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1 on pathway of matrix prometalloproteinase-2 (pro-MMP-2).
2 nt injury disrupts the enzymatic cleavage of pro-MMP-2.
3 e proteases necessary to cleave and activate pro-MMP-2.
4 ndirectly by activating soluble MMPs such as pro-MMP-2.
5 proteolysis and physiological activators of pro-MMP-2.
7 or P4C10 antibodies stimulated MMP-dependent pro-MMP-2 activation and accumulation of a M(r) 43,000 f
8 with concanavalin A stimulated MMP-dependent pro-MMP-2 activation and accumulation of M(r) 55,000 and
9 uncation mutant MT1 Delta C with more robust pro-MMP-2 activation and cell surface expression than wi
10 3-MMP and analyzed the exchange chimeras for pro-MMP-2 activation and collagen degradation at the cel
11 MT1-MMP itself, but also for MT3-MMP in both pro-MMP-2 activation and collagenolysis, consistent with
12 rosine phosphorylation, blocked ConA-induced pro-MMP-2 activation and ConA-induced MT1-MMP mRNA level
14 MT3-MMP requires TIMP-2 to accomplish full pro-MMP-2 activation and this process is enhanced in mar
15 ergistically with TIMP-2 in the promotion of pro-MMP-2 activation by MT1-MMP in a process that depend
20 MT3-MMP and TIMP-2 or TIMP-3 suggesting that pro-MMP-2 activation by MT3-MMP involves ternary complex
21 confirmed by the dose-dependent promotion of pro-MMP-2 activation by sodium orthovanadate in the pres
22 ffect of TIMP-2 on MT1-MMP processing and on pro-MMP-2 activation in a cellular system could not be e
23 talloproteinase (MT1-MMP) (MMP-14) initiates pro-MMP-2 activation in a process that is tightly regula
24 a broad-spectrum MMP inhibitor, in enhancing pro-MMP-2 activation in cells infected to express MT1-MM
25 are less likely to promote MT1-MMP-dependent pro-MMP-2 activation in the presence of TIMP-2, while ma
26 a suggest that beta1 integrin stimulation of pro-MMP-2 activation involves MT1-MMP posttranslational
28 genolysis is not required for stimulation of pro-MMP-2 activation, and denatured collagen does not el
29 T1080 fibrosarcoma cells results in enhanced pro-MMP-2 activation, proliferation within a three-dimen
30 t catalytic domains determine the pattern of pro-MMP-2 activation, whereas pexin-like domains modulat
34 decreased secretion of pro-MMP-9, as well as pro-MMP-2 and active MMP-2 from elastase-treated male ra
37 le P4C10 antibodies stimulated expression of pro-MMP-2 and its inhibitor, tissue inhibitor of metallo
38 zymes in culture media or affinity-purified (pro-MMP-2 and MMP-9) were examined by SDS-PAGE zymograph
39 orbent assay, we observed that CSF levels of pro-MMP-2 and pro-MMP-7 were increased in association wi
40 livers did not show an increase in inactive pro-MMP-2 and pro-MMP-9 and did not contain active MMP-2
41 TIMPs) and did not activate pro-gelatinases (pro-MMP-2 and pro-MMP-9) even in the presence of exogeno
42 e inactive matrix metalloproteinases (MMPs), pro-MMP-2 and pro-MMP-9, are elevated at 30 minutes and
45 agen-induced MT1-MMP-dependent activation of pro-MMP-2 and up-regulation of MT1-MMP at the gene and p
46 MT1-MMP and TIMP-2 was capable of activating pro-MMP-2, and exogenous TIMP-2 had a biphasic effect on
53 ctivation of pro-matrix metalloproteinase-2 (pro-MMP-2) by MDA-MB-231 human breast cancer cells is ap
54 chromatography experiments demonstrated that pro-MMP-2 can assemble trimolecular complexes with a cat
55 Ala+TIMP-2 variant exhibited conformational, pro-MMP-2 complex formation and fibroblast growth modula
58 P), a novel transmembrane MMP that activates pro-MMP-2 (gelatinase A), is expressed in human atherosc
59 helial cells (HUVECs) released pro-MMP-9 and pro-MMP-2 in a constitutive manner and were not influenc
60 6001 enhance MT1-MMP-dependent activation of pro-MMP-2 in the presence of tissue inhibitor of metallo
62 h activation and autocatalytic maturation of pro-MMP-2 in trans suggest that MT1-MMP should exist as
66 ctivation of pro-matrix metalloproteinase 2 (pro-MMP-2) is considered to be critical for cell migrati
67 y demonstrates that MT1-MMP, an activator of pro-MMP-2, is expressed by SMCs and Mphi in human athero
68 s multimolecular complex formation involving pro-MMP-2, membrane type 1-MMP (MT1-MMP), and tissue inh
69 the formation of a tri-molecular complex of pro-MMP-2, MMP-14, and tissue inhibitor of metalloprotei
71 al fibroblasts with concanavalin A activates pro-MMP-2 on the cell surface by converting it to the 65
73 trix metalloproteinase-1 that then activates pro-MMP-2-promoting migration and extracellular matrix i
74 or study showed that MMP-2 activity, but not pro-MMP-2 protein, decreases after RPE oxidative injury,
75 inity for pro-MMP-9 than for active MMP-9 or pro-MMP-2, requiring the N-terminal propeptide domain of
76 MP promotes matrix degradation by activating pro-MMP-2, these results suggest a novel mechanism where
81 ha(3)beta(1) strongly promotes activation of pro-MMP-2, whereas alpha(2)beta(1) integrin clustering h
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