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n3:pmcid
PMC0
bibo:doi
10.1038%2F35081571
n8:contains
_:vb235999
Subject Item
_:vb235999
rdf:type
n8:Section
dc:title
main
n8:contains
_:vb236024 _:vb236025 _:vb236026 _:vb236027 _:vb236028 _:vb236029 _:vb236030 _:vb236031 _:vb236016 _:vb236017 _:vb236018 _:vb236019 _:vb236020 _:vb236021 _:vb236022 _:vb236023 _:vb236008 _:vb236009 _:vb236010 _:vb236011 _:vb236012 _:vb236013 _:vb236014 _:vb236015 _:vb236000 _:vb236001 _:vb236002 _:vb236003 _:vb236004 _:vb236005 _:vb236006 _:vb236007 _:vb236056 _:vb236057 _:vb236058 _:vb236059 _:vb236060 _:vb236061 _:vb236062 _:vb236063 _:vb236048 _:vb236049 _:vb236050 _:vb236051 _:vb236052 _:vb236053 _:vb236054 _:vb236055 _:vb236040 _:vb236041 _:vb236042 _:vb236043 _:vb236044 _:vb236045 _:vb236046 _:vb236047 _:vb236032 _:vb236033 _:vb236034 _:vb236035 _:vb236036 _:vb236037 _:vb236038 _:vb236039 _:vb236088 _:vb236089 _:vb236090 _:vb236091 _:vb236092 _:vb236093 _:vb236094 _:vb236095 _:vb236080 _:vb236081 _:vb236082 _:vb236083 _:vb236084 _:vb236085 _:vb236086 _:vb236087 _:vb236072 _:vb236073 _:vb236074 _:vb236075 _:vb236076 _:vb236077 _:vb236078 _:vb236079 _:vb236064 _:vb236065 _:vb236066 _:vb236067 _:vb236068 _:vb236069 _:vb236070 _:vb236071 _:vb236120 _:vb236121 _:vb236122 _:vb236112 _:vb236113 _:vb236114 _:vb236115 _:vb236116 _:vb236117 _:vb236118 _:vb236119 _:vb236104 _:vb236105 _:vb236106 _:vb236107 _:vb236108 _:vb236109 _:vb236110 _:vb236111 _:vb236096 _:vb236097 _:vb236098 _:vb236099 _:vb236100 _:vb236101 _:vb236102 _:vb236103
Subject Item
_:vb236000
rdf:type
n3:Context
rdf:value
In the nervous system, MMPs have also been associated with pathogenesis, particularly in multiple sclerosis (MS) and malignant gliomas>>1<<. A growing literature has linked MMPs to stroke, to Alzheimer's disease and to viral infections of the central nervous system (CNS). The goal of this review is to acquaint the reader with the biology of MMPs, particularly the functions of
n3:mentions
n2:9498303
Subject Item
_:vb236001
rdf:type
n3:Context
rdf:value
There is about 20% similarity between metzincin subfamilies>>2<<, but identity at the catalytic domain is much higher.
n3:mentions
n2:7663339
Subject Item
_:vb236002
rdf:type
n3:Context
rdf:value
MT4-MMP (MMP17) and MT6-MMP (MMP25) are glycosyl-phosphatidylinositol (GPI)-anchored MMPs (Ref. >>3<<), whereas the other MT-MMPs are transmembrane proteins.
n3:mentions
n2:11034316
Subject Item
_:vb236003
rdf:type
n3:Context
rdf:value
Biological roles for ADAM members>>4<< include specialized functions in cell adhesion, sperm–egg fusion (for example, ADAM1 and -2), myoblast fusion (ADAM12) and the ectodomain shedding of cell-surface proteins (for example, ADAM9, -10 and -17).
n3:mentions
n2:10523497
Subject Item
_:vb236004
rdf:type
n3:Context
rdf:value
The cytoplasmic tails of ADAM9 and -12 interact with protein kinase C and with src, respectively, implicating some ADAM family members as signalling molecules>>5<<,6. Although most ADAMs are transmembrane proteins, some members (for example, ADAM11, -12, -17 and -28) also have alternatively spliced forms that diverge before the transmembrane module to generate a soluble, secreted protein. It is
n3:mentions
n2:9857183
Subject Item
_:vb236005
rdf:type
n3:Context
rdf:value
The cytoplasmic tails of ADAM9 and -12 interact with protein kinase C and with src, respectively, implicating some ADAM family members as signalling molecules5,>>6<<. Although most ADAMs are transmembrane proteins, some members (for example, ADAM11, -12, -17 and -28) also have alternatively spliced forms that diverge before the transmembrane module to generate a soluble, secreted protein. It is
n3:mentions
n2:11104699
Subject Item
_:vb236006
rdf:type
n3:Context
rdf:value
Recently, new members of the ADAM family have been identified>>7<<. They have THROMBOSPONDIN motifs and are therefore known as ADAMTSs.
n3:mentions
n2:8995297
Subject Item
_:vb236007
rdf:type
n3:Context
rdf:value
For example, an early description of ADAM10 in the CNS implicated this protein in oligodendrocyte and myelin biology>>8<<, although the molecule involved was not recognized as an ADAM until later.
n3:mentions
n2:1383841
Subject Item
_:vb236008
rdf:type
n3:Context
rdf:value
and myelin biology8, although the molecule involved was not recognized as an ADAM until later. But despite the limited evidence, ADAMs might be important proteins in the nervous system. At least 17 ADAMs are found in the CNS (Ref. >>9<<) and, in fact, some of these are expressed predominantly in the brain (for example, ADAM22 and -23).
n3:mentions
n2:10860581
Subject Item
_:vb236009
rdf:type
n3:Context
rdf:value
In particular, many of the inhibitors based on the functional group hydroxamate, which chelate the zinc ion from the active site of MMPs, also have activity against ADAMs (Refs >>10<<,11). Last, the thrombospondin motif of ADAMTSs confers degradative activity on several proteoglycans that are enriched in the CNS. Here, we will centre our discussion on two ADAMs, as several lines of evidence indicate their importance in
n3:mentions
n2:9920899
Subject Item
_:vb236010
rdf:type
n3:Context
rdf:value
In particular, many of the inhibitors based on the functional group hydroxamate, which chelate the zinc ion from the active site of MMPs, also have activity against ADAMs (Refs 10,>>11<<). Last, the thrombospondin motif of ADAMTSs confers degradative activity on several proteoglycans that are enriched in the CNS. Here, we will centre our discussion on two ADAMs, as several lines of evidence indicate their importance in
n3:mentions
n2:11301286
Subject Item
_:vb236011
rdf:type
n3:Context
rdf:value
include the plasminogen– plasmin cascade, as well as other MMPs (Table 1) that disrupt the interaction between cysteine and zinc (the so-called 'cysteine switch' mechanism) and then remove the propeptide region for full activation>>13<<. Non-proteolytic compounds such as sulphydryl-reactive agents (4-aminophenylmercuric acetate) and denaturants (urea) can also activate zymogens.
n3:mentions
n2:9165065
Subject Item
_:vb236012
rdf:type
n3:Context
rdf:value
of some MMPs. In this regard, a complex formed by TIMP2 and the carboxyl terminus of pro-MMP2 has been found to bind MT1-MMP (MMP14) on the cell surface. An adjacent MT1-MMP molecule then removes the propeptide region of MMP2 (Ref. >>16<<). The pro-MMP–TIMP–MT-MMP trimolecular complex highlights another feature of MMP regulation:
n3:mentions
n2:9138283
Subject Item
_:vb236013
rdf:type
n3:Context
rdf:value
For example, activated MMP2 can bind the αvβ3 integrin, whereas active MMP9 can interact with the HYALURONAN receptor CD44 on the cell membrane>>17<<.
n3:mentions
n2:9887098
Subject Item
_:vb236014
rdf:type
n3:Context
rdf:value
in MMPs, its secondary structure differs. These features might account for the finding that, whereas TIMP3 inhibits TACE, TIMP1 does not. Also, ADAM10 is inhibited by TIMP1 and -3, and by hydroxamates, but not by TIMP2 and -4 (Ref. >>18<<). So, TIMP3 might be a more general inhibitor of several ADAM family members, including the ADAMTSs.
n3:mentions
n2:10818225
Subject Item
_:vb236015
rdf:type
n3:Context
rdf:value
For example, RNASE PROTECTION ASSAYS have revealed a high constitutive expression of MMP11 and -14 in the adult mouse brain>>19<<. Similarly, the more sensitive polymerase chain reaction (PCR) technique has revealed the expression of MMP2, -3, -7, -9 and -13 in the normal rat spinal cord20. But, overall, MMPs are largely absent from the normal CNS and their
n3:mentions
n2:10878594
Subject Item
_:vb236016
rdf:type
n3:Context
rdf:value
Similarly, the more sensitive polymerase chain reaction (PCR) technique has revealed the expression of MMP2, -3, -7, -9 and -13 in the normal rat spinal cord>>20<<. But, overall, MMPs are largely absent from the normal CNS and their upregulation has been reported in several neurological disorders and after injury. By contrast, in the case of ADAMs, over 17 family members are normally expressed in
n3:mentions
n2:9119983
Subject Item
_:vb236017
rdf:type
n3:Context
rdf:value
are largely absent from the normal CNS and their upregulation has been reported in several neurological disorders and after injury. By contrast, in the case of ADAMs, over 17 family members are normally expressed in the adult CNS (Ref. >>9<<). For example, ADAM17 has been localized by immunohistochemistry to astrocytes and endothelial cells in adult human brain21, whereas ADAM8 has been detected in neurons and oligodendrocytes in the uninjured adult rat CNS (Ref.
n3:mentions
n2:10860581
Subject Item
_:vb236018
rdf:type
n3:Context
rdf:value
For example, ADAM17 has been localized by immunohistochemistry to astrocytes and endothelial cells in adult human brain>>21<<, whereas ADAM8 has been detected in neurons and oligodendrocytes in the uninjured adult rat CNS (Ref.
n3:mentions
n2:11360299
Subject Item
_:vb236019
rdf:type
n3:Context
rdf:value
(Ref. 9). For example, ADAM17 has been localized by immunohistochemistry to astrocytes and endothelial cells in adult human brain21, whereas ADAM8 has been detected in neurons and oligodendrocytes in the uninjured adult rat CNS (Ref. >>22<<). However, the literature on the expression of ADAMs in CNS pathology is limited.
n3:mentions
n2:11050116
Subject Item
_:vb236020
rdf:type
n3:Context
rdf:value
Specifically, MMP9, which is absent in the CSF of normal individuals, is upregulated in MS and in other inflammatory neurological diseases>>23<<. MMP profiles in serum and in leukocytes are also altered in MS. So, when compared to healthy controls, MS patients show increased MMP9 messenger RNA in leukocytes and elevated MMP9 levels in serum. Similarly, the MMP9:TIMP1 ratio in the
n3:mentions
n2:1334098
Subject Item
_:vb236021
rdf:type
n3:Context
rdf:value
Similarly, the MMP9:TIMP1 ratio in the serum of people with MS is higher than normal>>24<<. The serum MMP9 content in MS patients is higher during relapse than in an off-period25. By using GADOLINIUM-ENHANCED MAGNETIC RESONANCE IMAGING (MRI) techniques, it was found that MS patients with high MMP9 and low TIMP1 levels tended to
n3:mentions
n2:10496173
Subject Item
_:vb236022
rdf:type
n3:Context
rdf:value
The serum MMP9 content in MS patients is higher during relapse than in an off-period>>25<<. By using GADOLINIUM-ENHANCED MAGNETIC RESONANCE IMAGING (MRI) techniques, it was found that MS patients with high MMP9 and low TIMP1 levels tended to worsen26. Several groups have shown increased post-mortem expression of various MMP
n3:mentions
n2:10071048
Subject Item
_:vb236023
rdf:type
n3:Context
rdf:value
By using GADOLINIUM-ENHANCED MAGNETIC RESONANCE IMAGING (MRI) techniques, it was found that MS patients with high MMP9 and low TIMP1 levels tended to worsen>>26<<. Several groups have shown increased post-mortem expression of various MMP members (MMP2, -3, -7 and -9) in the brains of patients with MS (Refs 27,28). Cellular sources of MMPs in the diseased brain include infiltrating leukocytes
n3:mentions
n2:10534241
Subject Item
_:vb236024
rdf:type
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Several groups have shown increased post-mortem expression of various MMP members (MMP2, -3, -7 and -9) in the brains of patients with MS (Refs >>27<<,28). Cellular sources of MMPs in the diseased brain include infiltrating leukocytes (lymphocytes and macrophages) and intrinsic CNS cells (perivascular and parenchymal microglia, astrocytes and even neurons). Although it has been less
n3:mentions
n2:8957442
Subject Item
_:vb236025
rdf:type
n3:Context
rdf:value
Several groups have shown increased post-mortem expression of various MMP members (MMP2, -3, -7 and -9) in the brains of patients with MS (Refs 27,>>28<<). Cellular sources of MMPs in the diseased brain include infiltrating leukocytes (lymphocytes and macrophages) and intrinsic CNS cells (perivascular and parenchymal microglia, astrocytes and even neurons). Although it has been less
n3:mentions
n2:9364466
Subject Item
_:vb236026
rdf:type
n3:Context
rdf:value
Although it has been less thoroughly investigated, most studies indicate that TIMP1 and -2 might not be altered in MS compared with controls>>29<<. No data are available for TIMP3 and -4.
n3:mentions
n2:11222449
Subject Item
_:vb236027
rdf:type
n3:Context
rdf:value
By contrast, transcripts encoding MMP2, -3, -11 and -13 were unchanged>>20<<. Surprisingly, the elevation of MMP7 is not noted in mouse EAE, in which a prominent increase in MMP3, -9 and -12 occurs30.
n3:mentions
n2:9119983
Subject Item
_:vb236028
rdf:type
n3:Context
rdf:value
Surprisingly, the elevation of MMP7 is not noted in mouse EAE, in which a prominent increase in MMP3, -9 and -12 occurs>>30<<. So, overall, a common elevation of MMP9 and -12 is found in MS, and in mouse and rat EAE models.
n3:mentions
n2:9502415
Subject Item
_:vb236029
rdf:type
n3:Context
rdf:value
The correlation between elevated MMPs and disease activity is probably causal, as inhibitors of metalloproteinase activity (for example, GM6001, Ro-9790 and BB1101) alleviate or prevent EAE (Refs >>1<<,31). Also, 3–4-week-old mice that lack MMP9 are less impaired after the induction of EAE when compared with wild-type animals32.
n3:mentions
n2:9498303
Subject Item
_:vb236030
rdf:type
n3:Context
rdf:value
The correlation between elevated MMPs and disease activity is probably causal, as inhibitors of metalloproteinase activity (for example, GM6001, Ro-9790 and BB1101) alleviate or prevent EAE (Refs 1,>>31<<). Also, 3–4-week-old mice that lack MMP9 are less impaired after the induction of EAE when compared with wild-type animals32.
n3:mentions
n2:9042108
Subject Item
_:vb236031
rdf:type
n3:Context
rdf:value
Also, 3–4-week-old mice that lack MMP9 are less impaired after the induction of EAE when compared with wild-type animals>>32<<. In humans, interferon-β, a drug used against MS, attenuates MMP9 production by T cells in vitro, in agreement with the decreased capacity of T cells to traverse ECM barriers33,34. In addition, MS patients treated with interferon-β show a
n3:mentions
n2:10587514
Subject Item
_:vb236032
rdf:type
n3:Context
rdf:value
In humans, interferon-β, a drug used against MS, attenuates MMP9 production by T cells in vitro, in agreement with the decreased capacity of T cells to traverse ECM barriers>>33<<,34. In addition, MS patients treated with interferon-β show a decrease in the content of serum MMP9 and a lowering of the number of MMP9-expressing leukocytes35. Together, these observations indicate that the antagonism of MMP function
n3:mentions
n2:9007090
Subject Item
_:vb236033
rdf:type
n3:Context
rdf:value
In humans, interferon-β, a drug used against MS, attenuates MMP9 production by T cells in vitro, in agreement with the decreased capacity of T cells to traverse ECM barriers33,>>34<<. In addition, MS patients treated with interferon-β show a decrease in the content of serum MMP9 and a lowering of the number of MMP9-expressing leukocytes35. Together, these observations indicate that the antagonism of MMP function might
n3:mentions
n2:9007089
Subject Item
_:vb236034
rdf:type
n3:Context
rdf:value
In addition, MS patients treated with interferon-β show a decrease in the content of serum MMP9 and a lowering of the number of MMP9-expressing leukocytes>>35<<. Together, these observations indicate that the antagonism of MMP function might contribute to the efficacy of interferon-β in MS.
n3:mentions
n2:10900359
Subject Item
_:vb236035
rdf:type
n3:Context
rdf:value
In this regard, the capacity of macrophages from MMP12-null mice to penetrate basement membranes is markedly diminished in vitro and in vivo>>36<<. Also, when T cells are applied onto a monolayer of endothelial cells that overlie a barrier of collagen matrix, the addition of GM6001, an metalloproteinase inhibitor, did not prevent the T cells from traversing the endothelial barrier.
n3:mentions
n2:8632994
Subject Item
_:vb236036
rdf:type
n3:Context
rdf:value
However, the entry of T cells into the collagen matrix is abolished>>37<<. One result of disrupting the basement membrane is the breakdown of the blood–brain barrier (BBB).
n3:mentions
n2:9840619
Subject Item
_:vb236037
rdf:type
n3:Context
rdf:value
This has been shown experimentally by the intracerebral injection of MMPs and the subsequent leakage of microvessels>>31<<,38. In addition, there is a good correlation between gadolinium-enhanced MRI activity in humans, an index of BBB dysfunction, and the serum content of MMP9 (Refs 25,26).Figure 2Mechanisms by which MMPs contribute to neuropathology.
n3:mentions
n2:9042108
Subject Item
_:vb236038
rdf:type
n3:Context
rdf:value
This has been shown experimentally by the intracerebral injection of MMPs and the subsequent leakage of microvessels31,>>38<<. In addition, there is a good correlation between gadolinium-enhanced MRI activity in humans, an index of BBB dysfunction, and the serum content of MMP9 (Refs 25,26).Figure 2Mechanisms by which MMPs contribute to neuropathology.
n3:mentions
n2:1381261
Subject Item
_:vb236039
rdf:type
n3:Context
rdf:value
In addition, there is a good correlation between gadolinium-enhanced MRI activity in humans, an index of BBB dysfunction, and the serum content of MMP9 (Refs >>25<<,26).Figure 2Mechanisms by which MMPs contribute to neuropathology.
n3:mentions
n2:10071048
Subject Item
_:vb236040
rdf:type
n3:Context
rdf:value
In addition, there is a good correlation between gadolinium-enhanced MRI activity in humans, an index of BBB dysfunction, and the serum content of MMP9 (Refs 25,>>26<<).Figure 2Mechanisms by which MMPs contribute to neuropathology.
n3:mentions
n2:10534241
Subject Item
_:vb236041
rdf:type
n3:Context
rdf:value
When injected into the CNS, MMPs can disrupt myelin and cause demyelination>>39<<. Furthermore, some of the fragments of the MMP-mediated digestion of myelin basic protein (MBP) can induce EAE when injected into rodents31,40.
n3:mentions
n2:8823386
Subject Item
_:vb236042
rdf:type
n3:Context
rdf:value
Furthermore, some of the fragments of the MMP-mediated digestion of myelin basic protein (MBP) can induce EAE when injected into rodents>>31<<,40. Also, human MMP9 cleaves human MBP into peptide fragments, one of which is the immunodominant epitope in humans40. Another mechanism by which MMPs might promote an inflammatory response is by the conversion of precursor, inactive
n3:mentions
n2:9042108
Subject Item
_:vb236043
rdf:type
n3:Context
rdf:value
Furthermore, some of the fragments of the MMP-mediated digestion of myelin basic protein (MBP) can induce EAE when injected into rodents31,>>40<<. Also, human MMP9 cleaves human MBP into peptide fragments, one of which is the immunodominant epitope in humans40. Another mechanism by which MMPs might promote an inflammatory response is by the conversion of precursor, inactive
n3:mentions
n2:8172641
Subject Item
_:vb236044
rdf:type
n3:Context
rdf:value
Also, human MMP9 cleaves human MBP into peptide fragments, one of which is the immunodominant epitope in humans>>40<<. Another mechanism by which MMPs might promote an inflammatory response is by the conversion of precursor, inactive molecules into their activated forms. Tumour-necrosis factor (TNF)-α — a pro-inflammatory cytokine with several actions
n3:mentions
n2:8172641
Subject Item
_:vb236045
rdf:type
n3:Context
rdf:value
— is first made as a 26-kDa membrane-associated protein that requires proteolytic conversion to the fully active 17-kDa protein. Although TACE is known to be the protease that mediates the physiological maturation of TNF-α (Ref. >>41<<), it is clear that MMP7 and MT4-MMP can also efficiently mediate this conversion42.
n3:mentions
n2:9034190
Subject Item
_:vb236046
rdf:type
n3:Context
rdf:value
41), it is clear that MMP7 and MT4-MMP can also efficiently mediate this conversion>>42<<. Other molecules, such as transforming growth factor (TGF)-α, IL-6, TNF receptors, l-selectins and FAS LIGAND (FasL), are also synthesized as precursors that require processing by MMPs or ADAMs for maturation. So, in pathological
n3:mentions
n2:10799478
Subject Item
_:vb236047
rdf:type
n3:Context
rdf:value
Another pathogenic effect of MMPs in the CNS is neurotoxicity. Vos et al.>>43<< reported that MMP1 is toxic to spinal cord neurons in vitro, and we found a similar neurotoxic effect of MMP2 (Ref.
n3:mentions
n2:10833306
Subject Item
_:vb236048
rdf:type
n3:Context
rdf:value
43 reported that MMP1 is toxic to spinal cord neurons in vitro, and we found a similar neurotoxic effect of MMP2 (Ref. >>44<<). An alternative mechanism for MMP-mediated death might involve the phenomenon known as 'anoikis' (Greek for homelessness); cells that are attached to an ECM substrate survive through integrin signalling and death ensues when the cell is
n3:mentions
n2:11220743
Subject Item
_:vb236049
rdf:type
n3:Context
rdf:value
mechanism for MMP-mediated death might involve the phenomenon known as 'anoikis' (Greek for homelessness); cells that are attached to an ECM substrate survive through integrin signalling and death ensues when the cell is detached>>45<<. In principle, MMPs can indirectly cause cell death by degrading ECM and therefore interfering with cell attachment and integrin signalling.
n3:mentions
n2:10446041
Subject Item
_:vb236050
rdf:type
n3:Context
rdf:value
Indeed, neuronal death in the hippocampus after kainate-induced seizures in animals has been attributed to proteases that degrade laminin>>46<<. Finally, it has been noted that MMP7, but not MMP2, -3 or -9, acts on cell-associated FasL to convert it into soluble FasL, which induces apoptosis of epithelial cells47. Conversely, MMP7-mediated cleavage of FasL protects sarcoma and
n3:mentions
n2:9428515
Subject Item
_:vb236051
rdf:type
n3:Context
rdf:value
Finally, it has been noted that MMP7, but not MMP2, -3 or -9, acts on cell-associated FasL to convert it into soluble FasL, which induces apoptosis of epithelial cells>>47<<. Conversely, MMP7-mediated cleavage of FasL protects sarcoma and colon carcinoma cells from chemotherapy-induced cytotoxicity. Given the presence of Fas and FasL in the CNS, MMPs could affect cell survival or death by similar mechanisms.
n3:mentions
n2:10607586
Subject Item
_:vb236052
rdf:type
n3:Context
rdf:value
The literature on the upregulation of ADAMs in the CNS of MS patients is still in its infancy. Cells of the immune system produce various ADAMs (Ref. >>48<<), and it is likely that several ADAMs will be elevated in the CNS during neuroinflammation and MS.
n3:mentions
n2:10354553
Subject Item
_:vb236053
rdf:type
n3:Context
rdf:value
More recent studies have extended the roles of MMPs to other features of tumour progression, notably proliferation, angiogenesis and survival>>49<<. Essentially, all MMP members have been linked to cancers of various origins. So, it is not surprising that there are many reports of the increased expression of MMPs in brain tumours in situ and in vitro. Specifically, the upregulation
n3:mentions
n2:10740253
Subject Item
_:vb236054
rdf:type
n3:Context
rdf:value
Specifically, the upregulation of MMP2, -9 and all the MT-MMP members has been noted in high-grade specimens of GLIOBLASTOMA MULTIFORME (GBM) as compared to lower-grade cases or to non-transformed control brains>>50<<,51,52. The finding that AG3340 — an inhibitor of metalloproteinase activity — inhibits glioma growth, invasion and angiogenesis in animals53 highlights the importance of MMPs in the progression of brain tumours.
n3:mentions
n2:9708803
Subject Item
_:vb236055
rdf:type
n3:Context
rdf:value
Specifically, the upregulation of MMP2, -9 and all the MT-MMP members has been noted in high-grade specimens of GLIOBLASTOMA MULTIFORME (GBM) as compared to lower-grade cases or to non-transformed control brains50,>>51<<,52. The finding that AG3340 — an inhibitor of metalloproteinase activity — inhibits glioma growth, invasion and angiogenesis in animals53 highlights the importance of MMPs in the progression of brain tumours.
n3:mentions
n2:10206300
Subject Item
_:vb236056
rdf:type
n3:Context
rdf:value
Specifically, the upregulation of MMP2, -9 and all the MT-MMP members has been noted in high-grade specimens of GLIOBLASTOMA MULTIFORME (GBM) as compared to lower-grade cases or to non-transformed control brains50,51,>>52<<. The finding that AG3340 — an inhibitor of metalloproteinase activity — inhibits glioma growth, invasion and angiogenesis in animals53 highlights the importance of MMPs in the progression of brain tumours.
n3:mentions
n2:11235952
Subject Item
_:vb236057
rdf:type
n3:Context
rdf:value
The finding that AG3340 — an inhibitor of metalloproteinase activity — inhibits glioma growth, invasion and angiogenesis in animals>>53<< highlights the importance of MMPs in the progression of brain tumours.
n3:mentions
n2:10213221
Subject Item
_:vb236058
rdf:type
n3:Context
rdf:value
By contrast, MMP9 is predominantly expressed in blood vessels at proliferative margins>>51<<. A simplistic interpretation of these results is that MMP2 and MT-MMPs might regulate glioma invasiveness, whereas MMP9 might be crucial for angiogenesis. In this regard, the capacity of various glioma lines to migrate across a
n3:mentions
n2:10206300
Subject Item
_:vb236059
rdf:type
n3:Context
rdf:value
In this regard, the capacity of various glioma lines to migrate across a reconstituted basement membrane in vitro is correlated with the levels of MMP2 expression>>54<<. Furthermore, the ability of the C6 gliosarcoma line to migrate along myelin is related to MT1-MMP activity55. As mentioned earlier, MT1-MMP facilitates the activation of MMP2, and an excessive MT1-MMP activity was recently noted in GBMs
n3:mentions
n2:8871536
Subject Item
_:vb236060
rdf:type
n3:Context
rdf:value
Furthermore, the ability of the C6 gliosarcoma line to migrate along myelin is related to MT1-MMP activity>>55<<. As mentioned earlier, MT1-MMP facilitates the activation of MMP2, and an excessive MT1-MMP activity was recently noted in GBMs (Ref. 52). Similarly, factors that stimulate glioma motility, such as hepatocyte growth factor/scatter factor,
n3:mentions
n2:9922462
Subject Item
_:vb236061
rdf:type
n3:Context
rdf:value
the ability of the C6 gliosarcoma line to migrate along myelin is related to MT1-MMP activity55. As mentioned earlier, MT1-MMP facilitates the activation of MMP2, and an excessive MT1-MMP activity was recently noted in GBMs (Ref. >>52<<). Similarly, factors that stimulate glioma motility, such as hepatocyte growth factor/scatter factor, increase MMP2 or MT1-MMP levels.
n3:mentions
n2:11235952
Subject Item
_:vb236062
rdf:type
n3:Context
rdf:value
of urokinase plaminogen activator (uPA) to its receptor molecule uPAR. This results in uPA activation and the subsequent conversion of plasminogen to plasmin by uPA. It is noteworthy that the uPA and uPAR are upregulated in GBMs (Ref. >>57<<), endowing the tumour with the machinery to activate its own MMPs effectively.
n3:mentions
n2:8033079
Subject Item
_:vb236063
rdf:type
n3:Context
rdf:value
In support of this idea, downregulation of uPAR in a glioma cell line led to decreased capacity to invade brain aggregates>>58<<. The expression of MMPs by glioma cells highlights a difference between CNS and systemic cancers. In the latter (for example, breast cancers), MMPs are often expressed by the stroma, rather than by the tumour itself. So, several
n3:mentions
n2:9219733
Subject Item
_:vb236064
rdf:type
n3:Context
rdf:value
A decrease in TIMP2 content in GBM compared to lower-grade tumours has been noted in some>>52<<, but not all50, studies.
n3:mentions
n2:11235952
Subject Item
_:vb236065
rdf:type
n3:Context
rdf:value
A decrease in TIMP2 content in GBM compared to lower-grade tumours has been noted in some52, but not all>>50<<, studies. This decrease would potentially remove a counterbalance for MMP activity. Although earlier studies noted a decrease of TIMP1 with increasing grades of glioma, later studies noted that it was actually upregulated in GBM (Refs
n3:mentions
n2:9708803
Subject Item
_:vb236066
rdf:type
n3:Context
rdf:value
Although earlier studies noted a decrease of TIMP1 with increasing grades of glioma, later studies noted that it was actually upregulated in GBM (Refs >>50<<,52). It is worth noting in this context that TIMPs have several properties that can contribute to the pathophysiology of cancer cells. Indeed, TIMPs have mitogenic action, and regulate survival and apoptosis independently of their
n3:mentions
n2:9708803
Subject Item
_:vb236067
rdf:type
n3:Context
rdf:value
Although earlier studies noted a decrease of TIMP1 with increasing grades of glioma, later studies noted that it was actually upregulated in GBM (Refs 50,>>52<<). It is worth noting in this context that TIMPs have several properties that can contribute to the pathophysiology of cancer cells. Indeed, TIMPs have mitogenic action, and regulate survival and apoptosis independently of their inhibitory
n3:mentions
n2:11235952
Subject Item
_:vb236068
rdf:type
n3:Context
rdf:value
A role for ADAMs in glioma biology remains to be defined and the related literature is limited at present>>59<<.
n3:mentions
n2:11050470
Subject Item
_:vb236069
rdf:type
n3:Context
rdf:value
A role for metalloproteinases in stroke is indicated by the finding that MMP2 and -9 are rapidly upregulated after focal cerebral ischaemia in rats>>60<<,61. In humans, elevation of brain MMP9 is detected post mortem within days of infarction and, interestingly, this protein remained elevated in patients that died months after the event62. In another report, MMP9 was strongly expressed by
n3:mentions
n2:8621740
Subject Item
_:vb236070
rdf:type
n3:Context
rdf:value
A role for metalloproteinases in stroke is indicated by the finding that MMP2 and -9 are rapidly upregulated after focal cerebral ischaemia in rats60,>>61<<. In humans, elevation of brain MMP9 is detected post mortem within days of infarction and, interestingly, this protein remained elevated in patients that died months after the event62. In another report, MMP9 was strongly expressed by
n3:mentions
n2:9596253
Subject Item
_:vb236071
rdf:type
n3:Context
rdf:value
In humans, elevation of brain MMP9 is detected post mortem within days of infarction and, interestingly, this protein remained elevated in patients that died months after the event>>62<<. In another report, MMP9 was strongly expressed by neutrophils in tissues from patients up to one week after an infarct, whereas the expression of MMP2 and -7 was less marked. From one week to five years, neutrophils were absent in the
n3:mentions
n2:9464653
Subject Item
_:vb236072
rdf:type
n3:Context
rdf:value
one week after an infarct, whereas the expression of MMP2 and -7 was less marked. From one week to five years, neutrophils were absent in the lesions and the large number of macrophages present were immunoreactive for MMP2 and -7 (Ref. >>28<<). The elevated MMP expression might contribute to the tissue destruction in stroke.
n3:mentions
n2:9364466
Subject Item
_:vb236073
rdf:type
n3:Context
rdf:value
destruction in stroke. As noted earlier, MMPs have the capacity to kill neurons (Fig. 2). Indeed, the intravenous treatment of rats with a neutralizing MMP9 antibody one hour before vessel occlusion reduced infarct size by 28% (Ref. >>61<<). In addition, the size of infarcts after ischaemia in MMP9-null mice was less than that observed in wild-type controls63.
n3:mentions
n2:9596253
Subject Item
_:vb236074
rdf:type
n3:Context
rdf:value
In addition, the size of infarcts after ischaemia in MMP9-null mice was less than that observed in wild-type controls>>63<<.
n3:mentions
n2:11129784
Subject Item
_:vb236075
rdf:type
n3:Context
rdf:value
Elevated expression of MMP9 has been detected in the CSF of HIV-infected patients>>64<<. MMP2, -7 and -9 are increased in the CSF of patients with HIV-associated dementia compared to that of non-demented AIDS patients65. When brain-derived sequences of the HIV-transactivating protein TAT (tyrosine aminotransferase), obtained
n3:mentions
n2:9728558
Subject Item
_:vb236076
rdf:type
n3:Context
rdf:value
MMP2, -7 and -9 are increased in the CSF of patients with HIV-associated dementia compared to that of non-demented AIDS patients>>65<<. When brain-derived sequences of the HIV-transactivating protein TAT (tyrosine aminotransferase), obtained from demented patients, were expressed in U937 monocytoid cells and human macrophages, elevated MMP2 and -7 expression was obtained
n3:mentions
n2:10482270
Subject Item
_:vb236077
rdf:type
n3:Context
rdf:value
These elevated MMPs resulted in neuronal death>>44<<. Collectively, the results indicate that HIV infection induces MMP expression in macrophages and that the latter are the possible sources of MMPs and neurotoxicity in the CNS of people with HIV-associated dementia.
n3:mentions
n2:11220743
Subject Item
_:vb236078
rdf:type
n3:Context
rdf:value
Other viruses, including EPSTEIN–BARR VIRUS, HTLV-1 and CORONAVIRUS>>66<< have also been reported to increase the expression of MMPs in susceptible cell types.
n3:mentions
n2:10900340
Subject Item
_:vb236079
rdf:type
n3:Context
rdf:value
Three proteases — α-, β- and γ-secretase — are involved in APP cleavage at different sites to generate Aβ peptides of various lengths>>67<<. The predominant cleavage is mediated by γ-secretase, and this mode of cleavage is thought to be non-amyloidogenic. By contrast, the combination of β-secretase and γ-secretase activities releases the amyloidogenic Aβ peptide. The aspartyl
n3:mentions
n2:9854312
Subject Item
_:vb236080
rdf:type
n3:Context
rdf:value
The aspartyl protease BACE (β-site APP cleavage enzyme) is the best candidate to be the β-secretase>>68<<, whereas the γ-secretase activity depends on proteins known as presenilins.
n3:mentions
n2:10531052
Subject Item
_:vb236081
rdf:type
n3:Context
rdf:value
It was initially suggested that MMP2 was the α-secretase>>69<<, but this idea was quickly disputed. Moreover, it was also suggested that MMP2 had β-secretase-like activity70.
n3:mentions
n2:8479521
Subject Item
_:vb236082
rdf:type
n3:Context
rdf:value
Moreover, it was also suggested that MMP2 had β-secretase-like activity>>70<<. Furthermore, the presence of immunoreactive TIMP in plaques of Alzheimer's disease led to the speculation that an MMP was excessively produced or activated in the plaques, as TIMPs have high affinity for MMPs and would therefore localize
n3:mentions
n2:8543065
Subject Item
_:vb236083
rdf:type
n3:Context
rdf:value
TIMP in plaques of Alzheimer's disease led to the speculation that an MMP was excessively produced or activated in the plaques, as TIMPs have high affinity for MMPs and would therefore localize to sites of protease activity>>71<<. It was subsequently suggested that the α-secretase activity was mediated by a non-MMP metalloproteinase, largely on the basis of studies using pharmacological inhibitors72.
n3:mentions
n2:7815076
Subject Item
_:vb236084
rdf:type
n3:Context
rdf:value
It was subsequently suggested that the α-secretase activity was mediated by a non-MMP metalloproteinase, largely on the basis of studies using pharmacological inhibitors>>72<<. Indeed, there is now good evidence for ADAM10 (Ref. 73) and ADAM17 (Ref. 74) as α-secretases. If this proves to be the case, these ADAMs could have a protective action against Alzheimer's disease, as they would funnel APP towards the
n3:mentions
n2:9045694
Subject Item
_:vb236085
rdf:type
n3:Context
rdf:value
Indeed, there is now good evidence for ADAM10 (Ref. >>73<<) and ADAM17 (Ref. 74) as α-secretases.
n3:mentions
n2:10097139
Subject Item
_:vb236086
rdf:type
n3:Context
rdf:value
suggested that the α-secretase activity was mediated by a non-MMP metalloproteinase, largely on the basis of studies using pharmacological inhibitors72. Indeed, there is now good evidence for ADAM10 (Ref. 73) and ADAM17 (Ref. >>74<<) as α-secretases. If this proves to be the case, these ADAMs could have a protective action against Alzheimer's disease, as they would funnel APP towards the non-amyloidogenic pathway.
n3:mentions
n2:9774383
Subject Item
_:vb236087
rdf:type
n3:Context
rdf:value
Recently, hippocampal neurons that are immunoreactive for ADAM1 and -2 were detected in Alzheimer's disease patients but not in age-matched controls>>75<<. In addition, levels of these proteins were also elevated75.
n3:mentions
n2:10686596
Subject Item
_:vb236088
rdf:type
n3:Context
rdf:value
Recently, hippocampal neurons that are immunoreactive for ADAM1 and -2 were detected in Alzheimer's disease patients but not in age-matched controls75. In addition, levels of these proteins were also elevated>>75<<.
n3:mentions
n2:10686596
Subject Item
_:vb236089
rdf:type
n3:Context
rdf:value
MMPs are also implicated in other diseases of the nervous system, including inflammatory myopathies>>76<< and peripheral nerve axotomy. The involvement of MMPs in degenerative diseases of the CNS, including AMYOTROPHIC LATERAL SCLEROSIS, is an area of increasing interest.
n3:mentions
n2:11157561
Subject Item
_:vb236090
rdf:type
n3:Context
rdf:value
For example, some MMPs and TIMPs are expressed in the CNS during development>>77<<,78, pointing to their possible importance in brain maturation.
n3:mentions
n2:10366632
Subject Item
_:vb236091
rdf:type
n3:Context
rdf:value
For example, some MMPs and TIMPs are expressed in the CNS during development77,>>78<<, pointing to their possible importance in brain maturation.
n3:mentions
n2:11044612
Subject Item
_:vb236092
rdf:type
n3:Context
rdf:value
Furthermore, MMPs are rapidly upregulated after nearly all types of injury to the CNS, including trauma>>19<<,79, indicating their possible relevance in tissue repair.
n3:mentions
n2:10878594
Subject Item
_:vb236093
rdf:type
n3:Context
rdf:value
Furthermore, MMPs are rapidly upregulated after nearly all types of injury to the CNS, including trauma19,>>79<<, indicating their possible relevance in tissue repair.
n3:mentions
n2:11150324
Subject Item
_:vb236094
rdf:type
n3:Context
rdf:value
MMPs in modulating the motility of cells across tissue matrices, metalloproteinases might regulate the migration of precursor cells to their destinations during neural development. Neural stem cells express MMP2 and all four TIMPs (Ref. >>80<<), and the migration of an oligodendrocyte progenitor requires MMP activity in vitro.
n3:mentions
n2:10203333
Subject Item
_:vb236095
rdf:type
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Neural stem cells express MMP2 and all four TIMPs (Ref. 80), and the migration of an oligodendrocyte progenitor requires MMP activity in vitro. The protein NOTCH affects cell-fate decisions in neurogenesis, and both ADAM10 (Ref. >>81<<,82) and ADAM17 (Ref. 83) have been shown to activate the notch signalling cascade.
n3:mentions
n2:9244301
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Neural stem cells express MMP2 and all four TIMPs (Ref. 80), and the migration of an oligodendrocyte progenitor requires MMP activity in vitro. The protein NOTCH affects cell-fate decisions in neurogenesis, and both ADAM10 (Ref. 81,>>82<<) and ADAM17 (Ref. 83) have been shown to activate the notch signalling cascade.
n3:mentions
n2:9872749
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81,82) and ADAM17 (Ref. >>83<<) have been shown to activate the notch signalling cascade.
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Furthermore, the inhibition of MMP activity in vitro prevented the extension of oligodendroglial processes>>84<<. Other metalloproteinases could also regulate myelinogenesis, but this remains to be tested. The rabbit corpus callosum expresses MMP1 and -3 before and during myelination85, whereas ADAM10 is expressed in oligodendrocytes before and
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n2:10493747
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The rabbit corpus callosum expresses MMP1 and -3 before and during myelination>>85<<, whereas ADAM10 is expressed in oligodendrocytes before and during myelinogenesis8.
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n2:7656427
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The rabbit corpus callosum expresses MMP1 and -3 before and during myelination85, whereas ADAM10 is expressed in oligodendrocytes before and during myelinogenesis>>8<<.
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n2:1383841
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Early studies noted the presence of proteolytic activity at neuronal growth cones during attachment and reattachment events>>86<<. Some of the activity is probably contributed by metalloproteinases, as interference with MMP activity inhibited growth-cone motility87. Inducers of neuronal differentiation and axonal outgrowth, such as nerve growth factor, laminin or
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n2:2989045
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Some of the activity is probably contributed by metalloproteinases, as interference with MMP activity inhibited growth-cone motility>>87<<. Inducers of neuronal differentiation and axonal outgrowth, such as nerve growth factor, laminin or retinoic acid, enhanced the expression of MMP2, -3 and -9 by dorsal root ganglion (DRG) neurons, PC12 and neuroblastoma cells88,89.
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n2:8081016
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Inducers of neuronal differentiation and axonal outgrowth, such as nerve growth factor, laminin or retinoic acid, enhanced the expression of MMP2, -3 and -9 by dorsal root ganglion (DRG) neurons, PC12 and neuroblastoma cells>>88<<,89. Furthermore, growth cones of PC12 cells that stably expressed MMP3 had a reduced capacity to penetrate a reconstituted basement membrane. In vivo, Drosophila melanogaster flies that carry mutations in the protein Kuzbanian (the
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n2:2560648
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Inducers of neuronal differentiation and axonal outgrowth, such as nerve growth factor, laminin or retinoic acid, enhanced the expression of MMP2, -3 and -9 by dorsal root ganglion (DRG) neurons, PC12 and neuroblastoma cells88,>>89<<. Furthermore, growth cones of PC12 cells that stably expressed MMP3 had a reduced capacity to penetrate a reconstituted basement membrane.
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In vivo, Drosophila melanogaster flies that carry mutations in the protein Kuzbanian (the mammalian homologue is ADAM10) show axon stalling during development>>90<<. In a study in which neuritic outgrowth of DRG neurons that grow on top of normal adult nerves was evaluated, the slow neurite elongation was further reduced by treatment with metalloproteinase inhibitors91. By contrast, pretreating the
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n2:8917574
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In a study in which neuritic outgrowth of DRG neurons that grow on top of normal adult nerves was evaluated, the slow neurite elongation was further reduced by treatment with metalloproteinase inhibitors>>91<<. By contrast, pretreating the nerves with recombinant MMP2 accelerated neurite growth91. Further studies led to the conclusion that DRG neurons expressed MMP2 that degraded and inactivated the neurite-inhibiting activity of CHONDROITIN
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n2:9651203
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By contrast, pretreating the nerves with recombinant MMP2 accelerated neurite growth>>91<<. Further studies led to the conclusion that DRG neurons expressed MMP2 that degraded and inactivated the neurite-inhibiting activity of CHONDROITIN SULPHATE PROTEOGLYCANS present on nerves, leading to the exposure of permissive laminin
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to the conclusion that DRG neurons expressed MMP2 that degraded and inactivated the neurite-inhibiting activity of CHONDROITIN SULPHATE PROTEOGLYCANS present on nerves, leading to the exposure of permissive laminin for neurite outgrowth>>91<<. Indeed, cleavage of a specific peptide bond in an ECM molecule leads to profound functional changes in other systems.
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For example, the cleavage of the Ala586–Leu587 bond in the α2 chain of laminin-5 by MMP2 induced migration of breast epithelial cells by exposing a cryptic pro-migratory site on laminin-5 (Ref. >>92<<). The biologically active sites in matrix molecules that become exposed after structural or conformational alterations have been called 'matricryptic sites', and the name matricryptins has been used to describe the resulting ECM fragments
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concordance with the activity of MMP2 on proteoglycans described above, metalloproteinases might be used in the CNS to destroy other inhibitory proteins. C6 glioma cells and fibroblasts transfected with MT1-MMP could digest NI250 (Ref. >>55<<), a Nogo protein identified as one of the most potent inhibitors of axonal elongation.
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on the surface of another cell, this facilitates the adherence of the cells to each other and bidirectional signalling to occur. The growth cone then overcomes these adhesive forces and breaks away from the ephrin surface. Hattori et al.>>93<< showed that the adhesive ephrin–Eph interaction is broken in vitro by ADAM10, which becomes activated after engagement of the Eph receptor.
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When axon outgrowth from embryonic dorsal spinal explants was evaluated in vitro, the facilitatory activity of netrin 1 was potentiated by IC3 and GM6001, hydroxamate metalloproteinase inhibitors>>94<<. It was found that DCC was shed from the cell surface by the activity of an unidentified MMP; preventing the ectodomain shedding of DCC with a metalloproteinase inhibitor resulted in responsiveness to netrin 1 (Ref. 94). The recent report
n3:mentions
n2:10958786
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inhibitors94. It was found that DCC was shed from the cell surface by the activity of an unidentified MMP; preventing the ectodomain shedding of DCC with a metalloproteinase inhibitor resulted in responsiveness to netrin 1 (Ref. >>94<<). The recent report of a phenotype-based GENE-TRAP screen to identify genes that control wiring patterns in the mouse CNS further implicates metalloproteinases in axonal guidance.
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ADAM23 was one of the genes identified in this screening; its inactivation in vivo led to neurological defects, tremor and ataxia>>95<<.
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n2:11242070
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Regulation of synaptic plasticity could also be another function of metalloproteinases in CNS injury>>77<<. Of interest, MMP1, -2, -3 and -9 were upregulated after spinal-cord transection in the AXOLOTL during the period of regeneration and subsided when recovery was near completion97.
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n2:10366632
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Of interest, MMP1, -2, -3 and -9 were upregulated after spinal-cord transection in the AXOLOTL during the period of regeneration and subsided when recovery was near completion>>97<<.
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n2:11013020
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The prolonged incubation of IL-1β with MMP3, and to a lesser extent MMP2 and -9, resulted in IL-1β degradation>>98<<. Furthermore, MMP2 binds to the chemokine MCP3 (macrophage chemoattractant protein 3) and cleaves its first four amino-terminal amino acids. The cleaved MCP3 binds to several chemokine receptors, acting as an antagonist99. So, MMPs
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n2:8663297
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The cleaved MCP3 binds to several chemokine receptors, acting as an antagonist>>99<<. So, MMPs expressed in the CNS might serve to abolish a chemotactic gradient for leukocyte entry. Interestingly, MMP9 has been reported to truncate the amino terminus of IL-8, leading to a 30-fold potentiation of IL-8 activity100.
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Interestingly, MMP9 has been reported to truncate the amino terminus of IL-8, leading to a 30-fold potentiation of IL-8 activity>>100<<. Conversely, MMP9 degraded chemokines, such as gro-α, leaving RANTES (also known as SCYA5) and MCP2 intact100.
n3:mentions
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Conversely, MMP9 degraded chemokines, such as gro-α, leaving RANTES (also known as SCYA5) and MCP2 intact>>100<<.
n3:mentions
n2:11023497
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Many of the pharmacological inhibitors that are available at present lack specificity towards members of a subfamily and will often antagonize the activity of members of different metalloproteinase families>>10<<,11. So, when functions are ascribed to particular metalloproteinases, it has to be clear, not only which metalloproteinase is involved, but also whether one is dealing with the right subfamily of metzincin metalloproteinases. Clearly, the
n3:mentions
n2:9920899
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Many of the pharmacological inhibitors that are available at present lack specificity towards members of a subfamily and will often antagonize the activity of members of different metalloproteinase families10,>>11<<. So, when functions are ascribed to particular metalloproteinases, it has to be clear, not only which metalloproteinase is involved, but also whether one is dealing with the right subfamily of metzincin metalloproteinases. Clearly, the
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