S96, S100, S104) and Motif 2 (S107, S111, S115, S119)Wnt, PI3K/Akt, FGF[33],[34]Snail1Promoter:
n3:mentions
n4:17761946
Subject Item
_:vb33216022
rdf:type
n3:Context
rdf:value
MAPK[29]PARP-1Promoter: SIREILK[23]Gli1There are 4 candidate GLI binding sites (consensus sequence for binding: 5'-GACCACCCA-3')Shh, Wnt[26]STAT3PromoterIL-6/JAK, HB-EGF/EGFR/MEK/ERK (mice)[24],[25]MTA3PromoterER[27],[28]PAK1S246 [>>36<<]GSK-3βMotif 1 (S96, S100, S104) and Motif 2 (S107, S111, S115, S119)Wnt, PI3K/Akt, FGF[33],[34]Snail1Promoter:
n3:mentions
n4:15833848
Subject Item
_:vb33216023
rdf:type
n3:Context
rdf:value
sequence for binding: 5'-GACCACCCA-3')Shh, Wnt[26]STAT3PromoterIL-6/JAK, HB-EGF/EGFR/MEK/ERK (mice)[24],[25]MTA3PromoterER[27],[28]PAK1S246 [36]GSK-3βMotif 1 (S96, S100, S104) and Motif 2 (S107, S111, S115, S119)Wnt, PI3K/Akt, FGF[>>33<<],[34]Snail1Promoter:
n3:mentions
n4:15448698
Subject Item
_:vb33216024
rdf:type
n3:Context
rdf:value
sequence for binding: 5'-GACCACCCA-3')Shh, Wnt[26]STAT3PromoterIL-6/JAK, HB-EGF/EGFR/MEK/ERK (mice)[24],[25]MTA3PromoterER[27],[28]PAK1S246 [36]GSK-3βMotif 1 (S96, S100, S104) and Motif 2 (S107, S111, S115, S119)Wnt, PI3K/Akt, FGF[33],[>>34<<]Snail1Promoter:
n3:mentions
n4:16940750
Subject Item
_:vb33216025
rdf:type
n3:Context
rdf:value
HB-EGF/EGFR/MEK/ERK (mice)[24],[25]MTA3PromoterER[27],[28]PAK1S246 [36]GSK-3βMotif 1 (S96, S100, S104) and Motif 2 (S107, S111, S115, S119)Wnt, PI3K/Akt, FGF[33],[34]Snail1Promoter: E box within SIREBinds to own promoter[>>31<<
n3:mentions
n4:16617148
Subject Item
_:vb33216026
rdf:type
n3:Context
rdf:value
Thus, Snail1 is neither phosphorylated nor ubiquitylated [>>39<<]. FGF operates through the PI3K/Akt pathway to downregulate GSK-3β, and receptor tyrosine kinase induces EGF suppression of GSK-3β [34],[40].
n3:mentions
n4:19411070
Subject Item
_:vb33216027
rdf:type
n3:Context
rdf:value
FGF operates through the PI3K/Akt pathway to downregulate GSK-3β, and receptor tyrosine kinase induces EGF suppression of GSK-3β [>>34<<],[40]. Wnt can also suppress GSK-3β and, thus, the phosphorylation of Snail1 [41]. Additionally, miR-148a causes the phosphorylation of AKT and GSK-3β, which results in less Snail1 localized in the nucleus. This, in turn, inhibited EMT in
n3:mentions
n4:16940750
Subject Item
_:vb33216028
rdf:type
n3:Context
rdf:value
Wnt can also suppress GSK-3β and, thus, the phosphorylation of Snail1 [>>41<<]. Additionally, miR-148a causes the phosphorylation of AKT and GSK-3β, which results in less Snail1 localized in the nucleus.
n3:mentions
n4:15647282
Subject Item
_:vb33216029
rdf:type
n3:Context
rdf:value
For example, RANKL, in association with IκB, activates the NF-κB p65 subunit, and Akt influences the nuclear localization of NF-κB through its phosphorylation of IKKα and IκB in turn [>>43<<],[44]. TGF-β1 induces the phosphorylation of SMAD2 and SMAD3, which is necessary for their binding to Snail1 and the consequential upregulation of Snail1’s activities [45]. However, the cooperation of Ras signals is required for this
n3:mentions
n4:24011086
Subject Item
_:vb33216030
rdf:type
n3:Context
rdf:value
For example, RANKL, in association with IκB, activates the NF-κB p65 subunit, and Akt influences the nuclear localization of NF-κB through its phosphorylation of IKKα and IκB in turn [43],[>>44<<]. TGF-β1 induces the phosphorylation of SMAD2 and SMAD3, which is necessary for their binding to Snail1 and the consequential upregulation of Snail1’s activities [45]. However, the cooperation of Ras signals is required for this pathway,
n3:mentions
n4:17563753
Subject Item
_:vb33216031
rdf:type
n3:Context
rdf:value
TGF-β1 induces the phosphorylation of SMAD2 and SMAD3, which is necessary for their binding to Snail1 and the consequential upregulation of Snail1’s activities [>>45<<]. However, the cooperation of Ras signals is required for this pathway, since TGF- β1-mediated induction of Snail1 ceases with the silencing of Ras [46].
n3:mentions
n4:24106276
Subject Item
_:vb33216032
rdf:type
n3:Context
rdf:value
However, the cooperation of Ras signals is required for this pathway, since TGF- β1-mediated induction of Snail1 ceases with the silencing of Ras [>>46<<].
n3:mentions
n4:19010789
Subject Item
_:vb33216033
rdf:type
n3:Context
rdf:value
The small C-terminal domain phosphatase (SCP) induces dephosphorylation of both GSK-3β and the affected Snail1 motifs, thereby stabilizing Snail1 [>>47<<]. Additionally, histone deacetylase inhibitors promote the acetylation, likely of lysines, and increase Snail1’s nuclear localization by inhibiting ubiquitination [48].
n3:mentions
n4:19004823
Subject Item
_:vb33216034
rdf:type
n2:Section
dc:title
snail1’s targets
n2:contains
_:vb33216077 _:vb33216078 _:vb33216079 _:vb33216072 _:vb33216073 _:vb33216074 _:vb33216075 _:vb33216068 _:vb33216069 _:vb33216070 _:vb33216071 _:vb33216064 _:vb33216065 _:vb33216066 _:vb33216067 _:vb33216092 _:vb33216093 _:vb33216094 _:vb33216095 _:vb33216088 _:vb33216089 _:vb33216090 _:vb33216091 _:vb33216084 _:vb33216085 _:vb33216086 _:vb33216087 _:vb33216080 _:vb33216081 _:vb33216082 _:vb33216083 _:vb33216044 _:vb33216045 _:vb33216046 _:vb33216047 _:vb33216040 _:vb33216041 _:vb33216042 _:vb33216043 _:vb33216036 _:vb33216037 _:vb33216038 _:vb33216039 _:vb33216035 _:vb33216060 _:vb33216061 _:vb33216062 _:vb33216063 _:vb33216056 _:vb33216057 _:vb33216058 _:vb33216059 _:vb33216052 _:vb33216053 _:vb33216054 _:vb33216055 _:vb33216048 _:vb33216049 _:vb33216050 _:vb33216051 _:vb33216140 _:vb33216141 _:vb33216142 _:vb33216143 _:vb33216136 _:vb33216137 _:vb33216138 _:vb33216139 _:vb33216132 _:vb33216133 _:vb33216134 _:vb33216135 _:vb33216128 _:vb33216129 _:vb33216130 _:vb33216131 _:vb33216144 _:vb33216145 _:vb33216146 _:vb33216147 _:vb33216108 _:vb33216109 _:vb33216110 _:vb33216111 _:vb33216104 _:vb33216105 _:vb33216106 _:vb33216107 _:vb33216100 _:vb33216101 _:vb33216102 _:vb33216103 _:vb33216096 _:vb33216097 _:vb33216098 _:vb33216099 _:vb33216124 _:vb33216125 _:vb33216126 _:vb33216127 _:vb33216120 _:vb33216121 _:vb33216122 _:vb33216123 _:vb33216116 _:vb33216117 _:vb33216118 _:vb33216119 _:vb33216112 _:vb33216113 _:vb33216114 _:vb33216115 _:vb33216076
Subject Item
_:vb33216035
rdf:type
n3:Context
rdf:value
TargetTarget significanceSnail’s effectReference(s)E-cadherinEpithelial marker, adherens junctionsRepression[>>56<<],[57],[59]–[61]RKIPTumor suppressorRepression[68]PTENTumor suppressorRepression[70]OccludinEpithelial marker, tight junctionsRepression[13],[75]ClaudinsEpithelial markers, tight junctionsRepression[75]Mucin-1Epithelial
n3:mentions
n4:22406531
Subject Item
_:vb33216036
rdf:type
n3:Context
rdf:value
TargetTarget significanceSnail’s effectReference(s)E-cadherinEpithelial marker, adherens junctionsRepression[56],[>>57<<],[59]–[61]RKIPTumor suppressorRepression[68]PTENTumor suppressorRepression[70]OccludinEpithelial marker, tight junctionsRepression[13],[75]ClaudinsEpithelial markers, tight junctionsRepression[75]Mucin-1Epithelial
n3:mentions
n4:18347060
Subject Item
_:vb33216037
rdf:type
n3:Context
rdf:value
TargetTarget significanceSnail’s effectReference(s)E-cadherinEpithelial marker, adherens junctionsRepression[56],[57],[>>59<<]–[61]RKIPTumor suppressorRepression[68]PTENTumor suppressorRepression[70]OccludinEpithelial marker, tight junctionsRepression[13],[75]ClaudinsEpithelial markers, tight junctionsRepression[75]Mucin-1Epithelial
n3:mentions
n4:14673164
Subject Item
_:vb33216038
rdf:type
n3:Context
rdf:value
TargetTarget significanceSnail’s effectReference(s)E-cadherinEpithelial marker, adherens junctionsRepression[56],[57],[59]–[>>61<<]RKIPTumor suppressorRepression[68]PTENTumor suppressorRepression[70]OccludinEpithelial marker, tight junctionsRepression[13],[75]ClaudinsEpithelial markers, tight junctionsRepression[75]Mucin-1Epithelial markerRepression[83]ZEB-1Assists
n3:mentions
n4:22562246
Subject Item
_:vb33216039
rdf:type
n3:Context
rdf:value
TargetTarget significanceSnail’s effectReference(s)E-cadherinEpithelial marker, adherens junctionsRepression[56],[57],[59]–[61]RKIPTumor suppressorRepression[>>68<<]PTENTumor suppressorRepression[70]OccludinEpithelial marker, tight junctionsRepression[13],[75]ClaudinsEpithelial markers, tight junctionsRepression[75]Mucin-1Epithelial markerRepression[83]ZEB-1Assists in induction of
n3:mentions
n4:17952120
Subject Item
_:vb33216040
rdf:type
n3:Context
rdf:value
TargetTarget significanceSnail’s effectReference(s)E-cadherinEpithelial marker, adherens junctionsRepression[56],[57],[59]–[61]RKIPTumor suppressorRepression[68]PTENTumor suppressorRepression[>>70<<]OccludinEpithelial marker, tight junctionsRepression[13],[75]ClaudinsEpithelial markers, tight junctionsRepression[75]Mucin-1Epithelial markerRepression[83]ZEB-1Assists in induction of EMTUpregulation[83]VimentinMesenchymal
n3:mentions
n4:18172008
Subject Item
_:vb33216041
rdf:type
n3:Context
rdf:value
significanceSnail’s effectReference(s)E-cadherinEpithelial marker, adherens junctionsRepression[56],[57],[59]–[61]RKIPTumor suppressorRepression[68]PTENTumor suppressorRepression[70]OccludinEpithelial marker, tight junctionsRepression[>>13<<],[75]ClaudinsEpithelial markers, tight junctionsRepression[75]Mucin-1Epithelial markerRepression[83]ZEB-1Assists in induction of EMTUpregulation[83]VimentinMesenchymal markerUpregulation[54]FibronectinMesenchymal
n3:mentions
n4:15314165
Subject Item
_:vb33216042
rdf:type
n3:Context
rdf:value
effectReference(s)E-cadherinEpithelial marker, adherens junctionsRepression[56],[57],[59]–[61]RKIPTumor suppressorRepression[68]PTENTumor suppressorRepression[70]OccludinEpithelial marker, tight junctionsRepression[13],[>>75<<]ClaudinsEpithelial markers, tight junctionsRepression[75]Mucin-1Epithelial markerRepression[83]ZEB-1Assists in induction of EMTUpregulation[83]VimentinMesenchymal markerUpregulation[54]FibronectinMesenchymal
n3:mentions
n4:12668723
Subject Item
_:vb33216043
rdf:type
n3:Context
rdf:value
adherens junctionsRepression[56],[57],[59]–[61]RKIPTumor suppressorRepression[68]PTENTumor suppressorRepression[70]OccludinEpithelial marker, tight junctionsRepression[13],[75]ClaudinsEpithelial markers, tight junctionsRepression[>>75<<]Mucin-1Epithelial markerRepression[83]ZEB-1Assists in induction of EMTUpregulation[83]VimentinMesenchymal markerUpregulation[54]FibronectinMesenchymal markerUpregulation[54]Cytokeratin 18Epithelial
n3:mentions
n4:12668723
Subject Item
_:vb33216044
rdf:type
n3:Context
rdf:value
suppressorRepression[68]PTENTumor suppressorRepression[70]OccludinEpithelial marker, tight junctionsRepression[13],[75]ClaudinsEpithelial markers, tight junctionsRepression[75]Mucin-1Epithelial markerRepression[>>83<<]ZEB-1Assists in induction of EMTUpregulation[83]VimentinMesenchymal markerUpregulation[54]FibronectinMesenchymal markerUpregulation[54]Cytokeratin 18Epithelial markerRepression[75],[83]MMP-2/MMP-9Mesenchymal
n3:mentions
n4:12161443
Subject Item
_:vb33216045
rdf:type
n3:Context
rdf:value
suppressorRepression[70]OccludinEpithelial marker, tight junctionsRepression[13],[75]ClaudinsEpithelial markers, tight junctionsRepression[75]Mucin-1Epithelial markerRepression[83]ZEB-1Assists in induction of EMTUpregulation[>>83<<]VimentinMesenchymal markerUpregulation[54]FibronectinMesenchymal markerUpregulation[54]Cytokeratin 18Epithelial markerRepression[75],[83]MMP-2/MMP-9Mesenchymal markersUpregulation[113],[118]LEF-1Mesenchymal marker, assists in induction of
n3:mentions
n4:12161443
Subject Item
_:vb33216046
rdf:type
n3:Context
rdf:value
marker, tight junctionsRepression[13],[75]ClaudinsEpithelial markers, tight junctionsRepression[75]Mucin-1Epithelial markerRepression[83]ZEB-1Assists in induction of EMTUpregulation[83]VimentinMesenchymal markerUpregulation[>>54<<]FibronectinMesenchymal markerUpregulation[54]Cytokeratin 18Epithelial markerRepression[75],[83]MMP-2/MMP-9Mesenchymal markersUpregulation[113],[118]LEF-1Mesenchymal marker, assists in induction of
n3:mentions
n4:10655586
Subject Item
_:vb33216047
rdf:type
n3:Context
rdf:value
markers, tight junctionsRepression[75]Mucin-1Epithelial markerRepression[83]ZEB-1Assists in induction of EMTUpregulation[83]VimentinMesenchymal markerUpregulation[54]FibronectinMesenchymal markerUpregulation[>>54<<]Cytokeratin 18Epithelial markerRepression[75],[83]MMP-2/MMP-9Mesenchymal markersUpregulation[113],[118]LEF-1Mesenchymal marker, assists in induction of
n3:mentions
n4:10655586
Subject Item
_:vb33216048
rdf:type
n3:Context
rdf:value
markerRepression[83]ZEB-1Assists in induction of EMTUpregulation[83]VimentinMesenchymal markerUpregulation[54]FibronectinMesenchymal markerUpregulation[54]Cytokeratin 18Epithelial markerRepression[>>75<<],[83]MMP-2/MMP-9Mesenchymal markersUpregulation[113],[118]LEF-1Mesenchymal marker, assists in induction of
n3:mentions
n4:12668723
Subject Item
_:vb33216049
rdf:type
n3:Context
rdf:value
markerRepression[83]ZEB-1Assists in induction of EMTUpregulation[83]VimentinMesenchymal markerUpregulation[54]FibronectinMesenchymal markerUpregulation[54]Cytokeratin 18Epithelial markerRepression[75],[>>83<<]MMP-2/MMP-9Mesenchymal markersUpregulation[113],[118]LEF-1Mesenchymal marker, assists in induction of
n3:mentions
n4:12161443
Subject Item
_:vb33216050
rdf:type
n3:Context
rdf:value
in induction of EMTUpregulation[83]VimentinMesenchymal markerUpregulation[54]FibronectinMesenchymal markerUpregulation[54]Cytokeratin 18Epithelial markerRepression[75],[83]MMP-2/MMP-9Mesenchymal markersUpregulation[>>113<<],[118]LEF-1Mesenchymal marker, assists in induction of
n3:mentions
n4:20664935
Subject Item
_:vb33216051
rdf:type
n3:Context
rdf:value
markerUpregulation[54]FibronectinMesenchymal markerUpregulation[54]Cytokeratin 18Epithelial markerRepression[75],[83]MMP-2/MMP-9Mesenchymal markersUpregulation[113],[118]LEF-1Mesenchymal marker, assists in induction of EMTUpregulation[>>83<<
n3:mentions
n4:12161443
Subject Item
_:vb33216052
rdf:type
n3:Context
rdf:value
markerUpregulation[54]Cytokeratin 18Epithelial markerRepression[75],[83]MMP-2/MMP-9Mesenchymal markersUpregulation[113],[118]LEF-1Mesenchymal marker, assists in induction of EMTUpregulation[83],[>>125<<
n3:mentions
n4:15683729
Subject Item
_:vb33216053
rdf:type
n3:Context
rdf:value
E-cadherin is a transmembrane glycoprotein responsible for calcium-dependent cell-to-cell adhesion [>>49<<]. E-cadherin is a type I cadherin encoded by the gene CDH1, which is located on human chromosome 16q22.1 [50].
n3:mentions
n4:264120
Subject Item
_:vb33216054
rdf:type
n3:Context
rdf:value
E-cadherin is a type I cadherin encoded by the gene CDH1, which is located on human chromosome 16q22.1 [>>50<<]. The founding member of the cadherin superfamily, E-cadherin plays a pivotal role in cadherin-catenin-cytoskeleton complexes, and it grants anti-invasive and anti-migratory properties to epithelial cells [51]. E-cadherin expression
n3:mentions
n4:7601454
Subject Item
_:vb33216055
rdf:type
n3:Context
rdf:value
The founding member of the cadherin superfamily, E-cadherin plays a pivotal role in cadherin-catenin-cytoskeleton complexes, and it grants anti-invasive and anti-migratory properties to epithelial cells [>>51<<]. E-cadherin expression naturally decreases during gastrulation in order to properly form the mesoderm, and its expression increases once more for kidney organogenesis [52],[53]. The CDH1 promoter contains multiple E-boxes, and Snail1,
n3:mentions
n4:18726070
Subject Item
_:vb33216056
rdf:type
n3:Context
rdf:value
E-cadherin expression naturally decreases during gastrulation in order to properly form the mesoderm, and its expression increases once more for kidney organogenesis [>>52<<],[53]. The CDH1 promoter contains multiple E-boxes, and Snail1, Slug, ZEB1, ZEB2, and Twist, among others, have been shown to directly repress E-cadherin [54]. Total E-cadherin knockout in mice resulted in immediate death at implantation
n3:mentions
n4:9078437
Subject Item
_:vb33216057
rdf:type
n3:Context
rdf:value
E-cadherin expression naturally decreases during gastrulation in order to properly form the mesoderm, and its expression increases once more for kidney organogenesis [52],[>>53<<]. The CDH1 promoter contains multiple E-boxes, and Snail1, Slug, ZEB1, ZEB2, and Twist, among others, have been shown to directly repress E-cadherin [54]. Total E-cadherin knockout in mice resulted in immediate death at implantation [55].
n3:mentions
n4:2419126
Subject Item
_:vb33216058
rdf:type
n3:Context
rdf:value
The CDH1 promoter contains multiple E-boxes, and Snail1, Slug, ZEB1, ZEB2, and Twist, among others, have been shown to directly repress E-cadherin [>>54<<]. Total E-cadherin knockout in mice resulted in immediate death at implantation [55]. Decreases in E-cadherin expression correlate with epithelial-mesenchymal transition, metastasis, and lower patient survival rates [10].
n3:mentions
n4:10655586
Subject Item
_:vb33216059
rdf:type
n3:Context
rdf:value
Total E-cadherin knockout in mice resulted in immediate death at implantation [>>55<<]. Decreases in E-cadherin expression correlate with epithelial-mesenchymal transition, metastasis, and lower patient survival rates [10].
n3:mentions
n4:8058792
Subject Item
_:vb33216060
rdf:type
n3:Context
rdf:value
Decreases in E-cadherin expression correlate with epithelial-mesenchymal transition, metastasis, and lower patient survival rates [>>10<<].
n3:mentions
n4:19487818
Subject Item
_:vb33216061
rdf:type
n3:Context
rdf:value
The complex has been shown to increase H3K9me2 and decrease H3K9 acetylation [>>56<<]. (2) The Snail1-Ajuba-PRMT5 complex promotes the methylation of H4R3. This, too, operates at the E-cadherin promoter [57]. The demethylation of H3K4 by Co-REST, CtBP, and HDAC complexes also factors into the last two mechanisms [58]. (3)
n3:mentions
n4:22406531
Subject Item
_:vb33216062
rdf:type
n3:Context
rdf:value
This, too, operates at the E-cadherin promoter [>>57<<]. The demethylation of H3K4 by Co-REST, CtBP, and HDAC complexes also factors into the last two mechanisms [58].
n3:mentions
n4:18347060
Subject Item
_:vb33216063
rdf:type
n3:Context
rdf:value
The demethylation of H3K4 by Co-REST, CtBP, and HDAC complexes also factors into the last two mechanisms [>>58<<]. (3) Snail1 works in conjunction with Sin3A and HDAC1/2 to deacetylate H3 and H4, which suppress E-cadherin [59]. (4) In perhaps the most elucidated case, the Snail1 SNAG domain interacts with the LSD1 AO domain to form a
n3:mentions
n4:17218267
Subject Item
_:vb33216064
rdf:type
n3:Context
rdf:value
(3) Snail1 works in conjunction with Sin3A and HDAC1/2 to deacetylate H3 and H4, which suppress E-cadherin [>>59<<]. (4) In perhaps the most elucidated case, the Snail1 SNAG domain interacts with the LSD1 AO domain to form a Snail1-LSD1-CoREST complex. Snail1 residues Pro2, Arg3, Ser4, Phe5, Arg8, and Lys9 have been shown to be particularly crucial to
n3:mentions
n4:14673164
Subject Item
_:vb33216065
rdf:type
n3:Context
rdf:value
The formation of the Snail1-LSD1-CoREST complex results in the demethylation of H3K4me2 and consequential suppression of E-cadherin, while also increasing the stability of each of the components of the complex [>>60<<]. In a proposed second step to this mechanism, Snail1 recruits Suv39H1 to the E-cadherin promoter. Similar to prior cases, the Snail1 SNAG domain interacts with the Suv39H1 SET domain to suppress E-cadherin. Knockdown of Suv39H1 restored
n3:mentions
n4:20389281
Subject Item
_:vb33216066
rdf:type
n3:Context
rdf:value
Similar to prior cases, the Snail1 SNAG domain interacts with the Suv39H1 SET domain to suppress E-cadherin. Knockdown of Suv39H1 restored E-cadherin expression by inhibiting H3K9me3 [>>61<<].
n3:mentions
n4:22562246
Subject Item
_:vb33216067
rdf:type
n3:Context
rdf:value
Raf kinase inhibitor protein (RKIP), a member of the phosphatidylethanolamine-binding protein (PEBP) group, suppresses metastasis by inhibiting the Raf-MEK-ERK and NF-κB pathways [>>62<<]–[65]. In prostate, breast, and colorectal cancers, among others, RKIP expression is downregulated [64],[66].
n3:mentions
n4:10490027
Subject Item
_:vb33216068
rdf:type
n3:Context
rdf:value
Raf kinase inhibitor protein (RKIP), a member of the phosphatidylethanolamine-binding protein (PEBP) group, suppresses metastasis by inhibiting the Raf-MEK-ERK and NF-κB pathways [62]–[>>65<<]. In prostate, breast, and colorectal cancers, among others, RKIP expression is downregulated [64],[66].
n3:mentions
n4:15782137
Subject Item
_:vb33216069
rdf:type
n3:Context
rdf:value
In prostate, breast, and colorectal cancers, among others, RKIP expression is downregulated [>>64<<],[66]. Furthermore, elevated RKIP expression is a positive prognostic indicator for survival [66],[67]. Expression levels of RKIP correlate with those of E-cadherin, another Snail1 target, as they are both repressed by means of the
n3:mentions
n4:14766752
Subject Item
_:vb33216070
rdf:type
n3:Context
rdf:value
In prostate, breast, and colorectal cancers, among others, RKIP expression is downregulated [64],[>>66<<]. Furthermore, elevated RKIP expression is a positive prognostic indicator for survival [66],[67]. Expression levels of RKIP correlate with those of E-cadherin, another Snail1 target, as they are both repressed by means of the E-boxes in
n3:mentions
n4:17179102
Subject Item
_:vb33216071
rdf:type
n3:Context
rdf:value
Furthermore, elevated RKIP expression is a positive prognostic indicator for survival [>>66<<],[67]. Expression levels of RKIP correlate with those of E-cadherin, another Snail1 target, as they are both repressed by means of the E-boxes in their promoters [68].
n3:mentions
n4:17179102
Subject Item
_:vb33216072
rdf:type
n3:Context
rdf:value
Furthermore, elevated RKIP expression is a positive prognostic indicator for survival [66],[>>67<<]. Expression levels of RKIP correlate with those of E-cadherin, another Snail1 target, as they are both repressed by means of the E-boxes in their promoters [68].
n3:mentions
n4:16175585
Subject Item
_:vb33216073
rdf:type
n3:Context
rdf:value
Expression levels of RKIP correlate with those of E-cadherin, another Snail1 target, as they are both repressed by means of the E-boxes in their promoters [>>68<<].
n3:mentions
n4:17952120
Subject Item
_:vb33216074
rdf:type
n3:Context
rdf:value
Phosphatase and tensin homolog deleted in chromosome 10 (PTEN) dephosphorylates phosphoinositide-3,4,5-triphosphate (PIP3) and, thus, inhibits the PI3K pathway [>>69<<]. In this way, PTEN functions as a tumor suppressor. Snail1 binds to the PTEN promoter, which contains two E-boxes, and represses PTEN [70].
n3:mentions
n4:16861931
Subject Item
_:vb33216075
rdf:type
n3:Context
rdf:value
Snail1 binds to the PTEN promoter, which contains two E-boxes, and represses PTEN [>>70<<]. The specificity of this interaction is emphasized by the fact that neither Slug nor ZEB1 expression significantly alters PTEN levels [70]. Snail1’s association with the PTEN promoter inhibits the binding of p53, which activates PTEN
n3:mentions
n4:18172008
Subject Item
_:vb33216076
rdf:type
n3:Context
rdf:value
The specificity of this interaction is emphasized by the fact that neither Slug nor ZEB1 expression significantly alters PTEN levels [>>70<<]. Snail1’s association with the PTEN promoter inhibits the binding of p53, which activates PTEN during apoptosis, and it consequently increases resistance to gamma radiation-induced apoptosis [70],[71]. A positive feedback loop has been
n3:mentions
n4:18172008
Subject Item
_:vb33216077
rdf:type
n3:Context
rdf:value
Snail1’s association with the PTEN promoter inhibits the binding of p53, which activates PTEN during apoptosis, and it consequently increases resistance to gamma radiation-induced apoptosis [>>70<<],[71]. A positive feedback loop has been established around this interaction as well, since the repression of PTEN increases the expression of Akt [72]. Akt, operating through NF-κB, increases the expression of Snail1 [44]. Through this
n3:mentions
n4:18172008
Subject Item
_:vb33216078
rdf:type
n3:Context
rdf:value
Snail1’s association with the PTEN promoter inhibits the binding of p53, which activates PTEN during apoptosis, and it consequently increases resistance to gamma radiation-induced apoptosis [70],[>>71<<]. A positive feedback loop has been established around this interaction as well, since the repression of PTEN increases the expression of Akt [72]. Akt, operating through NF-κB, increases the expression of Snail1 [44]. Through this
n3:mentions
n4:11545734
Subject Item
_:vb33216079
rdf:type
n3:Context
rdf:value
A positive feedback loop has been established around this interaction as well, since the repression of PTEN increases the expression of Akt [>>72<<]. Akt, operating through NF-κB, increases the expression of Snail1 [44]. Through this pathway, Snail1 may contribute to raising its own expression levels [70].
n3:mentions
n4:11559746
Subject Item
_:vb33216080
rdf:type
n3:Context
rdf:value
Akt, operating through NF-κB, increases the expression of Snail1 [>>44<<]. Through this pathway, Snail1 may contribute to raising its own expression levels [70].
n3:mentions
n4:17563753
Subject Item
_:vb33216081
rdf:type
n3:Context
rdf:value
Through this pathway, Snail1 may contribute to raising its own expression levels [>>70<<].
n3:mentions
n4:18172008
Subject Item
_:vb33216082
rdf:type
n3:Context
rdf:value
The transmembrane protein has four hydrophobic domains within its 522 amino acid sequence and a molecular weight of 65 kDa [>>73<<],[74]. Though it is considered similar to connexins in gap junctions, occludin is found exclusively at tight junctions in epithelial and endothelial cells [73]. Snail1 functions as a transcriptional repressor of occludin, just as it does
n3:mentions
n4:8276896
Subject Item
_:vb33216083
rdf:type
n3:Context
rdf:value
The transmembrane protein has four hydrophobic domains within its 522 amino acid sequence and a molecular weight of 65 kDa [73],[>>74<<]. Though it is considered similar to connexins in gap junctions, occludin is found exclusively at tight junctions in epithelial and endothelial cells [73]. Snail1 functions as a transcriptional repressor of occludin, just as it does
n3:mentions
n4:8601611
Subject Item
_:vb33216084
rdf:type
n3:Context
rdf:value
Though it is considered similar to connexins in gap junctions, occludin is found exclusively at tight junctions in epithelial and endothelial cells [>>73<<]. Snail1 functions as a transcriptional repressor of occludin, just as it does E-cadherin in adherens junctions. By binding to the E-box in the occludin promoter sequence, Snail1 can completely repress the promoter activity [75].
n3:mentions
n4:8276896
Subject Item
_:vb33216085
rdf:type
n3:Context
rdf:value
By binding to the E-box in the occludin promoter sequence, Snail1 can completely repress the promoter activity [>>75<<]. Immunoblot analysis and immunocytochemistry confirm the considerable reduction of occludin expression in the presence of Snail1 [13]. This repression, along with that of E-cadherin and claudins, is critical to the loss of cell-to-cell
n3:mentions
n4:12668723
Subject Item
_:vb33216086
rdf:type
n3:Context
rdf:value
Immunoblot analysis and immunocytochemistry confirm the considerable reduction of occludin expression in the presence of Snail1 [>>13<<]. This repression, along with that of E-cadherin and claudins, is critical to the loss of cell-to-cell adhesion observed in EMT.
n3:mentions
n4:15314165
Subject Item
_:vb33216087
rdf:type
n3:Context
rdf:value
Family members range from 20-27 kDa, but they all share PDZ binding motifs, which allow them to interact with ZO-1, ZO-2, and MUPP-1, among others [>>76<<]. Claudins are components of tight junctions, and claudin-1 binds with occludin [76],[77]. The expression of claudins is frequently low or nonexistent in breast cancer cell lines, and it shares an inverse relationship with Snail1
n3:mentions
n4:19319969
Subject Item
_:vb33216088
rdf:type
n3:Context
rdf:value
Claudins are components of tight junctions, and claudin-1 binds with occludin [>>76<<],[77]. The expression of claudins is frequently low or nonexistent in breast cancer cell lines, and it shares an inverse relationship with Snail1 expression levels in invasive breast tumors [77].
n3:mentions
n4:19319969
Subject Item
_:vb33216089
rdf:type
n3:Context
rdf:value
Claudins are components of tight junctions, and claudin-1 binds with occludin [76],[>>77<<]. The expression of claudins is frequently low or nonexistent in breast cancer cell lines, and it shares an inverse relationship with Snail1 expression levels in invasive breast tumors [77].
n3:mentions
n4:16232121
Subject Item
_:vb33216090
rdf:type
n3:Context
rdf:value
The expression of claudins is frequently low or nonexistent in breast cancer cell lines, and it shares an inverse relationship with Snail1 expression levels in invasive breast tumors [>>77<<].
n3:mentions
n4:16232121
Subject Item
_:vb33216091
rdf:type
n3:Context
rdf:value
As such, Snail1 can completely inhibit their transcription [>>75<<]. The destruction of tight junctions that accompanies the repression of claudins and occludin leads to epithelial cells’ loss of apical polarity and increases proliferation [78].
n3:mentions
n4:12668723
Subject Item
_:vb33216092
rdf:type
n3:Context
rdf:value
The destruction of tight junctions that accompanies the repression of claudins and occludin leads to epithelial cells’ loss of apical polarity and increases proliferation [>>78<<]. This mechanism helps drive Snail1-induced EMT.
n3:mentions
n4:19059202
Subject Item
_:vb33216093
rdf:type
n3:Context
rdf:value
Mucin-1, a transmembrane glycoprotein encoded by MUC1, is an epithelial marker expressed at the apical surface of epithelial cells in the reproductive tract, digestive tract, lungs, kidney, liver, eyes, and other tissues [>>79<<]–[81]. Additionally, it is expressed in hematopoietic and T cells [80]. Mucin-1’s functions include lubrication and protection from pathogens, and its association with β-catenin has implicated Mucin-1 in cell signaling [80].
n3:mentions
n4:17083744
Subject Item
_:vb33216094
rdf:type
n3:Context
rdf:value
Mucin-1, a transmembrane glycoprotein encoded by MUC1, is an epithelial marker expressed at the apical surface of epithelial cells in the reproductive tract, digestive tract, lungs, kidney, liver, eyes, and other tissues [79]–[>>81<<]. Additionally, it is expressed in hematopoietic and T cells [80]. Mucin-1’s functions include lubrication and protection from pathogens, and its association with β-catenin has implicated Mucin-1 in cell signaling [80].
n3:mentions
n4:14681689
Subject Item
_:vb33216095
rdf:type
n3:Context
rdf:value
Additionally, it is expressed in hematopoietic and T cells [>>80<<]. Mucin-1’s functions include lubrication and protection from pathogens, and its association with β-catenin has implicated Mucin-1 in cell signaling [80].
n3:mentions
n4:14711375
Subject Item
_:vb33216096
rdf:type
n3:Context
rdf:value
Mucin-1’s functions include lubrication and protection from pathogens, and its association with β-catenin has implicated Mucin-1 in cell signaling [>>80<<]. O-linked glycosylation affects the protein significantly, as the core protein ranges from 120-225 kDa and the glycosylated form can reach up to 500 kDa [82]. In epithelial tumors, Mucin-1 is upregulated, and disparities in splice
n3:mentions
n4:14711375
Subject Item
_:vb33216097
rdf:type
n3:Context
rdf:value
O-linked glycosylation affects the protein significantly, as the core protein ranges from 120-225 kDa and the glycosylated form can reach up to 500 kDa [>>82<<]. In epithelial tumors, Mucin-1 is upregulated, and disparities in splice variants and glycosylation become apparent [79],[80]. Splice variants differ greatly—the protein can vary from 4-7 kb [82]. Perhaps most importantly, Mucin-1 also
n3:mentions
n4:7778880
Subject Item
_:vb33216098
rdf:type
n3:Context
rdf:value
In epithelial tumors, Mucin-1 is upregulated, and disparities in splice variants and glycosylation become apparent [>>79<<],[80]. Splice variants differ greatly—the protein can vary from 4-7 kb [82]. Perhaps most importantly, Mucin-1 also loses its apical restriction in malignant cases [80].
n3:mentions
n4:17083744
Subject Item
_:vb33216099
rdf:type
n3:Context
rdf:value
In epithelial tumors, Mucin-1 is upregulated, and disparities in splice variants and glycosylation become apparent [79],[>>80<<]. Splice variants differ greatly—the protein can vary from 4-7 kb [82]. Perhaps most importantly, Mucin-1 also loses its apical restriction in malignant cases [80].
n3:mentions
n4:14711375
Subject Item
_:vb33216100
rdf:type
n3:Context
rdf:value
Splice variants differ greatly—the protein can vary from 4-7 kb [>>82<<]. Perhaps most importantly, Mucin-1 also loses its apical restriction in malignant cases [80].
n3:mentions
n4:7778880
Subject Item
_:vb33216101
rdf:type
n3:Context
rdf:value
Perhaps most importantly, Mucin-1 also loses its apical restriction in malignant cases [>>80<<].
n3:mentions
n4:14711375
Subject Item
_:vb33216102
rdf:type
n3:Context
rdf:value
The 2872 bp promoter facilitates much of Mucin-1’s regulation, and it notably includes five sites for YY1 binding [>>79<<]. Snail1 interacts with the two E-boxes that begin -84 bp from the start of transcription.
n3:mentions
n4:17083744
Subject Item
_:vb33216103
rdf:type
n3:Context
rdf:value
Like E-cadherin, Mucin-1 is an epithelial marker repressed by Snail1 during the induction of EMT [>>83<<].
n3:mentions
n4:12161443
Subject Item
_:vb33216104
rdf:type
n3:Context
rdf:value
Using E-boxes and co-repressors such as CtBP and BRG1, ZEB-1 represses E-cadherin and Mucin-1 [>>83<<],[84]. However, ZEB-1 is at least ten times less potent a repressor of both E-cadherin and Mucin-1 than Snail1 [83]. Interference with the interaction between ZEB-1 and BRG1 results in the upregulation of E-cadherin and simultaneous
n3:mentions
n4:12161443
Subject Item
_:vb33216105
rdf:type
n3:Context
rdf:value
Using E-boxes and co-repressors such as CtBP and BRG1, ZEB-1 represses E-cadherin and Mucin-1 [83],[>>84<<]. However, ZEB-1 is at least ten times less potent a repressor of both E-cadherin and Mucin-1 than Snail1 [83]. Interference with the interaction between ZEB-1 and BRG1 results in the upregulation of E-cadherin and simultaneous
n3:mentions
n4:20418909
Subject Item
_:vb33216106
rdf:type
n3:Context
rdf:value
However, ZEB-1 is at least ten times less potent a repressor of both E-cadherin and Mucin-1 than Snail1 [>>83<<]. Interference with the interaction between ZEB-1 and BRG1 results in the upregulation of E-cadherin and simultaneous downregulation of vimentin, so an abundance of functional ZEB-1 is associated with a mesenchymal phenotype [84]. In
n3:mentions
n4:12161443
Subject Item
_:vb33216107
rdf:type
n3:Context
rdf:value
Interference with the interaction between ZEB-1 and BRG1 results in the upregulation of E-cadherin and simultaneous downregulation of vimentin, so an abundance of functional ZEB-1 is associated with a mesenchymal phenotype [>>84<<]. In contrast to the lethal effects of Snail1 knockout, ZEB-1 knockout does not prevent development to term and, thus, is not as critical for gastrulation [83].
n3:mentions
n4:20418909
Subject Item
_:vb33216108
rdf:type
n3:Context
rdf:value
In contrast to the lethal effects of Snail1 knockout, ZEB-1 knockout does not prevent development to term and, thus, is not as critical for gastrulation [>>83<<].
n3:mentions
n4:12161443
Subject Item
_:vb33216109
rdf:type
n3:Context
rdf:value
The abilities of Snail1 and ZEB-1 to repress E-cadherin are additive, and the two transcription factors work together to achieve a complete EMT [>>83<<].
n3:mentions
n4:12161443
Subject Item
_:vb33216110
rdf:type
n3:Context
rdf:value
Vimentin is 57 kDa intermediate filament generally restricted to mesenchymal cells [>>85<<]. Vimentin regulation is a complex interplay of epigenetic and post-translational modifications in addition to transcriptional regulation.
n3:mentions
n4:21637948
Subject Item
_:vb33216111
rdf:type
n3:Context
rdf:value
Of note, the human vimentin promoter contains an NF-κB binding site as well as a TGF-β1 response element [>>86<<],[87]. Akt1 protects vimentin from caspase proteolysis via phosphorylation of Ser39 [88]. During EMT, epithelial cells, which normally express keratin intermediate filaments, begin to express vimentin. Overexpression of vimentin is
n3:mentions
n4:8420985
Subject Item
_:vb33216112
rdf:type
n3:Context
rdf:value
Of note, the human vimentin promoter contains an NF-κB binding site as well as a TGF-β1 response element [86],[>>87<<]. Akt1 protects vimentin from caspase proteolysis via phosphorylation of Ser39 [88]. During EMT, epithelial cells, which normally express keratin intermediate filaments, begin to express vimentin. Overexpression of vimentin is evident in
n3:mentions
n4:17270292
Subject Item
_:vb33216113
rdf:type
n3:Context
rdf:value
Akt1 protects vimentin from caspase proteolysis via phosphorylation of Ser39 [>>88<<]. During EMT, epithelial cells, which normally express keratin intermediate filaments, begin to express vimentin. Overexpression of vimentin is evident in breast and prostate cancers, among many other types, and overexpression generally
n3:mentions
n4:20856200
Subject Item
_:vb33216114
rdf:type
n3:Context
rdf:value
Overexpression of vimentin is evident in breast and prostate cancers, among many other types, and overexpression generally correlates with invasiveness, migration, and poor prognosis [>>89<<]–[91]. Snail1 upregulates vimentin during EMT [54].
n3:mentions
n4:12750294
Subject Item
_:vb33216115
rdf:type
n3:Context
rdf:value
Overexpression of vimentin is evident in breast and prostate cancers, among many other types, and overexpression generally correlates with invasiveness, migration, and poor prognosis [89]–[>>91<<]. Snail1 upregulates vimentin during EMT [54].
n3:mentions
n4:18464297
Subject Item
_:vb33216116
rdf:type
n3:Context
rdf:value
Snail1 upregulates vimentin during EMT [>>54<<].
n3:mentions
n4:10655586
Subject Item
_:vb33216117
rdf:type
n3:Context
rdf:value
Fibronectin is a glycoprotein involved in cell adhesion, differentiation, and migration [>>92<<],[93]. A dimer with two 250 kDa components, fibronectin is greatly affected by splicing, and at least twenty variants of the human form have been identified [94].
n3:mentions
n4:6128348
Subject Item
_:vb33216118
rdf:type
n3:Context
rdf:value
A dimer with two 250 kDa components, fibronectin is greatly affected by splicing, and at least twenty variants of the human form have been identified [>>94<<]. Fibronectin interacts with many integrins in addition to heparin, collagen, and fibrin [95]–[99]. Inactivation of fibronectin is lethal in mice [100]. Snail1 upregulates fibronectin, a mesenchymal marker indicative of EMT [54].
n3:mentions
n4:12244123
Subject Item
_:vb33216119
rdf:type
n3:Context
rdf:value
Fibronectin interacts with many integrins in addition to heparin, collagen, and fibrin [>>95<<]–[99]. Inactivation of fibronectin is lethal in mice [100]. Snail1 upregulates fibronectin, a mesenchymal marker indicative of EMT [54].
n3:mentions
n4:3207688
Subject Item
_:vb33216120
rdf:type
n3:Context
rdf:value
Fibronectin interacts with many integrins in addition to heparin, collagen, and fibrin [95]–[>>99<<]. Inactivation of fibronectin is lethal in mice [100]. Snail1 upregulates fibronectin, a mesenchymal marker indicative of EMT [54].
n3:mentions
n4:23653354
Subject Item
_:vb33216121
rdf:type
n3:Context
rdf:value
Inactivation of fibronectin is lethal in mice [>>100<<]. Snail1 upregulates fibronectin, a mesenchymal marker indicative of EMT [54].
n3:mentions
n4:8306876
Subject Item
_:vb33216122
rdf:type
n3:Context
rdf:value
Inactivation of fibronectin is lethal in mice [100]. Snail1 upregulates fibronectin, a mesenchymal marker indicative of EMT [>>54<<].
n3:mentions
n4:10655586
Subject Item
_:vb33216123
rdf:type
n3:Context
rdf:value
Cytokeratins exist in two types, and each cytokeratin works with a complementary partner to form keratin filaments [>>101<<]. Cytokeratin 18 is the first type, acidic, and interacts with the basic cytokeratin 8 [101].
n3:mentions
n4:6186379
Subject Item
_:vb33216124
rdf:type
n3:Context
rdf:value
Cytokeratin 18 is the first type, acidic, and interacts with the basic cytokeratin 8 [>>101<<]. The cytokeratin 18 protein is encoded by the CK18 gene, which is located on chromosome 12q13. Cytokeratin 18 is an intermediate filament protein involved in cell structure, cell signaling, and the cell cycle [101]–[104]. Cytokeratin 18
n3:mentions
n4:6186379
Subject Item
_:vb33216125
rdf:type
n3:Context
rdf:value
Cytokeratin 18 is an intermediate filament protein involved in cell structure, cell signaling, and the cell cycle [>>101<<]–[104]. Cytokeratin 18 serves as an epithelial marker, and it localizes in epithelial organs, such as the kidney, liver, gastrointestinal tract, and mammary glands [105]. Snail1 represses cytokeratin 18 during the induction of EMT [83].
n3:mentions
n4:6186379
Subject Item
_:vb33216126
rdf:type
n3:Context
rdf:value
Cytokeratin 18 is an intermediate filament protein involved in cell structure, cell signaling, and the cell cycle [101]–[>>104<<]. Cytokeratin 18 serves as an epithelial marker, and it localizes in epithelial organs, such as the kidney, liver, gastrointestinal tract, and mammary glands [105]. Snail1 represses cytokeratin 18 during the induction of EMT [83]. Unlike
n3:mentions
n4:17112511
Subject Item
_:vb33216127
rdf:type
n3:Context
rdf:value
Cytokeratin 18 serves as an epithelial marker, and it localizes in epithelial organs, such as the kidney, liver, gastrointestinal tract, and mammary glands [>>105<<]. Snail1 represses cytokeratin 18 during the induction of EMT [83]. Unlike other targets, though, cytokeratin 18 expression is not completely subdued by Snail1’s presence [75].
n3:mentions
n4:9034603
Subject Item
_:vb33216128
rdf:type
n3:Context
rdf:value
Snail1 represses cytokeratin 18 during the induction of EMT [>>83<<]. Unlike other targets, though, cytokeratin 18 expression is not completely subdued by Snail1’s presence [75].
n3:mentions
n4:12161443
Subject Item
_:vb33216129
rdf:type
n3:Context
rdf:value
Unlike other targets, though, cytokeratin 18 expression is not completely subdued by Snail1’s presence [>>75<<].
n3:mentions
n4:12668723
Subject Item
_:vb33216130
rdf:type
n3:Context
rdf:value
Matrix metalloproteinases (MMP) cleave extracellular matrix substrates and, thereby, alter cell-matrix adhesions [>>106<<]. MMP-2 and -9 are a subcategory within the MMP group because they specifically act on gelatin, collagen, elastin, and fibronectin [107]–[111].
n3:mentions
n4:16730219
Subject Item
_:vb33216131
rdf:type
n3:Context
rdf:value
MMP-2 and -9 are a subcategory within the MMP group because they specifically act on gelatin, collagen, elastin, and fibronectin [>>107<<]–[111]. The genes that encode MMP-2 and -9 both contain fibronectin type II domains and are consequently three exons longer than the other MMP genes [107]. MMP-2 is a 72 kDa protein while MMP-9 is 92 kDa, and the main difference between
n3:mentions
n4:8435466
Subject Item
_:vb33216132
rdf:type
n3:Context
rdf:value
MMP-2 and -9 are a subcategory within the MMP group because they specifically act on gelatin, collagen, elastin, and fibronectin [107]–[>>111<<]. The genes that encode MMP-2 and -9 both contain fibronectin type II domains and are consequently three exons longer than the other MMP genes [107]. MMP-2 is a 72 kDa protein while MMP-9 is 92 kDa, and the main difference between them is
n3:mentions
n4:2542740
Subject Item
_:vb33216133
rdf:type
n3:Context
rdf:value
The genes that encode MMP-2 and -9 both contain fibronectin type II domains and are consequently three exons longer than the other MMP genes [>>107<<]. MMP-2 is a 72 kDa protein while MMP-9 is 92 kDa, and the main difference between them is the MMP-9’s 54 amino acid hinge region [107],[112]. Additionally, MMP-2 localizes in the nucleus and MMP-9 in the cytoplasm [113]. Overexpression
n3:mentions
n4:8435466
Subject Item
_:vb33216134
rdf:type
n3:Context
rdf:value
MMP-2 is a 72 kDa protein while MMP-9 is 92 kDa, and the main difference between them is the MMP-9’s 54 amino acid hinge region [>>107<<],[112]. Additionally, MMP-2 localizes in the nucleus and MMP-9 in the cytoplasm [113]. Overexpression of MMP-2 and MMP-9 is frequently associated with invasive, metastatic tumors [114]–[117].
n3:mentions
n4:8435466
Subject Item
_:vb33216135
rdf:type
n3:Context
rdf:value
MMP-2 is a 72 kDa protein while MMP-9 is 92 kDa, and the main difference between them is the MMP-9’s 54 amino acid hinge region [107],[>>112<<]. Additionally, MMP-2 localizes in the nucleus and MMP-9 in the cytoplasm [113]. Overexpression of MMP-2 and MMP-9 is frequently associated with invasive, metastatic tumors [114]–[117].
n3:mentions
n4:1653238
Subject Item
_:vb33216136
rdf:type
n3:Context
rdf:value
Additionally, MMP-2 localizes in the nucleus and MMP-9 in the cytoplasm [>>113<<]. Overexpression of MMP-2 and MMP-9 is frequently associated with invasive, metastatic tumors [114]–[117].
n3:mentions
n4:20664935
Subject Item
_:vb33216137
rdf:type
n3:Context
rdf:value
Overexpression of MMP-2 and MMP-9 is frequently associated with invasive, metastatic tumors [>>114<<]–[117].
n3:mentions
n4:6243750
Subject Item
_:vb33216138
rdf:type
n3:Context
rdf:value
Overexpression of MMP-2 and MMP-9 is frequently associated with invasive, metastatic tumors [114]–[>>117<<].
n3:mentions
n4:2162246
Subject Item
_:vb33216139
rdf:type
n3:Context
rdf:value
One suggested interaction includes the upregulation of MMP-2 and -9 by Snail1 to trigger EMT and, then, the coordinated effort of Snail1 and Slug to sustain EMT by continually stimulating MMP-9 [>>113<<].
n3:mentions
n4:20664935
Subject Item
_:vb33216140
rdf:type
n3:Context
rdf:value
Lymphoid enhancer-binding factor 1 (LEF-1) is a T-cell factor commonly detected in tumors [>>119<<],[120]. The transcription factor represses E-cadherin by forming complexes with β-catenin, which, like Snail1, is degraded as a result of GSK-3β-mediated phosphorylation [11],[121]–[123].
n3:mentions
n4:9419974
Subject Item
_:vb33216141
rdf:type
n3:Context
rdf:value
Lymphoid enhancer-binding factor 1 (LEF-1) is a T-cell factor commonly detected in tumors [119],[>>120<<]. The transcription factor represses E-cadherin by forming complexes with β-catenin, which, like Snail1, is degraded as a result of GSK-3β-mediated phosphorylation [11],[121]–[123].
n3:mentions
n4:9065403
Subject Item
_:vb33216142
rdf:type
n3:Context
rdf:value
The transcription factor represses E-cadherin by forming complexes with β-catenin, which, like Snail1, is degraded as a result of GSK-3β-mediated phosphorylation [>>11<<],[121]–[123].
n3:mentions
n4:11689706
Subject Item
_:vb33216143
rdf:type
n3:Context
rdf:value
The transcription factor represses E-cadherin by forming complexes with β-catenin, which, like Snail1, is degraded as a result of GSK-3β-mediated phosphorylation [11],[>>121<<]–[123]. LEF-1 interacts with Snail1 via Wnt, PI3K and TGF-β1 pathways, and both Snail1 and LEF-1 are necessary for a complete EMT [124]. LEF-1 is considered a mesenchymal marker, and Snail1 induces its expression and continues to
n3:mentions
n4:12646922
Subject Item
_:vb33216144
rdf:type
n3:Context
rdf:value
The transcription factor represses E-cadherin by forming complexes with β-catenin, which, like Snail1, is degraded as a result of GSK-3β-mediated phosphorylation [11],[121]–[>>123<<]. LEF-1 interacts with Snail1 via Wnt, PI3K and TGF-β1 pathways, and both Snail1 and LEF-1 are necessary for a complete EMT [124]. LEF-1 is considered a mesenchymal marker, and Snail1 induces its expression and continues to upregulate it
n3:mentions
n4:15000148
Subject Item
_:vb33216145
rdf:type
n3:Context
rdf:value
LEF-1 interacts with Snail1 via Wnt, PI3K and TGF-β1 pathways, and both Snail1 and LEF-1 are necessary for a complete EMT [>>124<<]. LEF-1 is considered a mesenchymal marker, and Snail1 induces its expression and continues to upregulate it [82],[125].
n3:mentions
n4:16467384
Subject Item
_:vb33216146
rdf:type
n3:Context
rdf:value
LEF-1 is considered a mesenchymal marker, and Snail1 induces its expression and continues to upregulate it [>>82<<],[125].
n3:mentions
n4:7778880
Subject Item
_:vb33216147
rdf:type
n3:Context
rdf:value
LEF-1 is considered a mesenchymal marker, and Snail1 induces its expression and continues to upregulate it [82],[>>125<<].
n3:mentions
n4:15683729
Subject Item
_:vb33216148
rdf:type
n2:Section
dc:title
snail1 expression in cancer
n2:contains
_:vb33216180 _:vb33216181 _:vb33216182 _:vb33216183 _:vb33216176 _:vb33216177 _:vb33216178 _:vb33216179 _:vb33216188 _:vb33216189 _:vb33216190 _:vb33216191 _:vb33216184 _:vb33216185 _:vb33216186 _:vb33216187 _:vb33216164 _:vb33216165 _:vb33216166 _:vb33216167 _:vb33216160 _:vb33216161 _:vb33216162 _:vb33216163 _:vb33216172 _:vb33216173 _:vb33216174 _:vb33216175 _:vb33216168 _:vb33216169 _:vb33216170 _:vb33216171 _:vb33216149 _:vb33216150 _:vb33216151 _:vb33216156 _:vb33216157 _:vb33216158 _:vb33216159 _:vb33216152 _:vb33216153 _:vb33216154 _:vb33216155 _:vb33216244 _:vb33216245 _:vb33216246 _:vb33216247 _:vb33216240 _:vb33216241 _:vb33216242 _:vb33216243 _:vb33216252 _:vb33216253 _:vb33216254 _:vb33216248 _:vb33216249 _:vb33216250 _:vb33216251 _:vb33216228 _:vb33216229 _:vb33216230 _:vb33216231 _:vb33216224 _:vb33216225 _:vb33216226 _:vb33216227 _:vb33216236 _:vb33216237 _:vb33216238 _:vb33216239 _:vb33216232 _:vb33216233 _:vb33216234 _:vb33216235 _:vb33216212 _:vb33216213 _:vb33216214 _:vb33216215 _:vb33216208 _:vb33216209 _:vb33216210 _:vb33216211 _:vb33216220 _:vb33216221 _:vb33216222 _:vb33216223 _:vb33216216 _:vb33216217 _:vb33216218 _:vb33216219 _:vb33216196 _:vb33216197 _:vb33216198 _:vb33216199 _:vb33216192 _:vb33216193 _:vb33216194 _:vb33216195 _:vb33216204 _:vb33216205 _:vb33216206 _:vb33216207 _:vb33216200 _:vb33216201 _:vb33216202 _:vb33216203
Subject Item
_:vb33216149
rdf:type
n3:Context
rdf:value
Type of CancerSnail ExpressionChange in expression over disease progressionPrognostic significanceReference(s)Bladder carcinomaInverse correlation with E-cadherin [>>130<<]; low expression level (only 16% of carcinoma tissues, n = 120)—Slug and Twist appear to be more important [140]Increased expression in node-positive vs.
n3:mentions
n4:11857019
Subject Item
_:vb33216150
rdf:type
n3:Context
rdf:value
expression over disease progressionPrognostic significanceReference(s)Bladder carcinomaInverse correlation with E-cadherin [130]; low expression level (only 16% of carcinoma tissues, n = 120)—Slug and Twist appear to be more important [>>140<<]Increased expression in node-positive vs.
n3:mentions
n4:23342249
Subject Item
_:vb33216151
rdf:type
n3:Context
rdf:value
node-negative tumors; 3 year progression free survival rate with positive Snail expression only 15% [>>140<<]Snail expression associated with tumor recurrence; elevated expression is significant, independent prognostic factor [140],[141][130],[140],[141]Breast carcinomaNone in normal breast epithelium; in 47% of IDCs (n = 17); none in ILCs (n =
n3:mentions
n4:23342249
Subject Item
_:vb33216152
rdf:type
n3:Context
rdf:value
node-negative tumors; 3 year progression free survival rate with positive Snail expression only 15% [140]Snail expression associated with tumor recurrence; elevated expression is significant, independent prognostic factor [>>140<<],[141][130],[140],[141]Breast carcinomaNone in normal breast epithelium; in 47% of IDCs (n = 17); none in ILCs (n = 4); expression correlates with lymph node metastases; not found in cells with constitutively inactive E-cadherin;
n3:mentions
n4:23342249
Subject Item
_:vb33216153
rdf:type
n3:Context
rdf:value
node-negative tumors; 3 year progression free survival rate with positive Snail expression only 15% [140]Snail expression associated with tumor recurrence; elevated expression is significant, independent prognostic factor [140],[>>141<<][130],[140],[141]Breast carcinomaNone in normal breast epithelium; in 47% of IDCs (n = 17); none in ILCs (n = 4); expression correlates with lymph node metastases; not found in cells with constitutively inactive E-cadherin; expression
n3:mentions
n4:20809941
Subject Item
_:vb33216154
rdf:type
n3:Context
rdf:value
node-negative tumors; 3 year progression free survival rate with positive Snail expression only 15% [140]Snail expression associated with tumor recurrence; elevated expression is significant, independent prognostic factor [140],[141][>>130<<],[140],[141]Breast carcinomaNone in normal breast epithelium; in 47% of IDCs (n = 17); none in ILCs (n = 4); expression correlates with lymph node metastases; not found in cells with constitutively inactive E-cadherin; expression opposes
n3:mentions
n4:11857019
Subject Item
_:vb33216155
rdf:type
n3:Context
rdf:value
tumors; 3 year progression free survival rate with positive Snail expression only 15% [140]Snail expression associated with tumor recurrence; elevated expression is significant, independent prognostic factor [140],[141][130],[>>140<<],[141]Breast carcinomaNone in normal breast epithelium; in 47% of IDCs (n = 17); none in ILCs (n = 4); expression correlates with lymph node metastases; not found in cells with constitutively inactive E-cadherin; expression opposes
n3:mentions
n4:23342249
Subject Item
_:vb33216156
rdf:type
n3:Context
rdf:value
tumors; 3 year progression free survival rate with positive Snail expression only 15% [140]Snail expression associated with tumor recurrence; elevated expression is significant, independent prognostic factor [140],[141][130],[140],[>>141<<]Breast carcinomaNone in normal breast epithelium; in 47% of IDCs (n = 17); none in ILCs (n = 4); expression correlates with lymph node metastases; not found in cells with constitutively inactive E-cadherin; expression opposes E-cadherin
n3:mentions
n4:20809941
Subject Item
_:vb33216157
rdf:type
n3:Context
rdf:value
carcinomaNone in normal breast epithelium; in 47% of IDCs (n = 17); none in ILCs (n = 4); expression correlates with lymph node metastases; not found in cells with constitutively inactive E-cadherin; expression opposes E-cadherin [>>128<<]; Snail overexpressed; Snail/E-cadherin ratio significantly higher [129]Snail expression in IDCs (n = 17):
n3:mentions
n4:12082640
Subject Item
_:vb33216158
rdf:type
n3:Context
rdf:value
none in ILCs (n = 4); expression correlates with lymph node metastases; not found in cells with constitutively inactive E-cadherin; expression opposes E-cadherin [128]; Snail overexpressed; Snail/E-cadherin ratio significantly higher [>>129<<]Snail expression in IDCs (n = 17):
n3:mentions
n4:15742334
Subject Item
_:vb33216159
rdf:type
n3:Context
rdf:value
with constitutively inactive E-cadherin; expression opposes E-cadherin [128]; Snail overexpressed; Snail/E-cadherin ratio significantly higher [129]Snail expression in IDCs (n = 17): grade 1—none; grade 2—more than half; grade 3—most [>>128<<]Potential marker of IDC malignancy [128]; High expression correlated with shorter effusion-free, disease-free, and overall survival; correlated with lymph node metastases and high histologic grade (n = 16) [129][128],[129]Cervical
n3:mentions
n4:12082640
Subject Item
_:vb33216160
rdf:type
n3:Context
rdf:value
expression opposes E-cadherin [128]; Snail overexpressed; Snail/E-cadherin ratio significantly higher [129]Snail expression in IDCs (n = 17): grade 1—none; grade 2—more than half; grade 3—most [128]Potential marker of IDC malignancy [>>128<<]; High expression correlated with shorter effusion-free, disease-free, and overall survival; correlated with lymph node metastases and high histologic grade (n = 16) [129][128],[129]Cervical carcinomaSnail expressed in 94% of samples (n =
n3:mentions
n4:12082640
Subject Item
_:vb33216161
rdf:type
n3:Context
rdf:value
than half; grade 3—most [128]Potential marker of IDC malignancy [128]; High expression correlated with shorter effusion-free, disease-free, and overall survival; correlated with lymph node metastases and high histologic grade (n = 16) [>>129<<][128],[129]Cervical carcinomaSnail expressed in 94% of samples (n = 70) and ZEB-1 in 96%; nuclear expression of both correlates with advanced FIGO stage and lymph node metastasis; expression of Snail correlates with poor differentiation
n3:mentions
n4:15742334
Subject Item
_:vb33216162
rdf:type
n3:Context
rdf:value
half; grade 3—most [128]Potential marker of IDC malignancy [128]; High expression correlated with shorter effusion-free, disease-free, and overall survival; correlated with lymph node metastases and high histologic grade (n = 16) [129][>>128<<],[129]Cervical carcinomaSnail expressed in 94% of samples (n = 70) and ZEB-1 in 96%; nuclear expression of both correlates with advanced FIGO stage and lymph node metastasis; expression of Snail correlates with poor differentiation
n3:mentions
n4:12082640
Subject Item
_:vb33216163
rdf:type
n3:Context
rdf:value
grade 3—most [128]Potential marker of IDC malignancy [128]; High expression correlated with shorter effusion-free, disease-free, and overall survival; correlated with lymph node metastases and high histologic grade (n = 16) [129][128],[>>129<<]Cervical carcinomaSnail expressed in 94% of samples (n = 70) and ZEB-1 in 96%; nuclear expression of both correlates with advanced FIGO stage and lymph node metastasis; expression of Snail correlates with poor differentiation [153]High
n3:mentions
n4:15742334
Subject Item
_:vb33216164
rdf:type
n3:Context
rdf:value
carcinomaSnail expressed in 94% of samples (n = 70) and ZEB-1 in 96%; nuclear expression of both correlates with advanced FIGO stage and lymph node metastasis; expression of Snail correlates with poor differentiation [>>153<<]High Snail expression associated with late FIGO stage, lymph node metastasis, and poor differentiation [153] [153]Colorectal carcinomaInverse correlation with E-cadherin [130]; markedly high expression (78% of tested tumors, n = 59) of
n3:mentions
n4:23791009
Subject Item
_:vb33216165
rdf:type
n3:Context
rdf:value
both correlates with advanced FIGO stage and lymph node metastasis; expression of Snail correlates with poor differentiation [153]High Snail expression associated with late FIGO stage, lymph node metastasis, and poor differentiation [>>153<<] [153]Colorectal carcinomaInverse correlation with E-cadherin [130]; markedly high expression (78% of tested tumors, n = 59) of Snail; Snail-positive in older age group than Snail-negative (mean 58.9 vs.
n3:mentions
n4:23791009
Subject Item
_:vb33216166
rdf:type
n3:Context
rdf:value
correlates with advanced FIGO stage and lymph node metastasis; expression of Snail correlates with poor differentiation [153]High Snail expression associated with late FIGO stage, lymph node metastasis, and poor differentiation [153] [>>153<<]Colorectal carcinomaInverse correlation with E-cadherin [130]; markedly high expression (78% of tested tumors, n = 59) of Snail; Snail-positive in older age group than Snail-negative (mean 58.9 vs.
n3:mentions
n4:23791009
Subject Item
_:vb33216167
rdf:type
n3:Context
rdf:value
expression of Snail correlates with poor differentiation [153]High Snail expression associated with late FIGO stage, lymph node metastasis, and poor differentiation [153] [153]Colorectal carcinomaInverse correlation with E-cadherin [>>130<<]; markedly high expression (78% of tested tumors, n = 59) of Snail; Snail-positive in older age group than Snail-negative (mean 58.9 vs.
n3:mentions
n4:11857019
Subject Item
_:vb33216168
rdf:type
n3:Context
rdf:value
49.8, n = 59) [>>138<<]; Snail expressed in all tested CRC cell lines (Western blot); expression increased migration and invasiveness; decreased E-cadherin; led to CSC-like phenotype and spindle morphology [139]Increase in expression over disease progression:
n3:mentions
n4:19474385
Subject Item
_:vb33216169
rdf:type
n3:Context
rdf:value
49.8, n = 59) [138]; Snail expressed in all tested CRC cell lines (Western blot); expression increased migration and invasiveness; decreased E-cadherin; led to CSC-like phenotype and spindle morphology [>>139<<]Increase in expression over disease progression:
n3:mentions
n4:15712635
Subject Item
_:vb33216170
rdf:type
n3:Context
rdf:value
6/6 stage IV [>>138<<]; significantly higher rate of metastasis among Snail-expressing than Snail-negative [139]Snail expression indicates high risk of distant metastases [138],[139][130],[138],[139]Gastric carcinomaSnail expression higher in diffuse than
n3:mentions
n4:19474385
Subject Item
_:vb33216171
rdf:type
n3:Context
rdf:value
6/6 stage IV [138]; significantly higher rate of metastasis among Snail-expressing than Snail-negative [>>139<<]Snail expression indicates high risk of distant metastases [138],[139][130],[138],[139]Gastric carcinomaSnail expression higher in diffuse than intestinal type [134]; inverse correlation with E-cadherin; significantly reduced E-cadherin
n3:mentions
n4:15712635
Subject Item
_:vb33216172
rdf:type
n3:Context
rdf:value
6/6 stage IV [138]; significantly higher rate of metastasis among Snail-expressing than Snail-negative [139]Snail expression indicates high risk of distant metastases [>>138<<],[139][130],[138],[139]Gastric carcinomaSnail expression higher in diffuse than intestinal type [134]; inverse correlation with E-cadherin; significantly reduced E-cadherin expression; Snail expression more comparable to breast than
n3:mentions
n4:19474385
Subject Item
_:vb33216173
rdf:type
n3:Context
rdf:value
6/6 stage IV [138]; significantly higher rate of metastasis among Snail-expressing than Snail-negative [139]Snail expression indicates high risk of distant metastases [138],[>>139<<][130],[138],[139]Gastric carcinomaSnail expression higher in diffuse than intestinal type [134]; inverse correlation with E-cadherin; significantly reduced E-cadherin expression; Snail expression more comparable to breast than ovarian
n3:mentions
n4:15712635
Subject Item
_:vb33216174
rdf:type
n3:Context
rdf:value
6/6 stage IV [138]; significantly higher rate of metastasis among Snail-expressing than Snail-negative [139]Snail expression indicates high risk of distant metastases [138],[139][>>130<<],[138],[139]Gastric carcinomaSnail expression higher in diffuse than intestinal type [134]; inverse correlation with E-cadherin; significantly reduced E-cadherin expression; Snail expression more comparable to breast than ovarian
n3:mentions
n4:11857019
Subject Item
_:vb33216175
rdf:type
n3:Context
rdf:value
6/6 stage IV [138]; significantly higher rate of metastasis among Snail-expressing than Snail-negative [139]Snail expression indicates high risk of distant metastases [138],[139][130],[>>138<<],[139]Gastric carcinomaSnail expression higher in diffuse than intestinal type [134]; inverse correlation with E-cadherin; significantly reduced E-cadherin expression; Snail expression more comparable to breast than ovarian carcinoma
n3:mentions
n4:19474385
Subject Item
_:vb33216176
rdf:type
n3:Context
rdf:value
6/6 stage IV [138]; significantly higher rate of metastasis among Snail-expressing than Snail-negative [139]Snail expression indicates high risk of distant metastases [138],[139][130],[138],[>>139<<]Gastric carcinomaSnail expression higher in diffuse than intestinal type [134]; inverse correlation with E-cadherin; significantly reduced E-cadherin expression; Snail expression more comparable to breast than ovarian carcinoma
n3:mentions
n4:15712635
Subject Item
_:vb33216177
rdf:type
n3:Context
rdf:value
higher rate of metastasis among Snail-expressing than Snail-negative [139]Snail expression indicates high risk of distant metastases [138],[139][130],[138],[139]Gastric carcinomaSnail expression higher in diffuse than intestinal type [>>134<<]; inverse correlation with E-cadherin; significantly reduced E-cadherin expression; Snail expression more comparable to breast than ovarian carcinoma [129]Overexpression associated with tumor size, depth of invasion, lymph node
n3:mentions
n4:12414534
Subject Item
_:vb33216178
rdf:type
n3:Context
rdf:value
carcinomaSnail expression higher in diffuse than intestinal type [134]; inverse correlation with E-cadherin; significantly reduced E-cadherin expression; Snail expression more comparable to breast than ovarian carcinoma [>>129<<]Overexpression associated with tumor size, depth of invasion, lymph node metastasis, shortened survival [135]Considered independent predictor of poor prognosis [135][129],[134],[135]Hepatocellular carcinomaInverse correlation of mRNA and
n3:mentions
n4:15742334
Subject Item
_:vb33216179
rdf:type
n3:Context
rdf:value
E-cadherin; significantly reduced E-cadherin expression; Snail expression more comparable to breast than ovarian carcinoma [129]Overexpression associated with tumor size, depth of invasion, lymph node metastasis, shortened survival [>>135<<]Considered independent predictor of poor prognosis [135][129],[134],[135]Hepatocellular carcinomaInverse correlation of mRNA and protein levels with E-cadherin (E-cadherin in Hep-G2 while Snail in HuL-1, Changliver, HLE, and HLF cells)
n3:mentions
n4:23151184
Subject Item
_:vb33216180
rdf:type
n3:Context
rdf:value
Snail expression more comparable to breast than ovarian carcinoma [129]Overexpression associated with tumor size, depth of invasion, lymph node metastasis, shortened survival [135]Considered independent predictor of poor prognosis [>>135<<][129],[134],[135]Hepatocellular carcinomaInverse correlation of mRNA and protein levels with E-cadherin (E-cadherin in Hep-G2 while Snail in HuL-1, Changliver, HLE, and HLF cells) [130]; Snail correlates with invasiveness and metastasis,
n3:mentions
n4:23151184
Subject Item
_:vb33216181
rdf:type
n3:Context
rdf:value
expression more comparable to breast than ovarian carcinoma [129]Overexpression associated with tumor size, depth of invasion, lymph node metastasis, shortened survival [135]Considered independent predictor of poor prognosis [135][>>129<<],[134],[135]Hepatocellular carcinomaInverse correlation of mRNA and protein levels with E-cadherin (E-cadherin in Hep-G2 while Snail in HuL-1, Changliver, HLE, and HLF cells) [130]; Snail correlates with invasiveness and metastasis, Snail
n3:mentions
n4:15742334
Subject Item
_:vb33216182
rdf:type
n3:Context
rdf:value
more comparable to breast than ovarian carcinoma [129]Overexpression associated with tumor size, depth of invasion, lymph node metastasis, shortened survival [135]Considered independent predictor of poor prognosis [135][129],[>>134<<],[135]Hepatocellular carcinomaInverse correlation of mRNA and protein levels with E-cadherin (E-cadherin in Hep-G2 while Snail in HuL-1, Changliver, HLE, and HLF cells) [130]; Snail correlates with invasiveness and metastasis, Snail
n3:mentions
n4:12414534
Subject Item
_:vb33216183
rdf:type
n3:Context
rdf:value
more comparable to breast than ovarian carcinoma [129]Overexpression associated with tumor size, depth of invasion, lymph node metastasis, shortened survival [135]Considered independent predictor of poor prognosis [135][129],[134],[>>135<<]Hepatocellular carcinomaInverse correlation of mRNA and protein levels with E-cadherin (E-cadherin in Hep-G2 while Snail in HuL-1, Changliver, HLE, and HLF cells) [130]; Snail correlates with invasiveness and metastasis, Snail
n3:mentions
n4:23151184
Subject Item
_:vb33216184
rdf:type
n3:Context
rdf:value
independent predictor of poor prognosis [135][129],[134],[135]Hepatocellular carcinomaInverse correlation of mRNA and protein levels with E-cadherin (E-cadherin in Hep-G2 while Snail in HuL-1, Changliver, HLE, and HLF cells) [>>130<<]; Snail correlates with invasiveness and metastasis, Snail overexpression in 23% of cases (n = 47) [131]Higher Snail expression in higher grade cases (n = 12) [132]Risk factor for early recurrence (n = 47) [131]; Snail correlated with
n3:mentions
n4:11857019
Subject Item
_:vb33216185
rdf:type
n3:Context
rdf:value
correlation of mRNA and protein levels with E-cadherin (E-cadherin in Hep-G2 while Snail in HuL-1, Changliver, HLE, and HLF cells) [130]; Snail correlates with invasiveness and metastasis, Snail overexpression in 23% of cases (n = 47) [>>131<<]Higher Snail expression in higher grade cases (n = 12) [132]Risk factor for early recurrence (n = 47) [131]; Snail correlated with portal vein invasion, metastasis, poorer prognosis in recurrence-free survival
n3:mentions
n4:15668718
Subject Item
_:vb33216186
rdf:type
n3:Context
rdf:value
in Hep-G2 while Snail in HuL-1, Changliver, HLE, and HLF cells) [130]; Snail correlates with invasiveness and metastasis, Snail overexpression in 23% of cases (n = 47) [131]Higher Snail expression in higher grade cases (n = 12) [>>132<<]Risk factor for early recurrence (n = 47) [131]; Snail correlated with portal vein invasion, metastasis, poorer prognosis in recurrence-free survival [132][130]–[132]MelanomasHigh mRNA expression in all tested melanoma cell lines but not
n3:mentions
n4:21494073
Subject Item
_:vb33216187
rdf:type
n3:Context
rdf:value
HLE, and HLF cells) [130]; Snail correlates with invasiveness and metastasis, Snail overexpression in 23% of cases (n = 47) [131]Higher Snail expression in higher grade cases (n = 12) [132]Risk factor for early recurrence (n = 47) [>>131<<]; Snail correlated with portal vein invasion, metastasis, poorer prognosis in recurrence-free survival [132][130]–[132]MelanomasHigh mRNA expression in all tested melanoma cell lines but not primary melanocytes; low E-cadherin in presence
n3:mentions
n4:15668718
Subject Item
_:vb33216188
rdf:type
n3:Context
rdf:value
of cases (n = 47) [131]Higher Snail expression in higher grade cases (n = 12) [132]Risk factor for early recurrence (n = 47) [131]; Snail correlated with portal vein invasion, metastasis, poorer prognosis in recurrence-free survival [>>132<<][130]–[132]MelanomasHigh mRNA expression in all tested melanoma cell lines but not primary melanocytes; low E-cadherin in presence of Snail [142]; inverse correlation with E-cadherin [130]; Snail confers invasive and immunosuppressive
n3:mentions
n4:21494073
Subject Item
_:vb33216189
rdf:type
n3:Context
rdf:value
cases (n = 47) [131]Higher Snail expression in higher grade cases (n = 12) [132]Risk factor for early recurrence (n = 47) [131]; Snail correlated with portal vein invasion, metastasis, poorer prognosis in recurrence-free survival [132][>>130<<]–[132]MelanomasHigh mRNA expression in all tested melanoma cell lines but not primary melanocytes; low E-cadherin in presence of Snail [142]; inverse correlation with E-cadherin [130]; Snail confers invasive and immunosuppressive
n3:mentions
n4:11857019
Subject Item
_:vb33216190
rdf:type
n3:Context
rdf:value
(n = 47) [131]Higher Snail expression in higher grade cases (n = 12) [132]Risk factor for early recurrence (n = 47) [131]; Snail correlated with portal vein invasion, metastasis, poorer prognosis in recurrence-free survival [132][130]–[>>132<<]MelanomasHigh mRNA expression in all tested melanoma cell lines but not primary melanocytes; low E-cadherin in presence of Snail [142]; inverse correlation with E-cadherin [130]; Snail confers invasive and immunosuppressive properties
n3:mentions
n4:21494073
Subject Item
_:vb33216191
rdf:type
n3:Context
rdf:value
with portal vein invasion, metastasis, poorer prognosis in recurrence-free survival [132][130]–[132]MelanomasHigh mRNA expression in all tested melanoma cell lines but not primary melanocytes; low E-cadherin in presence of Snail [>>142<<]; inverse correlation with E-cadherin [130]; Snail confers invasive and immunosuppressive properties [143]  [130],[142],[143]Oral squamous carcinomaLow E-cadherin/high Snail expression cells more invasive; E-cadherin positive had cuboidal
n3:mentions
n4:19162513
Subject Item
_:vb33216192
rdf:type
n3:Context
rdf:value
poorer prognosis in recurrence-free survival [132][130]–[132]MelanomasHigh mRNA expression in all tested melanoma cell lines but not primary melanocytes; low E-cadherin in presence of Snail [142]; inverse correlation with E-cadherin [>>130<<]; Snail confers invasive and immunosuppressive properties [143]  [130],[142],[143]Oral squamous carcinomaLow E-cadherin/high Snail expression cells more invasive; E-cadherin positive had cuboidal shape and E-cadherin negative cells were
n3:mentions
n4:11857019
Subject Item
_:vb33216193
rdf:type
n3:Context
rdf:value
mRNA expression in all tested melanoma cell lines but not primary melanocytes; low E-cadherin in presence of Snail [142]; inverse correlation with E-cadherin [130]; Snail confers invasive and immunosuppressive properties [>>143<<]  [130],[142],[143]Oral squamous carcinomaLow E-cadherin/high Snail expression cells more invasive; E-cadherin positive had cuboidal shape and E-cadherin negative cells were spindle-shaped; inverse correlation with E-cadherin [136]
n3:mentions
n4:11323412
Subject Item
_:vb33216194
rdf:type
n3:Context
rdf:value
mRNA expression in all tested melanoma cell lines but not primary melanocytes; low E-cadherin in presence of Snail [142]; inverse correlation with E-cadherin [130]; Snail confers invasive and immunosuppressive properties [143]  [>>130<<],[142],[143]Oral squamous carcinomaLow E-cadherin/high Snail expression cells more invasive; E-cadherin positive had cuboidal shape and E-cadherin negative cells were spindle-shaped; inverse correlation with E-cadherin [136]  [136]Ovarian
n3:mentions
n4:11857019
Subject Item
_:vb33216195
rdf:type
n3:Context
rdf:value
mRNA expression in all tested melanoma cell lines but not primary melanocytes; low E-cadherin in presence of Snail [142]; inverse correlation with E-cadherin [130]; Snail confers invasive and immunosuppressive properties [143]  [130],[>>142<<],[143]Oral squamous carcinomaLow E-cadherin/high Snail expression cells more invasive; E-cadherin positive had cuboidal shape and E-cadherin negative cells were spindle-shaped; inverse correlation with E-cadherin [136]  [136]Ovarian
n3:mentions
n4:19162513
Subject Item
_:vb33216196
rdf:type
n3:Context
rdf:value
expression in all tested melanoma cell lines but not primary melanocytes; low E-cadherin in presence of Snail [142]; inverse correlation with E-cadherin [130]; Snail confers invasive and immunosuppressive properties [143]  [130],[142],[>>143<<]Oral squamous carcinomaLow E-cadherin/high Snail expression cells more invasive; E-cadherin positive had cuboidal shape and E-cadherin negative cells were spindle-shaped; inverse correlation with E-cadherin [136]  [136]Ovarian
n3:mentions
n4:11323412
Subject Item
_:vb33216197
rdf:type
n3:Context
rdf:value
[143]  [130],[142],[143]Oral squamous carcinomaLow E-cadherin/high Snail expression cells more invasive; E-cadherin positive had cuboidal shape and E-cadherin negative cells were spindle-shaped; inverse correlation with E-cadherin [>>136<<]  [136]Ovarian carcinomaLess expressed than in breast carcinoma [129]; lower expression in effusions than primary tumors and solid metastases; mRNA levels not statistically different among the three; complete cytoplasmic localization in
n3:mentions
n4:11120485
Subject Item
_:vb33216198
rdf:type
n3:Context
rdf:value
[130],[142],[143]Oral squamous carcinomaLow E-cadherin/high Snail expression cells more invasive; E-cadherin positive had cuboidal shape and E-cadherin negative cells were spindle-shaped; inverse correlation with E-cadherin [136]  [>>136<<]Ovarian carcinomaLess expressed than in breast carcinoma [129]; lower expression in effusions than primary tumors and solid metastases; mRNA levels not statistically different among the three; complete cytoplasmic localization in
n3:mentions
n4:11120485
Subject Item
_:vb33216199
rdf:type
n3:Context
rdf:value
Snail expression cells more invasive; E-cadherin positive had cuboidal shape and E-cadherin negative cells were spindle-shaped; inverse correlation with E-cadherin [136]  [136]Ovarian carcinomaLess expressed than in breast carcinoma [>>129<<]; lower expression in effusions than primary tumors and solid metastases; mRNA levels not statistically different among the three; complete cytoplasmic localization in effusions [133] High E-cadherin expression correlated with
n3:mentions
n4:15742334
Subject Item
_:vb33216200
rdf:type
n3:Context
rdf:value
carcinomaLess expressed than in breast carcinoma [129]; lower expression in effusions than primary tumors and solid metastases; mRNA levels not statistically different among the three; complete cytoplasmic localization in effusions [>>133<<] High E-cadherin expression correlated with disease-free survival; MMP-2 is considered a marker of poor prognosis; Snail associated with distant metastases [129][129],[133]Pancreatic carcinomaInverse correlation with E-cadherin [130];
n3:mentions
n4:17024425
Subject Item
_:vb33216201
rdf:type
n3:Context
rdf:value
different among the three; complete cytoplasmic localization in effusions [133] High E-cadherin expression correlated with disease-free survival; MMP-2 is considered a marker of poor prognosis; Snail associated with distant metastases [>>129<<][129],[133]Pancreatic carcinomaInverse correlation with E-cadherin [130]; significantly reduced E-cadherin expression [129]; 78% of tested tissues (n = 36, ductal adenocarcinoma) showed Snail expression; Snail higher in undifferentiated
n3:mentions
n4:15742334
Subject Item
_:vb33216202
rdf:type
n3:Context
rdf:value
among the three; complete cytoplasmic localization in effusions [133] High E-cadherin expression correlated with disease-free survival; MMP-2 is considered a marker of poor prognosis; Snail associated with distant metastases [129][>>129<<],[133]Pancreatic carcinomaInverse correlation with E-cadherin [130]; significantly reduced E-cadherin expression [129]; 78% of tested tissues (n = 36, ductal adenocarcinoma) showed Snail expression; Snail higher in undifferentiated cell
n3:mentions
n4:15742334
Subject Item
_:vb33216203
rdf:type
n3:Context
rdf:value
the three; complete cytoplasmic localization in effusions [133] High E-cadherin expression correlated with disease-free survival; MMP-2 is considered a marker of poor prognosis; Snail associated with distant metastases [129][129],[>>133<<]Pancreatic carcinomaInverse correlation with E-cadherin [130]; significantly reduced E-cadherin expression [129]; 78% of tested tissues (n = 36, ductal adenocarcinoma) showed Snail expression; Snail higher in undifferentiated cell lines
n3:mentions
n4:17024425
Subject Item
_:vb33216204
rdf:type
n3:Context
rdf:value
[133] High E-cadherin expression correlated with disease-free survival; MMP-2 is considered a marker of poor prognosis; Snail associated with distant metastases [129][129],[133]Pancreatic carcinomaInverse correlation with E-cadherin [>>130<<]; significantly reduced E-cadherin expression [129]; 78% of tested tissues (n = 36, ductal adenocarcinoma) showed Snail expression; Snail higher in undifferentiated cell lines (MiaPaCa-2 and Panc-1) than differentiated (Capan-1, HPAF-2,
n3:mentions
n4:11857019
Subject Item
_:vb33216205
rdf:type
n3:Context
rdf:value
disease-free survival; MMP-2 is considered a marker of poor prognosis; Snail associated with distant metastases [129][129],[133]Pancreatic carcinomaInverse correlation with E-cadherin [130]; significantly reduced E-cadherin expression [>>129<<]; 78% of tested tissues (n = 36, ductal adenocarcinoma) showed Snail expression; Snail higher in undifferentiated cell lines (MiaPaCa-2 and Panc-1) than differentiated (Capan-1, HPAF-2, AsPC-1) [137]  [129],[130],[137]Prostate
n3:mentions
n4:15742334
Subject Item
_:vb33216206
rdf:type
n3:Context
rdf:value
reduced E-cadherin expression [129]; 78% of tested tissues (n = 36, ductal adenocarcinoma) showed Snail expression; Snail higher in undifferentiated cell lines (MiaPaCa-2 and Panc-1) than differentiated (Capan-1, HPAF-2, AsPC-1) [>>137<<]  [129],[130],[137]Prostate cancerSignificant loss of E-cadherin and syndecan 1 in high grades, along with high Snail; only nuclear localization in PC3 cell lines [151]High Snail expression correlates with high Gleason grade, increased
n3:mentions
n4:17699854
Subject Item
_:vb33216207
rdf:type
n3:Context
rdf:value
E-cadherin expression [129]; 78% of tested tissues (n = 36, ductal adenocarcinoma) showed Snail expression; Snail higher in undifferentiated cell lines (MiaPaCa-2 and Panc-1) than differentiated (Capan-1, HPAF-2, AsPC-1) [137]  [>>129<<],[130],[137]Prostate cancerSignificant loss of E-cadherin and syndecan 1 in high grades, along with high Snail; only nuclear localization in PC3 cell lines [151]High Snail expression correlates with high Gleason grade, increased
n3:mentions
n4:15742334
Subject Item
_:vb33216208
rdf:type
n3:Context
rdf:value
E-cadherin expression [129]; 78% of tested tissues (n = 36, ductal adenocarcinoma) showed Snail expression; Snail higher in undifferentiated cell lines (MiaPaCa-2 and Panc-1) than differentiated (Capan-1, HPAF-2, AsPC-1) [137]  [129],[>>130<<],[137]Prostate cancerSignificant loss of E-cadherin and syndecan 1 in high grades, along with high Snail; only nuclear localization in PC3 cell lines [151]High Snail expression correlates with high Gleason grade, increased malignancy
n3:mentions
n4:11857019
Subject Item
_:vb33216209
rdf:type
n3:Context
rdf:value
expression [129]; 78% of tested tissues (n = 36, ductal adenocarcinoma) showed Snail expression; Snail higher in undifferentiated cell lines (MiaPaCa-2 and Panc-1) than differentiated (Capan-1, HPAF-2, AsPC-1) [137]  [129],[130],[>>137<<]Prostate cancerSignificant loss of E-cadherin and syndecan 1 in high grades, along with high Snail; only nuclear localization in PC3 cell lines [151]High Snail expression correlates with high Gleason grade, increased malignancy [151]
n3:mentions
n4:17699854
Subject Item
_:vb33216210
rdf:type
n3:Context
rdf:value
and Panc-1) than differentiated (Capan-1, HPAF-2, AsPC-1) [137]  [129],[130],[137]Prostate cancerSignificant loss of E-cadherin and syndecan 1 in high grades, along with high Snail; only nuclear localization in PC3 cell lines [>>151<<]High Snail expression correlates with high Gleason grade, increased malignancy [151] [151]Synovial sarcomaSnail mRNA found in all cases tested (n = 20), but E-cadherin mutations appear to be more important than Snail expression [144]
n3:mentions
n4:9221815
Subject Item
_:vb33216211
rdf:type
n3:Context
rdf:value
cancerSignificant loss of E-cadherin and syndecan 1 in high grades, along with high Snail; only nuclear localization in PC3 cell lines [151]High Snail expression correlates with high Gleason grade, increased malignancy [>>151<<] [151]Synovial sarcomaSnail mRNA found in all cases tested (n = 20), but E-cadherin mutations appear to be more important than Snail expression [144]  [144]Breast
n3:mentions
n4:9221815
Subject Item
_:vb33216212
rdf:type
n3:Context
rdf:value
cancerSignificant loss of E-cadherin and syndecan 1 in high grades, along with high Snail; only nuclear localization in PC3 cell lines [151]High Snail expression correlates with high Gleason grade, increased malignancy [151] [>>151<<]Synovial sarcomaSnail mRNA found in all cases tested (n = 20), but E-cadherin mutations appear to be more important than Snail expression [144]  [144]Breast
n3:mentions
n4:9221815
Subject Item
_:vb33216213
rdf:type
n3:Context
rdf:value
[151]High Snail expression correlates with high Gleason grade, increased malignancy [151] [151]Synovial sarcomaSnail mRNA found in all cases tested (n = 20), but E-cadherin mutations appear to be more important than Snail expression [>>144<<]  [144]Breast
n3:mentions
n4:19249678
Subject Item
_:vb33216214
rdf:type
n3:Context
rdf:value
Snail expression correlates with high Gleason grade, increased malignancy [151] [151]Synovial sarcomaSnail mRNA found in all cases tested (n = 20), but E-cadherin mutations appear to be more important than Snail expression [144]  [>>144<<]Breast
n3:mentions
n4:19249678
Subject Item
_:vb33216215
rdf:type
n3:Context
rdf:value
Assigned histological grades, with three being the highest, correlate with prognosis [>>126<<]. Breast carcinomas can give rise to malignant pleural effusions, and typical survival rates at that point are a matter of months [127].
n3:mentions
n4:1757079
Subject Item
_:vb33216216
rdf:type
n3:Context
rdf:value
Breast carcinomas can give rise to malignant pleural effusions, and typical survival rates at that point are a matter of months [>>127<<].
n3:mentions
n4:7992584
Subject Item
_:vb33216217
rdf:type
n3:Context
rdf:value
Of 17 patients, Snail1 was expressed in 47% of IDCs, and its expression correlated with lymph node metastases and high histologic grades [>>128<<]. E-cadherin and Snail1 expression levels are inversely related, and high expression levels of Snail1 correlate with shorter effusion-free, disease-free, and overall survival rates (n = 16) [129]. As such, Snail1 has prognostic
n3:mentions
n4:12082640
Subject Item
_:vb33216218
rdf:type
n3:Context
rdf:value
E-cadherin and Snail1 expression levels are inversely related, and high expression levels of Snail1 correlate with shorter effusion-free, disease-free, and overall survival rates (n = 16) [>>129<<]. As such, Snail1 has prognostic significance as a marker of IDC malignancy [128].
n3:mentions
n4:15742334
Subject Item
_:vb33216219
rdf:type
n3:Context
rdf:value
As such, Snail1 has prognostic significance as a marker of IDC malignancy [>>128<<].
n3:mentions
n4:12082640
Subject Item
_:vb33216220
rdf:type
n3:Context
rdf:value
Snail1 mRNA and protein levels are inversely correlated with E-cadherin in hepatocellular carcinoma (HCC) [>>130<<]. Snail1 overexpression, which in one study included 23% of cases (n = 47), is associated with portal vein invasion, metastasis, and poor differentiation.
n3:mentions
n4:11857019
Subject Item
_:vb33216221
rdf:type
n3:Context
rdf:value
Furthermore, Snail1 expression correlates with a poor prognosis in recurrence-free survival and, thus, is considered a potential risk factor for early recurrence [>>131<<],[132].
n3:mentions
n4:15668718
Subject Item
_:vb33216222
rdf:type
n3:Context
rdf:value
Furthermore, Snail1 expression correlates with a poor prognosis in recurrence-free survival and, thus, is considered a potential risk factor for early recurrence [131],[>>132<<].
n3:mentions
n4:21494073
Subject Item
_:vb33216223
rdf:type
n3:Context
rdf:value
Overall, Snail1 expression is lower in ovarian carcinoma than in breast carcinoma, though its expression is still associated with distant metastases [>>129<<]. Expression is higher among primary tumors and metastases than effusions, and effusions show complete cytoplasmic localization of Snail1 [133].
n3:mentions
n4:15742334
Subject Item
_:vb33216224
rdf:type
n3:Context
rdf:value
Expression is higher among primary tumors and metastases than effusions, and effusions show complete cytoplasmic localization of Snail1 [>>133<<]. Snail1 represses E-cadherin and upregulates MMPs, and E-cadherin expression correlates with disease-free survival while MMP-2 is considered a marker of poor prognosis [129].
n3:mentions
n4:17024425
Subject Item
_:vb33216225
rdf:type
n3:Context
rdf:value
Snail1 represses E-cadherin and upregulates MMPs, and E-cadherin expression correlates with disease-free survival while MMP-2 is considered a marker of poor prognosis [>>129<<].
n3:mentions
n4:15742334
Subject Item
_:vb33216226
rdf:type
n3:Context
rdf:value
E-cadherin expression is drastically reduced in gastric carcinoma, and Snail1 expression levels once again share an inverse relationship with E-cadherin expression levels [>>129<<]. Snail1 expression levels are more comparable to breast than ovarian carcinomas, and Snail1 expression is still higher in diffuse rather than intestinal varieties of gastric carcinomas [129],[134].
n3:mentions
n4:15742334
Subject Item
_:vb33216227
rdf:type
n3:Context
rdf:value
Snail1 expression levels are more comparable to breast than ovarian carcinomas, and Snail1 expression is still higher in diffuse rather than intestinal varieties of gastric carcinomas [>>129<<],[134]. Elevated Snail1 expression increases cells’ capacities for migration and invasion. Overexpression correlates with tumor size, depth of invasion, and lymph node metastasis. Shortened survival rates are also directly related to
n3:mentions
n4:15742334
Subject Item
_:vb33216228
rdf:type
n3:Context
rdf:value
Snail1 expression levels are more comparable to breast than ovarian carcinomas, and Snail1 expression is still higher in diffuse rather than intestinal varieties of gastric carcinomas [129],[>>134<<]. Elevated Snail1 expression increases cells’ capacities for migration and invasion. Overexpression correlates with tumor size, depth of invasion, and lymph node metastasis. Shortened survival rates are also directly related to Snail1
n3:mentions
n4:12414534
Subject Item
_:vb33216229
rdf:type
n3:Context
rdf:value
Shortened survival rates are also directly related to Snail1 overexpression, and Snail1 is considered a predictor of poor prognosis [>>135<<].
n3:mentions
n4:23151184
Subject Item
_:vb33216230
rdf:type
n3:Context
rdf:value
This is a typical sign of EMT, and it shows Snail1’s repression of E-cadherin [>>136<<].
n3:mentions
n4:11120485
Subject Item
_:vb33216231
rdf:type
n3:Context
rdf:value
Pancreatic carcinoma tissues show significantly reduced E-cadherin levels and relatively high Snail1 expression [>>129<<]. In one study, 78% (n = 36) of ductal adenocarcinoma tissues expressed Snail1, and Snail1 expression is higher in undifferentiated cell lines than in differentiated ones [137].
n3:mentions
n4:15742334
Subject Item
_:vb33216232
rdf:type
n3:Context
rdf:value
In one study, 78% (n = 36) of ductal adenocarcinoma tissues expressed Snail1, and Snail1 expression is higher in undifferentiated cell lines than in differentiated ones [>>137<<].
n3:mentions
n4:17699854
Subject Item
_:vb33216233
rdf:type
n3:Context
rdf:value
Colorectal cancer (CRC) begins in gland cells that line the colon and rectum, and it is one of the most commonly newly diagnosed cancers and a leading cause of cancer-related deaths [>>138<<]. Snail1 expression is again inversely correlated to E-cadherin expression in CRC, and the expression level of Snail1 is quite high in CRC (78%, n = 59) [130],[139].
n3:mentions
n4:19474385
Subject Item
_:vb33216234
rdf:type
n3:Context
rdf:value
Snail1 expression is again inversely correlated to E-cadherin expression in CRC, and the expression level of Snail1 is quite high in CRC (78%, n = 59) [>>130<<],[139]. Interestingly, the mean age of the Snail1-positive group was nine years older than the Snail1-negative group in one study, with a standard deviation of 12.7 years (58.9 years vs. 49.8 years, n = 59) [139]. In another study, Snail1
n3:mentions
n4:11857019
Subject Item
_:vb33216235
rdf:type
n3:Context
rdf:value
Snail1 expression is again inversely correlated to E-cadherin expression in CRC, and the expression level of Snail1 is quite high in CRC (78%, n = 59) [130],[>>139<<]. Interestingly, the mean age of the Snail1-positive group was nine years older than the Snail1-negative group in one study, with a standard deviation of 12.7 years (58.9 years vs. 49.8 years, n = 59) [139]. In another study, Snail1
n3:mentions
n4:15712635
Subject Item
_:vb33216236
rdf:type
n3:Context
rdf:value
49.8 years, n = 59) [>>139<<]. In another study, Snail1 expression was detected by Western blot in all tested CRC lines, and its expression increased both migratory and invasive properties.
n3:mentions
n4:15712635
Subject Item
_:vb33216237
rdf:type
n3:Context
rdf:value
Additionally, Snail1 expression led to a stem-cell like phenotype and spindle shape, as usually accompanies the loss of E-cadherin [>>140<<]. Snail1 expression also increased with the stage of the tumors, with 15/23 stage III expressing Snail1 and 6/6 of stage IV. The significantly higher rate of metastasis associated with Snail1 expression suggests that Snail1’s presence
n3:mentions
n4:23342249
Subject Item
_:vb33216238
rdf:type
n3:Context
rdf:value
The significantly higher rate of metastasis associated with Snail1 expression suggests that Snail1’s presence indicates a high risk of distant metastases [>>139<<],[140].
n3:mentions
n4:15712635
Subject Item
_:vb33216239
rdf:type
n3:Context
rdf:value
The significantly higher rate of metastasis associated with Snail1 expression suggests that Snail1’s presence indicates a high risk of distant metastases [139],[>>140<<].
n3:mentions
n4:23342249
Subject Item
_:vb33216240
rdf:type
n3:Context
rdf:value
However, Snail1 expression increased in node-positive compared to node-negative tumors, and Snail1’s presence lowered the three-year progression free survival rate to only 15% [>>141<<]. Since Snail1 expression is closely linked with tumor recurrence, its elevation is considered a significant prognostic factor [141],[142].
n3:mentions
n4:20809941
Subject Item
_:vb33216241
rdf:type
n3:Context
rdf:value
Since Snail1 expression is closely linked with tumor recurrence, its elevation is considered a significant prognostic factor [>>141<<],[142].
n3:mentions
n4:20809941
Subject Item
_:vb33216242
rdf:type
n3:Context
rdf:value
Since Snail1 expression is closely linked with tumor recurrence, its elevation is considered a significant prognostic factor [141],[>>142<<].
n3:mentions
n4:19162513
Subject Item
_:vb33216243
rdf:type
n3:Context
rdf:value
By contrast, no Snail1 mRNA was detected in primary melanocytes [>>143<<]. Snail1 expression confers both invasive and immunosuppressive properties in melanoma [144].
n3:mentions
n4:11323412
Subject Item
_:vb33216244
rdf:type
n3:Context
rdf:value
Snail1 expression confers both invasive and immunosuppressive properties in melanoma [>>144<<].
n3:mentions
n4:19249678
Subject Item
_:vb33216245
rdf:type
n3:Context
rdf:value
In this case, mutations of the CDH1 gene, which encodes E-cadherin, seem to be more influential than the presence of Snail1 [>>145<<].
n3:mentions
n4:11733362
Subject Item
_:vb33216246
rdf:type
n3:Context
rdf:value
Prostate cancer is the second most commonly diagnosed cancer in men worldwide, with estimates of over 900,000 new cases per year [>>146<<]. A Gleason grade, which describes the two most important histopathological patterns of that patient’s cancer, accompanies a diagnosis.
n3:mentions
n4:21296855
Subject Item
_:vb33216247
rdf:type
n3:Context
rdf:value
The grade ranges from 2-10 with a higher score meaning less differentiated [>>147<<]. Significant losses of E-cadherin and syndecan 1, two proteins involved in cellular adhesion, have been observed in malignant prostate cancer [148],[149]. Both promoters contain E-boxes, so Snail1 can directly bind and repress them
n3:mentions
n4:22212079
Subject Item
_:vb33216248
rdf:type
n3:Context
rdf:value
Significant losses of E-cadherin and syndecan 1, two proteins involved in cellular adhesion, have been observed in malignant prostate cancer [>>148<<],[149]. Both promoters contain E-boxes, so Snail1 can directly bind and repress them [150],[151]. The presence of E-boxes may explain the inverse correlation between E-cadherin/syndecan 1 and Snail1 expression levels. Poblete et al. found
n3:mentions
n4:14613514
Subject Item
_:vb33216249
rdf:type
n3:Context
rdf:value
Significant losses of E-cadherin and syndecan 1, two proteins involved in cellular adhesion, have been observed in malignant prostate cancer [148],[>>149<<]. Both promoters contain E-boxes, so Snail1 can directly bind and repress them [150],[151]. The presence of E-boxes may explain the inverse correlation between E-cadherin/syndecan 1 and Snail1 expression levels. Poblete et al. found that
n3:mentions
n4:22349653
Subject Item
_:vb33216250
rdf:type
n3:Context
rdf:value
Both promoters contain E-boxes, so Snail1 can directly bind and repress them [>>150<<],[151]. The presence of E-boxes may explain the inverse correlation between E-cadherin/syndecan 1 and Snail1 expression levels. Poblete et al. found that high Snail1 expression correlated with a high Gleason grade and increased malignancy.
n3:mentions
n4:23076049
Subject Item
_:vb33216251
rdf:type
n3:Context
rdf:value
Both promoters contain E-boxes, so Snail1 can directly bind and repress them [150],[>>151<<]. The presence of E-boxes may explain the inverse correlation between E-cadherin/syndecan 1 and Snail1 expression levels. Poblete et al. found that high Snail1 expression correlated with a high Gleason grade and increased malignancy.
n3:mentions
n4:9221815
Subject Item
_:vb33216252
rdf:type
n3:Context
rdf:value
By contrast, Snail1 had both cytoplasmic and nuclear localization in less malignant cell lines [>>152<<].
n3:mentions
n4:24424718
Subject Item
_:vb33216253
rdf:type
n3:Context
rdf:value
Cervical cancer is one of the most common malignancies in women worldwide [>>138<<]. Chen et al. found Snail1 expressed in 94% of samples (n = 70), and the elevated expression of Snail1 correlated with late FIGO stage, lymph node metastasis, and poor differentiation [153].
n3:mentions
n4:19474385
Subject Item
_:vb33216254
rdf:type
n3:Context
rdf:value
Chen et al. found Snail1 expressed in 94% of samples (n = 70), and the elevated expression of Snail1 correlated with late FIGO stage, lymph node metastasis, and poor differentiation [>>153<<].
n3:mentions
n4:23791009
Subject Item
_:vb33216255
rdf:type
n2:Section
dc:title
snail1 and cancer stem cells
n2:contains
_:vb33216264 _:vb33216265 _:vb33216266 _:vb33216267 _:vb33216268 _:vb33216269 _:vb33216256 _:vb33216257 _:vb33216258 _:vb33216259 _:vb33216260 _:vb33216261 _:vb33216262 _:vb33216263
Subject Item
_:vb33216256
rdf:type
n3:Context
rdf:value
Cancer stem cells (CSCs), or tumor-initiating cells, are subpopulations within tumors that possess self-renewing capabilities [>>154<<]. In breast tissue, for example, populations with a CD44high/CD24low phenotype have a higher tumor-initiating capacity than do their CD44low/CD24high counterparts within the same tumors [155]. CSCs are also associated with
n3:mentions
n4:11689955
Subject Item
_:vb33216257
rdf:type
n3:Context
rdf:value
In breast tissue, for example, populations with a CD44high/CD24low phenotype have a higher tumor-initiating capacity than do their CD44low/CD24high counterparts within the same tumors [>>155<<]. CSCs are also associated with chemoresistance, relapse, and metastasis [156].
n3:mentions
n4:12629218
Subject Item
_:vb33216258
rdf:type
n3:Context
rdf:value
CSCs are also associated with chemoresistance, relapse, and metastasis [>>156<<].
n3:mentions
n4:15100335
Subject Item
_:vb33216259
rdf:type
n3:Context
rdf:value
Mani et al. reported that EMT could induce stem-like properties in non-cancerous mammary epithelial cells [>>14<<]. The CD44high/CD24low phenotype correlates with both breast CSCs and normal mammary stem cells, and both Snail1- and Twist-induced EMTs stimulated this same phenotype in nontumorigenic human mammary epithelial cells (HMLEs).
n3:mentions
n4:18485877
Subject Item
_:vb33216260
rdf:type
n3:Context
rdf:value
Furthermore, these CD44high/CD24low cells exhibited a decrease of E-cadherin expression along with elevated fibronectin, vimentin, Snail1, and Twist, as measured by RT-PCR [>>14<<]. Thus, EMT promotes self-renewal capabilities and the stem-like phenotype.
n3:mentions
n4:18485877
Subject Item
_:vb33216261
rdf:type
n3:Context
rdf:value
Given that Snail1 induced EMT and a stem-like phenotype in human colorectal cancer cells (as mentioned in “Colorectal Carcinoma,” above), Zhou et al. examined human pancreatic cancer cells and reached similar conclusions [>>15<<]. Epithelial BxPC-3 cells were compared with more morphologically diverse Panc-1 cells, and the comparison identified Panc-1 cells, which had higher Snail1 expression and were more poorly differentiated than BxPC-3 cells, as CSChigh with
n3:mentions
n4:24489910
Subject Item
_:vb33216262
rdf:type
n3:Context
rdf:value
compared with more morphologically diverse Panc-1 cells, and the comparison identified Panc-1 cells, which had higher Snail1 expression and were more poorly differentiated than BxPC-3 cells, as CSChigh with a larger ALDHhigh population [>>15<<]. Stem cells’ pluripotent capabilities are maintained in part by the polycomb complex protein BMI-1 (Bmi-1), homeobox protein Nanog, sex-determining region Y-box 2 (Sox2), and octamer-binding transcription factor 4 (Oct4) [157]–[159].
n3:mentions
n4:24489910
Subject Item
_:vb33216263
rdf:type
n3:Context
rdf:value
Stem cells’ pluripotent capabilities are maintained in part by the polycomb complex protein BMI-1 (Bmi-1), homeobox protein Nanog, sex-determining region Y-box 2 (Sox2), and octamer-binding transcription factor 4 (Oct4) [>>157<<]–[159]. Snail1 silencing resulted in a decrease in ALDH, Sox-2, Oct-4, and invasive properties. Following Snail1 knockdown, E-cadherin expression increased as vimentin and ZEB1 expressions both decreased. Without Snail1, the Panc-1 cells
n3:mentions
n4:16904174
Subject Item
_:vb33216264
rdf:type
n3:Context
rdf:value
Stem cells’ pluripotent capabilities are maintained in part by the polycomb complex protein BMI-1 (Bmi-1), homeobox protein Nanog, sex-determining region Y-box 2 (Sox2), and octamer-binding transcription factor 4 (Oct4) [157]–[>>159<<]. Snail1 silencing resulted in a decrease in ALDH, Sox-2, Oct-4, and invasive properties. Following Snail1 knockdown, E-cadherin expression increased as vimentin and ZEB1 expressions both decreased. Without Snail1, the Panc-1 cells
n3:mentions
n4:23333380
Subject Item
_:vb33216265
rdf:type
n3:Context
rdf:value
Without Snail1, the Panc-1 cells underwent MET and consequently lost their stem-like phenotype [>>15<<].
n3:mentions
n4:24489910
Subject Item
_:vb33216266
rdf:type
n3:Context
rdf:value
In a similar study of non-small cell lung cancer, Wang et al. compared ciplatin-resistant A549 cells with their A549 counterparts [>>16<<]. A549/CDDP cells showed increased expression levels of Nanog, Oct4, and Bmi-1, as detected by Western blot.
n3:mentions
n4:24333218
Subject Item
_:vb33216267
rdf:type
n3:Context
rdf:value
E-cadherin increased as vimentin decreased, and the cells became more responsive to cisplatin [>>16<<]. Since β-catenin had effects on the system comparable to active Snail1, an antagonist of the PI3K/Akt pathway was introduced, and this resulted in a decrease in β-catenin, Snail1, Nanog, migration, invasiveness, and mammosphere-forming
n3:mentions
n4:24333218
Subject Item
_:vb33216268
rdf:type
n3:Context
rdf:value
had effects on the system comparable to active Snail1, an antagonist of the PI3K/Akt pathway was introduced, and this resulted in a decrease in β-catenin, Snail1, Nanog, migration, invasiveness, and mammosphere-forming ability [>>16<<]. Thus, the Akt pathway plays a crucial role in stem-like phenotype in lung cancer cells.
n3:mentions
n4:24333218
Subject Item
_:vb33216269
rdf:type
n3:Context
rdf:value
Poor differentiation, sphere-forming capacity, self-renewal, and typical markers such as ALDH and CD44, among other properties, characterize the stem-like phenotype [>>15<<]. Clearly, Snail1 overexpression is associated with all of these properties. After Snail1 induces EMT, cells adopt a mesenchymal morphology, become more invasive, increase migratory capacity, and express a stem-like phenotype.
n3:mentions
n4:24489910
Subject Item
_:vb33216270
rdf:type
n2:Section
dc:title
regulation of emt, in part, by snail1
n2:contains
_:vb33216272 _:vb33216273 _:vb33216274 _:vb33216275 _:vb33216271
Subject Item
_:vb33216271
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Snail1 drives EMT primarily through the direct repression of E-cadherin [>>53<<]. Other targets that contribute to Snail1’s EMT program were detailed above (See Section “Snail1’s Targets”, Table 2).
n3:mentions
n4:2419126
Subject Item
_:vb33216272
rdf:type
n3:Context
rdf:value
Zhu et al. have examined the relationship between the expression of the Response Gene to Complement-32 (RGC-32) and TGF-β-mediated EMT [>>160<<]. RGC-32 is over-expressed in many cancers and correlates with the lower level of expression of E-cadherin in pancreatic cancer.
n3:mentions
n4:22458379
Subject Item
_:vb33216273
rdf:type
n3:Context
rdf:value
Huang et al. investigated the expression level of Notch1 in lung adenocarcinoma and its relationship to metastasis [>>161<<]. They found that lung tumors express low levels of Notch1 and were associated with advanced clinical stage and lymph node metastasis.
n3:mentions
n4:24423157
Subject Item
_:vb33216274
rdf:type
n3:Context
rdf:value
Notch1 protects Snail1 from degradation by preventing GSK-3β-mediated phosphorylation via LOXL2 oxidation, as detailed above [>>18<<].
n3:mentions
n4:16096638
Subject Item
_:vb33216275
rdf:type
n3:Context
rdf:value
The relationship between the expression of cyclooxegnase-2 (Cox-2) and the downregulation of E-cadherin and its relationship to the EMT phenotype was reported by Fujii et al. [>>162<<]. These investigators examined Head and Neck Squamous Cell Carcinoma (HNSCC) cells and treated the cells with Cox-2 inhibitors (Celecoxib, NS-398 and SC-791) and examined EMT-associated gene products by quantitative real-time PCR and
n3:mentions
n4:24887090
Subject Item
_:vb33216276
rdf:type
n2:Section
dc:title
snail1 regulates chemo and immune resistance
n2:contains
_:vb33216277 _:vb33216278 _:vb33216279 _:vb33216284 _:vb33216285 _:vb33216286 _:vb33216287 _:vb33216280 _:vb33216281 _:vb33216282 _:vb33216283
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Tumor-specific T cell responses also intensify as a result of this knockdown [>>144<<]. Similarly, shRNA treatment induces apoptosis in adriamycin-resistant melanoma cells, and Snail1 reduction leads to cisplatin sensitization in lung adenocarcinoma, head and neck squamous, and ovarian cancers [13],[163]–[165].
n3:mentions
n4:19249678
Subject Item
_:vb33216278
rdf:type
n3:Context
rdf:value
Similarly, shRNA treatment induces apoptosis in adriamycin-resistant melanoma cells, and Snail1 reduction leads to cisplatin sensitization in lung adenocarcinoma, head and neck squamous, and ovarian cancers [>>13<<],[163]–[165].
n3:mentions
n4:15314165
Subject Item
_:vb33216279
rdf:type
n3:Context
rdf:value
Similarly, shRNA treatment induces apoptosis in adriamycin-resistant melanoma cells, and Snail1 reduction leads to cisplatin sensitization in lung adenocarcinoma, head and neck squamous, and ovarian cancers [13],[>>163<<]–[165]. Additionally, Snail1 has been implicated in resistance to radiation and paclitaxel in ovarian cancer cell lines as well as protection against 5-fluorouracil and gemcitabine in Panc-1 cells [166],[167].
n3:mentions
n4:18372076
Subject Item
_:vb33216280
rdf:type
n3:Context
rdf:value
Similarly, shRNA treatment induces apoptosis in adriamycin-resistant melanoma cells, and Snail1 reduction leads to cisplatin sensitization in lung adenocarcinoma, head and neck squamous, and ovarian cancers [13],[163]–[>>165<<]. Additionally, Snail1 has been implicated in resistance to radiation and paclitaxel in ovarian cancer cell lines as well as protection against 5-fluorouracil and gemcitabine in Panc-1 cells [166],[167].
n3:mentions
n4:22429801
Subject Item
_:vb33216281
rdf:type
n3:Context
rdf:value
Additionally, Snail1 has been implicated in resistance to radiation and paclitaxel in ovarian cancer cell lines as well as protection against 5-fluorouracil and gemcitabine in Panc-1 cells [>>166<<],[167].
n3:mentions
n4:19544473
Subject Item
_:vb33216282
rdf:type
n3:Context
rdf:value
Additionally, Snail1 has been implicated in resistance to radiation and paclitaxel in ovarian cancer cell lines as well as protection against 5-fluorouracil and gemcitabine in Panc-1 cells [166],[>>167<<].
n3:mentions
n4:17583745
Subject Item
_:vb33216283
rdf:type
n3:Context
rdf:value
Snail1’s activation of MAPK and PI3K survival pathways leads to resistance to serum depletion and TNF-α [>>168<<]. The repression of NF-κB and therefore Snail1, its downstream target, sensitizes tumor cells to cisplatin and TNF-related apoptosis-inducing ligand (TRAIL)-induced apoptosis. Treatments with nitric oxide, the proteasome inhibitor
n3:mentions
n4:15155580
Subject Item
_:vb33216284
rdf:type
n3:Context
rdf:value
These treatments have proven effective in prostate cancers and B-Non-Hodgkin’s Lymphoma, respectively [>>168<<]–[171].
n3:mentions
n4:15155580
Subject Item
_:vb33216285
rdf:type
n3:Context
rdf:value
These treatments have proven effective in prostate cancers and B-Non-Hodgkin’s Lymphoma, respectively [168]–[>>171<<].
n3:mentions
n4:21133714
Subject Item
_:vb33216286
rdf:type
n3:Context
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Hence, tumor cells’ resistance to CTL is mediated by EMT-induced activation of autophagy-dependent mechanisms [>>172<<],[173].
n3:mentions
n4:23635487
Subject Item
_:vb33216287
rdf:type
n3:Context
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Hence, tumor cells’ resistance to CTL is mediated by EMT-induced activation of autophagy-dependent mechanisms [172],[>>173<<].
n3:mentions
n4:23436798
Subject Item
_:vb33216288
rdf:type
n2:Section
dc:title
chemical inhibitors targeting snail1
n2:contains
_:vb33216292 _:vb33216293 _:vb33216294 _:vb33216295 _:vb33216289 _:vb33216290 _:vb33216291 _:vb33216300 _:vb33216301 _:vb33216302 _:vb33216303 _:vb33216296 _:vb33216297 _:vb33216298 _:vb33216299 _:vb33216308 _:vb33216309 _:vb33216310 _:vb33216311 _:vb33216304 _:vb33216305 _:vb33216306 _:vb33216307
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A) GN 25 and GN 29 [>>175<<]B) Co(III)-Ebox [176]C) Tranylcypromine [183]D) Trichostatin A [184]E) Pargyline [185]F) LBH589 [186] and G) Entinostat [187].
n3:mentions
n4:20531295
Subject Item
_:vb33216290
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A) GN 25 and GN 29 [175]B) Co(III)-Ebox [>>176<<]C) Tranylcypromine [183]D) Trichostatin A [184]E) Pargyline [185]F) LBH589 [186] and G) Entinostat [187].
n3:mentions
n4:22393397
Subject Item
_:vb33216291
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A) GN 25 and GN 29 [175]B) Co(III)-Ebox [176]C) Tranylcypromine [>>183<<]D) Trichostatin A [184]E) Pargyline [185]F) LBH589 [186] and G) Entinostat [187].
n3:mentions
n4:18039463
Subject Item
_:vb33216292
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NameInhibitsEffectKnown limitationsReferenceGN25, GN29Snail/p53 interactionReduced proliferation, tumor progression; increased tumor regressionOnly effective in K-Ras activated cancer cells and on wild-type p53[>>174<<],[175]Co(III)-EboxSnail/E-cadherin interactionIncreased E-cadherin expression [176]TranylcypromineLSD1/LSD2Decreased Snail’s effects on EMT markers [177]Trichostatin AHDAC1/HDAC2Reversed EMT marker expression [177]PargylineLSD1Abrogated
n3:mentions
n4:19347028
Subject Item
_:vb33216293
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NameInhibitsEffectKnown limitationsReferenceGN25, GN29Snail/p53 interactionReduced proliferation, tumor progression; increased tumor regressionOnly effective in K-Ras activated cancer cells and on wild-type p53[174],[>>175<<]Co(III)-EboxSnail/E-cadherin interactionIncreased E-cadherin expression [176]TranylcypromineLSD1/LSD2Decreased Snail’s effects on EMT markers [177]Trichostatin AHDAC1/HDAC2Reversed EMT marker expression [177]PargylineLSD1Abrogated
n3:mentions
n4:20531295
Subject Item
_:vb33216294
rdf:type
n3:Context
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interactionReduced proliferation, tumor progression; increased tumor regressionOnly effective in K-Ras activated cancer cells and on wild-type p53[174],[175]Co(III)-EboxSnail/E-cadherin interactionIncreased E-cadherin expression [>>176<<]TranylcypromineLSD1/LSD2Decreased Snail’s effects on EMT markers [177]Trichostatin AHDAC1/HDAC2Reversed EMT marker expression [177]PargylineLSD1Abrogated Snail-induced EMT [177]LBH589HDACAbrogated Snail-induced EMT
n3:mentions
n4:22393397
Subject Item
_:vb33216295
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regressionOnly effective in K-Ras activated cancer cells and on wild-type p53[174],[175]Co(III)-EboxSnail/E-cadherin interactionIncreased E-cadherin expression [176]TranylcypromineLSD1/LSD2Decreased Snail’s effects on EMT markers [>>177<<]Trichostatin AHDAC1/HDAC2Reversed EMT marker expression [177]PargylineLSD1Abrogated Snail-induced EMT [177]LBH589HDACAbrogated Snail-induced EMT [177]EntinostatHDACIncreased E-cadherin and cytokeratin 18 expression, Decreased Twist,
n3:mentions
n4:24360956
Subject Item
_:vb33216296
rdf:type
n3:Context
rdf:value
and on wild-type p53[174],[175]Co(III)-EboxSnail/E-cadherin interactionIncreased E-cadherin expression [176]TranylcypromineLSD1/LSD2Decreased Snail’s effects on EMT markers [177]Trichostatin AHDAC1/HDAC2Reversed EMT marker expression [>>177<<]PargylineLSD1Abrogated Snail-induced EMT [177]LBH589HDACAbrogated Snail-induced EMT [177]EntinostatHDACIncreased E-cadherin and cytokeratin 18 expression, Decreased Twist, Snail, vimentin, N-cadherin; encouraged epithelial morphology;
n3:mentions
n4:24360956
Subject Item
_:vb33216297
rdf:type
n3:Context
rdf:value
interactionIncreased E-cadherin expression [176]TranylcypromineLSD1/LSD2Decreased Snail’s effects on EMT markers [177]Trichostatin AHDAC1/HDAC2Reversed EMT marker expression [177]PargylineLSD1Abrogated Snail-induced EMT [>>177<<]LBH589HDACAbrogated Snail-induced EMT [177]EntinostatHDACIncreased E-cadherin and cytokeratin 18 expression, Decreased Twist, Snail, vimentin, N-cadherin; encouraged epithelial morphology; decreased cell migration
n3:mentions
n4:24360956
Subject Item
_:vb33216298
rdf:type
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expression [176]TranylcypromineLSD1/LSD2Decreased Snail’s effects on EMT markers [177]Trichostatin AHDAC1/HDAC2Reversed EMT marker expression [177]PargylineLSD1Abrogated Snail-induced EMT [177]LBH589HDACAbrogated Snail-induced EMT [>>177<<]EntinostatHDACIncreased E-cadherin and cytokeratin 18 expression, Decreased Twist, Snail, vimentin, N-cadherin; encouraged epithelial morphology; decreased cell migration
n3:mentions
n4:24360956
Subject Item
_:vb33216299
rdf:type
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EMT [177]LBH589HDACAbrogated Snail-induced EMT [177]EntinostatHDACIncreased E-cadherin and cytokeratin 18 expression, Decreased Twist, Snail, vimentin, N-cadherin; encouraged epithelial morphology; decreased cell migration [>>178<<
n3:mentions
n4:24305977
Subject Item
_:vb33216300
rdf:type
n3:Context
rdf:value
K-Ras-induced Snail1 represses p53, a tumor suppressor encoded by the TP53 gene, by binding directly and inducing exocytosis [>>174<<]. Lee et al. have developed two chemical inhibitors, GN25 and GN29, which prevent this binding and thereby protect p53 and its downstream targets, like p21, from Snail1 [175].
n3:mentions
n4:19347028
Subject Item
_:vb33216301
rdf:type
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Lee et al. have developed two chemical inhibitors, GN25 and GN29, which prevent this binding and thereby protect p53 and its downstream targets, like p21, from Snail1 [>>175<<]. In K-Ras-mutated A549, HCT116, and MKN45 cell lines, both inhibitors were shown to be effective, though GN25 was more so. GN25 and GN29 also inhibited proliferation with more success than did Nutlin-3, which interferes with p53/MDM2
n3:mentions
n4:20531295
Subject Item
_:vb33216302
rdf:type
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Additionally, this mechanism is effective exclusively in K-Ras-activated cancer cells, not N-Ras/Myc-transformed cells [>>175<<].
n3:mentions
n4:20531295
Subject Item
_:vb33216303
rdf:type
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Harney et al. reported that Co(III)-Ebox, a Co(III) Schiff base complex, interferes with Snail1/E-cadherin binding and thereby inhibits Snail’s repression of the E-cadherin promoter in breast cancer cells [>>176<<]. Both the zinc finger region and ability to bind to E-box sequences are critical to this mechanism.
n3:mentions
n4:22393397
Subject Item
_:vb33216304
rdf:type
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While Co(III)-Ebox decreased DNA binding, it did not have an effect on Snail1 protein levels in this study [>>176<<].
n3:mentions
n4:22393397
Subject Item
_:vb33216305
rdf:type
n3:Context
rdf:value
Javaid et al. showed that LSD1, LSD2, and HDAC inhibitors are also effective in countering Snail1-induced EMT [>>177<<]. In breast epithelial cells, the LSD1/LSD2 inhibitor Tranylcypromine (TCP) and the HDAC class I and II inhibitor Trichostatin A (TSA) individually decreased Snail1’s effects on epithelial and mesenchymal markers.
n3:mentions
n4:24360956
Subject Item
_:vb33216306
rdf:type
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The LSD1 inhibitor Pargyline and the HDAC1, HDAC2, HDAC3, and HDAC6 inhibitor LBH589 were also successful in inhibiting Snail1-induced EMT [>>177<<].
n3:mentions
n4:24360956
Subject Item
_:vb33216307
rdf:type
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Furthermore, Shah et al. found that the HDAC inhibitor entinostat (ENT) reverses Snail1-induced EMT in breast cancer cells [>>178<<]. Treating MDA-MB-231 and Hs578T cells with ENT caused an increase in E-cadherin transcription with a concomitant reduction of N-cadherin mRNA.
n3:mentions
n4:24305977
Subject Item
_:vb33216308
rdf:type
n3:Context
rdf:value
ENT thus reverses EMT in triple-negative breast cancer cells, limiting invasive and metastatic potential [>>178<<].
n3:mentions
n4:24305977
Subject Item
_:vb33216309
rdf:type
n3:Context
rdf:value
MEK is an attractive target for selective inhibition because of its allosteric binding site, which allows for noncompetitive inhibition, and because all tumors dependent on MAPK signaling are potentially vulnerable to MEK inhibitors [>>179<<]. For example, trametinib, a MEK inhibitor, showed higher progression-free and overall survival at six months in phase III trials and was approved by the FDA in May 2013.
n3:mentions
n4:23934108
Subject Item
_:vb33216310
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Selumetinib, which is in phase II trials, has also shown increased PFS and OS [>>180<<]. Since PI3K and mTOR have similar catalytic sites, ATP-competitive compounds that target both have been developed in an attempt to increase efficacy. Pre-clinical studies show that dual PI3K/mTOR inhibitors reduce proliferation and
n3:mentions
n4:24434059
Subject Item
_:vb33216311
rdf:type
n3:Context
rdf:value
Pre-clinical studies show that dual PI3K/mTOR inhibitors reduce proliferation and induce apoptosis [>>181<<].
n3:mentions
n4:23085539
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20
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