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PMC0
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10.1186%2Fs12885-017-3477-0
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results
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Next from SHH-MB of Ptch1 +/− mice [>>28<<], we isolated and characterized CSCs capable to grow as oncospheres in stem cell-medium [26].
n2:mentions
n3:18691548
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_:vb65793257
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Next from SHH-MB of Ptch1 +/− mice [28], we isolated and characterized CSCs capable to grow as oncospheres in stem cell-medium [>>26<<]. In this study we aimed to investigate the Hh/Gli signaling and miR-326 network in SHH-MB CSCs context. First we observed that Hh/Gli signaling components, including Gli1, Gli2 and Smo, together with stemness markers Nanog, Sox2 and
n2:mentions
n3:20581804
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_:vb65793258
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Notably, miR-326 and Arrb1 share common regulatory sequences acting as a single transcriptional unit [>>35<<]. Together these data prompted us to investigate Arrb1 in CSCs. We found low Arrb1 expression levels of both mRNA and protein (Fig. 2b), while Arrb1 was expressed in differentiated CSCs (DFM) (Fig. 2c). These results highlighted that low
n2:mentions
n3:20075166
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The observation of low levels of miR-326 and Arrb1 in CSCs derived from SHH-MBs suggests that they can negatively regulate the major pro-proliferative signaling in these cells, namely the Hh/Gli pathway [>>25<<–28].
n2:mentions
n3:20581804 n3:25646180 n3:18691548 n3:18691547
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_:vb65793260
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Indeed, miR-326 reduced Smo protein, as already described in undifferentiated GCPs [>>23<<], but also downregulated Gli2 levels (Fig.
n2:mentions
n3:18756266
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_:vb65793261
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that the overexpression of miR-326 impaired the expression levels of the transcription target genes of the Hh/Gli pathway as defined by KEGG pathway analysis and literature Gli1, Ptch1, Hhip1, Mycn, Ccnd1, Ccnd2, Bcl2, Nanog, Srfp1 [36, >>37<<] (Fig. 3c).Fig.
n2:mentions
n3:17089004
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_:vb65793262
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Next, since Hh/Gli pathway controls CSCs [>>25<<] and their stemness marker Nanog [26] we investigated whether miR-326 re-expression impairs self-renewal and cell proliferation rate in our cellular model.
n2:mentions
n3:25646180
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_:vb65793263
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Next, since Hh/Gli pathway controls CSCs [25] and their stemness marker Nanog [>>26<<] we investigated whether miR-326 re-expression impairs self-renewal and cell proliferation rate in our cellular model.
n2:mentions
n3:20581804
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Arrb1 encodes a multifunctional adaptor and scaffold protein regulating several signaling pathways critically involved in cell development in both physiological and pathological (i.e. cancer) contexts [>>38<<]. Arrb1 was reported to function as a protein that interacts with the histone acetyl-transferase (HAT) facilitating its recruitment to target histones, with consequent increased chromatin acetylation and transcription activation [31, 39].
n2:mentions
n3:17305471
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Arrb1 was reported to function as a protein that interacts with the histone acetyl-transferase (HAT) facilitating its recruitment to target histones, with consequent increased chromatin acetylation and transcription activation [>>31<<, 39]. We previously reported that Gli transcription factors activity is regulated by acetylation via the acetyl-transferase p300 [20, 32].
n2:mentions
n3:16325578
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Arrb1 was reported to function as a protein that interacts with the histone acetyl-transferase (HAT) facilitating its recruitment to target histones, with consequent increased chromatin acetylation and transcription activation [31, >>39<<]. We previously reported that Gli transcription factors activity is regulated by acetylation via the acetyl-transferase p300 [20, 32].
n2:mentions
n3:20935513
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_:vb65793267
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We previously reported that Gli transcription factors activity is regulated by acetylation via the acetyl-transferase p300 [>>20<<, 32].
n2:mentions
n3:20081843
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_:vb65793268
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We previously reported that Gli transcription factors activity is regulated by acetylation via the acetyl-transferase p300 [20, >>32<<].
n2:mentions
n3:23762415
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These results show that shifting SHH-MB CSCs to DFM induces the expression of Arrb1 and is linked to Gli1 acetylation, a modification that limits the activity of this transcription factor [>>20<<]. Since Gli1 acetylation is regulated by p300 [20] we sought to investigate the role of Arrb1 in this regulatory mechanism.
n2:mentions
n3:20081843
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_:vb65793270
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Since Gli1 acetylation is regulated by p300 [>>20<<] we sought to investigate the role of Arrb1 in this regulatory mechanism.
n2:mentions
n3:20081843
Subject Item
_:vb65793271
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link Arrb1 to Gli1 acetylation and activity, we tested the effects of exogenously expressed Arrb1 on transcriptional activation of a Gli-responsive luciferase reporter by wild-type Gli1 or the Gli1K518R acetylation defective mutant [>>20<<]. As shown in Fig. 4f, Arrb1 inhibited the activity of wild type Gli1, whereas the Gli1K518R mutant was not affected.
n2:mentions
n3:20081843
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Collectively, this data suggest that the previously described acetylation mechanism of Gli1 and Gli2 function [>>20<<] is a part of a regulatory Arrb1/p300-dependent circuitry in cancer context.
n2:mentions
n3:20081843
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We previously reported that human SHH-MB expressed low levels of mature miR-326 [>>23<<, 33]. Taking in consideration our results in mouse models of SHH-MB we evaluated ARRB1 and pri-miR-326 expression levels in primary tumors derived from SHH-MB patients.
n2:mentions
n3:18756266
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We previously reported that human SHH-MB expressed low levels of mature miR-326 [23, >>33<<]. Taking in consideration our results in mouse models of SHH-MB we evaluated ARRB1 and pri-miR-326 expression levels in primary tumors derived from SHH-MB patients.
n2:mentions
n3:18973228
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n11:Section
dc:title
methods
n11:contains
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Murine CSCs were isolated, as previously reported [>>26<<] from Ptch1+/− mice model of SHH-MB (The Jackson Laboratory, Bar Harbor, ME, USA) maintained in the Molecular Medicine Department Animal Facility at Sapienza University of Rome.
n2:mentions
n3:20581804
Subject Item
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CSCs were cultured as previously reported [>>26<<]. Selective medium (SM) was used for CSCs enrichment, consisting of DMEM/F12 with B27 supplement without vitamin A and 2 mg/ml heparin, 0,6% glucose, 60 mg/ml N-acetyl-L-cysteine, 25 μg/ml insulin, 20 ng/ml EGF, 20 ng/ml bFGF.
n2:mentions
n3:20581804
Subject Item
_:vb65793278
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Oncosphere-forming assay was performed as previously described [>>26<<]. In detail, cells were plated at clonal density (1–2 cells/mm2) into 96-well plates and cultured in SM.
n2:mentions
n3:20581804
Subject Item
_:vb65793279
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miR-326 vector and its negative control were purchased from GeneCopoeia (MmiR3333-MR01); Arrb1 vector was obtained from Addgene [>>29<<]. For rescue experiments, cells were transfected with both miR-326 vector and SmoM2 and Gli2-Flag plasmid vectors [23, 26].
n2:mentions
n3:9924018
Subject Item
_:vb65793280
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For rescue experiments, cells were transfected with both miR-326 vector and SmoM2 and Gli2-Flag plasmid vectors [>>23<<, 26].
n2:mentions
n3:18756266
Subject Item
_:vb65793281
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For rescue experiments, cells were transfected with both miR-326 vector and SmoM2 and Gli2-Flag plasmid vectors [23, >>26<<].
n2:mentions
n3:20581804
Subject Item
_:vb65793282
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Proliferation of MB CSCs was evaluated by BrdU incorporation, as previously described [>>30<<]. Cells were counted in triplicate and the number of BrdU-positive nuclei was annotated.
n2:mentions
n3:24076654
Subject Item
_:vb65793283
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HEK293T cells were cultured and transfected as previsouly described [>>26<<] with the indicated plasmids as in [31].
n2:mentions
n3:20581804
Subject Item
_:vb65793284
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HEK293T cells were cultured and transfected as previsouly described [26] with the indicated plasmids as in [>>31<<].
n2:mentions
n3:16325578
Subject Item
_:vb65793285
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anti-Nanog (Cosmo Bio Co, Japan), anti-Actin I-19 (sc-1616; Santa Cruz Biotechnology), anti-β-III-Tubulin (MAB 1637 Millipore), anti-Gli1 H-300 (sc-20,687; Santa Cruz Biotechnology), anti-acetyl-Gli1 (Lys518) (Eurogentec) [>>32<<], anti-p300 C-20 (sc-585; Santa Cruz Biotechnology), anti-FLAG M2-Peroxidase (HRP) (A8592 Sigma), anti-HA (sc-7392 Santa Cruz), anti-Gli2 H-300 (sc-28,674; Santa Cruz Biotechnology), anti-Smo N-19 (sc-6366; Santa Cruz Biotechnology),
n2:mentions
n3:23762415
Subject Item
_:vb65793286
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One μg was reverse transcribed using random primers and SuperScript II as previously described [>>23<<]. Quantitative RT-PCR (qRT-PCR) analysis was performed using the ABI Prism 7900HT Sequence Detection System, using the “best coverage” TaqMan gene expression assays, specific for each analyzed mRNA, according to manufacturer’s protocol.
n2:mentions
n3:18756266
Subject Item
_:vb65793287
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For analysis of luciferase activity from the Gli-responsive reporter in presence of Arrb1, cells were transfected with Gli-responsive reporter (Gli8x_luc) and with a wild-type Gli1 vector (Gli1 wt) or a Gli1 mutant (Gli1 K518R) [>>20<<], together with the Arrb1 plasmid or an empty vector as control. In all luciferase experiments pRL-CMV-Renilla Luciferase control vector was used.
n2:mentions
n3:20081843
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Surgical specimens used in this study originate from a cohort of patients, recruited with Institutional Review Board approval of the contributing Centers, as previously described [>>23<<, 33]. For this study 10 ng of cDNA from each MB was analyzed for the expression levels of genes specific for SHH-MB molecular classification (as described in [10, 34]).
n2:mentions
n3:18756266
Subject Item
_:vb65793289
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Surgical specimens used in this study originate from a cohort of patients, recruited with Institutional Review Board approval of the contributing Centers, as previously described [23, >>33<<]. For this study 10 ng of cDNA from each MB was analyzed for the expression levels of genes specific for SHH-MB molecular classification (as described in [10, 34]).
n2:mentions
n3:18973228
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For this study 10 ng of cDNA from each MB was analyzed for the expression levels of genes specific for SHH-MB molecular classification (as described in [>>10<<, 34]).
n2:mentions
n3:22358457
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miR-326 is a recognized tumor-suppressing miRNA, in fact among its targets there are Gli2, Smo, Notch1, Notch2 and Nob1 [>>23<<, 40–46]. miR-326 has been already described down regulated in several tumors [40–42], including brain tumor, e.g. medulloblastoma itself [23] and glioblastoma [43–45] where it targets key molecules of gliomagenesis [43, 46] and its
n2:mentions
n3:18756266
Subject Item
_:vb65793293
rdf:type
n2:Context
rdf:value
miR-326 is a recognized tumor-suppressing miRNA, in fact among its targets there are Gli2, Smo, Notch1, Notch2 and Nob1 [23, >>40<<–46]. miR-326 has been already described down regulated in several tumors [40–42], including brain tumor, e.g. medulloblastoma itself [23] and glioblastoma [43–45] where it targets key molecules of gliomagenesis [43, 46] and its ectopic
n2:mentions
n3:19883630 n3:25760058 n3:19955368 n3:23869222 n3:26840018 n3:25173582
Subject Item
_:vb65793294
rdf:type
n2:Context
rdf:value
miR-326 has been already described down regulated in several tumors [>>40<<–42], including brain tumor, e.g. medulloblastoma itself [23] and glioblastoma [43–45] where it targets key molecules of gliomagenesis [43, 46] and its ectopic expression impaired the viability of both glioma cell lines and glioma
n2:mentions
n3:19883630 n3:25760058 n3:26840018
Subject Item
_:vb65793295
rdf:type
n2:Context
rdf:value
miR-326 has been already described down regulated in several tumors [40–42], including brain tumor, e.g. medulloblastoma itself [>>23<<] and glioblastoma [43–45] where it targets key molecules of gliomagenesis [43, 46] and its ectopic expression impaired the viability of both glioma cell lines and glioma stem-like cells [43].
n2:mentions
n3:18756266
Subject Item
_:vb65793296
rdf:type
n2:Context
rdf:value
miR-326 has been already described down regulated in several tumors [40–42], including brain tumor, e.g. medulloblastoma itself [23] and glioblastoma [>>43<<–45] where it targets key molecules of gliomagenesis [43, 46] and its ectopic expression impaired the viability of both glioma cell lines and glioma stem-like cells [43].
n2:mentions
n3:19955368 n3:25173582
Subject Item
_:vb65793297
rdf:type
n2:Context
rdf:value
miR-326 has been already described down regulated in several tumors [40–42], including brain tumor, e.g. medulloblastoma itself [23] and glioblastoma [43–45] where it targets key molecules of gliomagenesis [>>43<<, 46] and its ectopic expression impaired the viability of both glioma cell lines and glioma stem-like cells [43].
n2:mentions
n3:19955368
Subject Item
_:vb65793298
rdf:type
n2:Context
rdf:value
miR-326 has been already described down regulated in several tumors [40–42], including brain tumor, e.g. medulloblastoma itself [23] and glioblastoma [43–45] where it targets key molecules of gliomagenesis [43, >>46<<] and its ectopic expression impaired the viability of both glioma cell lines and glioma stem-like cells [43].
n2:mentions
n3:23869222
Subject Item
_:vb65793299
rdf:type
n2:Context
rdf:value
brain tumor, e.g. medulloblastoma itself [23] and glioblastoma [43–45] where it targets key molecules of gliomagenesis [43, 46] and its ectopic expression impaired the viability of both glioma cell lines and glioma stem-like cells [>>43<<]. Of note, miR-326 levels have been shown to have a prognostic significance in glioblastoma patients [47].
n2:mentions
n3:19955368
Subject Item
_:vb65793300
rdf:type
n2:Context
rdf:value
Of note, miR-326 levels have been shown to have a prognostic significance in glioblastoma patients [>>47<<].
n2:mentions
n3:23302469
Subject Item
_:vb65793301
rdf:type
n2:Context
rdf:value
adaptor/scaffold protein that shuttles between the cytoplasm and the nucleus, where it interacts with CREB and with p300 acetyltransferase on the promoters of target genes to enhance H3 and H4 histones acetylation and gene expression [>>48<<–51]. Our observation that Arrb1 promotes p300-mediated acetylation of Gli1 is consistent with such described ability to facilitate p300-dependent acetylation [31, 39] and extends to a more direct modality to modulate gene expression in
n2:mentions
n3:24937675 n3:16325578 n3:20935513 n3:21212384
Subject Item
_:vb65793302
rdf:type
n2:Context
rdf:value
Our observation that Arrb1 promotes p300-mediated acetylation of Gli1 is consistent with such described ability to facilitate p300-dependent acetylation [>>31<<, 39] and extends to a more direct modality to modulate gene expression in the nucleus.
n2:mentions
n3:16325578
Subject Item
_:vb65793303
rdf:type
n2:Context
rdf:value
Our observation that Arrb1 promotes p300-mediated acetylation of Gli1 is consistent with such described ability to facilitate p300-dependent acetylation [31, >>39<<] and extends to a more direct modality to modulate gene expression in the nucleus.
n2:mentions
n3:20935513
Subject Item
_:vb65793304
rdf:type
n2:Context
rdf:value
We previously reported that Gli1 activity is regulated by acetylation [>>20<<, 32]. HDAC1-mediated deacetylation enhances Gli1 transcriptional activity, whereas acetylation at specific lysine residues inhibits their function [20, 32].
n2:mentions
n3:20081843
Subject Item
_:vb65793305
rdf:type
n2:Context
rdf:value
We previously reported that Gli1 activity is regulated by acetylation [20, >>32<<]. HDAC1-mediated deacetylation enhances Gli1 transcriptional activity, whereas acetylation at specific lysine residues inhibits their function [20, 32].
n2:mentions
n3:23762415
Subject Item
_:vb65793306
rdf:type
n2:Context
rdf:value
HDAC1-mediated deacetylation enhances Gli1 transcriptional activity, whereas acetylation at specific lysine residues inhibits their function [>>20<<, 32]. We show here that p300 is the HAT involved and, more importantly, that Arrb1 enhances this function. Thus, Arrb1 targets Gli1 and has a specific role in controlling Hh/Gli pathway and stemness. However we cannot exclude that such
n2:mentions
n3:20081843
Subject Item
_:vb65793307
rdf:type
n2:Context
rdf:value
HDAC1-mediated deacetylation enhances Gli1 transcriptional activity, whereas acetylation at specific lysine residues inhibits their function [20, >>32<<]. We show here that p300 is the HAT involved and, more importantly, that Arrb1 enhances this function. Thus, Arrb1 targets Gli1 and has a specific role in controlling Hh/Gli pathway and stemness. However we cannot exclude that such
n2:mentions
n3:23762415
Subject Item
_:vb65793308
rdf:type
n2:Context
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However we cannot exclude that such mechanism could involve other acetyl-transferases, e.g. p300/CBP-associated factor (PCAF) which has been reported to be able to interact with both Gli1 [>>52<<] and Arrb1 [53].
n2:mentions
n3:24013724
Subject Item
_:vb65793309
rdf:type
n2:Context
rdf:value
However we cannot exclude that such mechanism could involve other acetyl-transferases, e.g. p300/CBP-associated factor (PCAF) which has been reported to be able to interact with both Gli1 [52] and Arrb1 [>>53<<]. Similarly, the pleiotropic effect achievable by modulating protein acetylation may underlie other possible functions of Arrb1 in controlling other mechanisms of cell growth arrest [48].
n2:mentions
n3:27308406
Subject Item
_:vb65793310
rdf:type
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Similarly, the pleiotropic effect achievable by modulating protein acetylation may underlie other possible functions of Arrb1 in controlling other mechanisms of cell growth arrest [>>48<<].
n2:mentions
n3:20935513
Subject Item
_:vb65793311
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n11:Section
dc:title
background
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_:vb65793328 _:vb65793329 _:vb65793330 _:vb65793320 _:vb65793321 _:vb65793322 _:vb65793323 _:vb65793324 _:vb65793325 _:vb65793326 _:vb65793327 _:vb65793312 _:vb65793313 _:vb65793314 _:vb65793315 _:vb65793316 _:vb65793317 _:vb65793318 _:vb65793319
Subject Item
_:vb65793312
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CSCs could trigger tumor formation, drive resistance to conventional therapeutics and underlie patient relapse [>>1<<, 2]. Indeed, stem cell signatures have been associated with poor prognosis in various tumors [1, 3–7]. CSCs have also been identified in medulloblastoma (MB) [8], the most common pediatric malignant brain tumor and a leading cause of
n2:mentions
n3:24739212
Subject Item
_:vb65793313
rdf:type
n2:Context
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CSCs could trigger tumor formation, drive resistance to conventional therapeutics and underlie patient relapse [1, >>2<<]. Indeed, stem cell signatures have been associated with poor prognosis in various tumors [1, 3–7]. CSCs have also been identified in medulloblastoma (MB) [8], the most common pediatric malignant brain tumor and a leading cause of
n2:mentions
n3:23178582
Subject Item
_:vb65793314
rdf:type
n2:Context
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Indeed, stem cell signatures have been associated with poor prognosis in various tumors [>>1<<, 3–7]. CSCs have also been identified in medulloblastoma (MB) [8], the most common pediatric malignant brain tumor and a leading cause of cancer-related morbidity and mortality in childhood [9].
n2:mentions
n3:24739212
Subject Item
_:vb65793315
rdf:type
n2:Context
rdf:value
Indeed, stem cell signatures have been associated with poor prognosis in various tumors [1, >>3<<–7]. CSCs have also been identified in medulloblastoma (MB) [8], the most common pediatric malignant brain tumor and a leading cause of cancer-related morbidity and mortality in childhood [9].
n2:mentions
n3:22970250 n3:24954133 n3:21169407 n3:18443585 n3:21829201
Subject Item
_:vb65793316
rdf:type
n2:Context
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CSCs have also been identified in medulloblastoma (MB) [>>8<<], the most common pediatric malignant brain tumor and a leading cause of cancer-related morbidity and mortality in childhood [9].
n2:mentions
n3:23592496
Subject Item
_:vb65793317
rdf:type
n2:Context
rdf:value
CSCs have also been identified in medulloblastoma (MB) [8], the most common pediatric malignant brain tumor and a leading cause of cancer-related morbidity and mortality in childhood [>>9<<].
n2:mentions
n3:22832581
Subject Item
_:vb65793318
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They represent an intermediate prognosis subgroup, with overall survival rates ranging from ~35% to ~80% [>>10<<]. Recurrence is a common event in SHH-MBs (30%) making the treatment challenging [11].
n2:mentions
n3:22358457
Subject Item
_:vb65793319
rdf:type
n2:Context
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Recurrence is a common event in SHH-MBs (30%) making the treatment challenging [>>11<<].
n2:mentions
n3:24140199
Subject Item
_:vb65793320
rdf:type
n2:Context
rdf:value
The canonical Hh/Gli pathway activation is modulated by the receptor Patched (Ptch) that suppresses the activity of Smoothened (Smo) [>>12<<, 13]. The binding of SHH protein ligand to Ptch relieves Smo suppression, leading to Hh/Gli activation that culminates in Gli2 transcription factor activation and subsequent translocation to the nucleus [13–15]. Gli2 is able to enhance
n2:mentions
n3:18488998
Subject Item
_:vb65793321
rdf:type
n2:Context
rdf:value
The canonical Hh/Gli pathway activation is modulated by the receptor Patched (Ptch) that suppresses the activity of Smoothened (Smo) [12, >>13<<]. The binding of SHH protein ligand to Ptch relieves Smo suppression, leading to Hh/Gli activation that culminates in Gli2 transcription factor activation and subsequent translocation to the nucleus [13–15]. Gli2 is able to enhance the
n2:mentions
n3:19996169
Subject Item
_:vb65793322
rdf:type
n2:Context
rdf:value
The binding of SHH protein ligand to Ptch relieves Smo suppression, leading to Hh/Gli activation that culminates in Gli2 transcription factor activation and subsequent translocation to the nucleus [>>13<<–15]. Gli2 is able to enhance the transcription of Hh/Gli target genes, including Ptch1 and the transcription factor Gli1, main effector of the signaling. Thus, mutations/focal deletions or amplifications of genes encoding pathway
n2:mentions
n3:16136078 n3:19996169 n3:17641202
Subject Item
_:vb65793323
rdf:type
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On the other hand, non-canonical Hh/Gli activation mechanisms have been described, involving post-transcriptional modification of Gli1, histone methylation, p53/17p deletion and PI3K/Akt/S6 K aberrant activation [>>9<<, 16–22].
n2:mentions
n3:22832581
Subject Item
_:vb65793324
rdf:type
n2:Context
rdf:value
On the other hand, non-canonical Hh/Gli activation mechanisms have been described, involving post-transcriptional modification of Gli1, histone methylation, p53/17p deletion and PI3K/Akt/S6 K aberrant activation [9, >>16<<–22].
n2:mentions
n3:22722829 n3:22820256 n3:22340590 n3:20081843 n3:23231521 n3:24651015 n3:26460945
Subject Item
_:vb65793325
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microRNAs (miRNAs) are major regulators of Hh/Gli signaling [>>23<<] and we have previously shown that miR-326 is downregulated in SHH-MBs where it inhibits Smo [23].
n2:mentions
n3:18756266
Subject Item
_:vb65793326
rdf:type
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microRNAs (miRNAs) are major regulators of Hh/Gli signaling [23] and we have previously shown that miR-326 is downregulated in SHH-MBs where it inhibits Smo [>>23<<]. Recent evidence highlighted the crucial role of miRNAs also in CSCs [24]. The pivotal role of Hh/Gli pathway in controlling CSCs maintenance, including SHH-MB, has already been demonstrated [25–28].
n2:mentions
n3:18756266
Subject Item
_:vb65793327
rdf:type
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Recent evidence highlighted the crucial role of miRNAs also in CSCs [>>24<<]. The pivotal role of Hh/Gli pathway in controlling CSCs maintenance, including SHH-MB, has already been demonstrated [25–28].
n2:mentions
n3:23728460
Subject Item
_:vb65793328
rdf:type
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The pivotal role of Hh/Gli pathway in controlling CSCs maintenance, including SHH-MB, has already been demonstrated [>>25<<–28].
n2:mentions
n3:25646180 n3:18691547 n3:18691548 n3:20581804
Subject Item
_:vb65793329
rdf:type
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We have previously isolated and characterized MB CSCs from mouse model of SHH-MB [>>26<<]. Such CSCs were capable to grow as oncospheres in stem cell-medium and expressed the stemness marker Nanog under Hh/Gli transcriptional regulation [26].
n2:mentions
n3:20581804
Subject Item
_:vb65793330
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Such CSCs were capable to grow as oncospheres in stem cell-medium and expressed the stemness marker Nanog under Hh/Gli transcriptional regulation [>>26<<].
n2:mentions
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