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1 so target, Matrix metalloproteinase-7 (MMP-7/Matrilysin).
2 ursors by matrix metalloproteinase-7 (MMP-7; matrilysin).
3 r two MMPs, MMP-3 (stromelysin-1) and MMP-7 (matrilysin).
4 r epithelia in the prostate also overexpress matrilysin.
5 thus be exploited to yield metallohybrids of matrilysin.
6 es that are more similar to stromelysin than matrilysin.
7 arterectomy tissue in organ culture released matrilysin.
8 ith Leu in subsite P1' relative to wild type matrilysin.
9 MAT:A215V are similar to those of wild type matrilysin.
10 TIMP-1 inhibits re-epithelialization through matrilysin.
11 ctors enhance the activation and activity of matrilysin.
12 r pocket found in fibroblast collagenase and matrilysin.
13 ecific cleavage of the beta(4) integrin with matrilysin.
18 strate that there is increased expression of matrilysin-1 in human lesions and BOA in the CC10-human
20 haete-scute homolog-1 mice were crossed with matrilysin-1 null mice and was correlated with reduced m
22 d HPLD1 cells, which do not normally express matrilysin-1, promoted cellular migration, suggesting a
24 trix metalloproteinase-26 (MMP-26/endometase/matrilysin-2) is a newly identified MMP and its structur
25 We previously reported that human endometase/matrilysin-2/matrix metalloproteinase (MMP) 26-mediated
27 ve biochemical mechanism by which endometase/matrilysin-2/matrix metalloproteinase-26 (MMP-26) may pr
30 ions demonstrate that sulfated GAGs regulate matrilysin activation and its activity against specific
32 with matrix metalloproteinases and regulates matrilysin activity during airway epithelial repair.
33 ts airway re-epithelialization by inhibiting matrilysin activity, contributing to a stereotypic injur
34 itin-2,6-sulfate (CS-D) also did not enhance matrilysin activity, suggesting that the presentation of
35 identify E-cadherin as a novel substrate for matrilysin and indicate that shedding of E-cadherin ecto
39 l lines differed from the HaCaT line in that matrilysin and TIMP-1 proteins were detected in conditio
41 rated by the action of the metalloproteinase matrilysin, and suggest that matrilysin cleavage of FasL
44 single tyrosine residue in the S1' pocket of matrilysin by leucine alters its P1' specificity to rese
45 ific product of myeloperoxidase, inactivates matrilysin by modifying adjacent tryptophan and glycine
46 We have shown that inactivation of MMP-7 (matrilysin) by HOCl coincides with the formation of a no
47 we report that the matrix metalloproteinase matrilysin can process recombinant and cell-associated F
48 three His ligands and the scaffolding of the matrilysin catalytic zinc site are different from that o
49 talloproteinase matrilysin, and suggest that matrilysin cleavage of FasL is an important mediator of
54 In the involuting mouse prostate, FasL and matrilysin colocalized to the cell surface in a restrict
56 ined to sites of macrophage-elastin contact, matrilysin confers macrophages with their most potent MM
61 sure of corneal wounds were observed between matrilysin-deficient and wild-type mice after wounding.
62 vascular endothelial growth factor (VEGF) in matrilysin-deficient and wild-type mouse corneas (experi
65 re the area of corneal neovascularization in matrilysin-deficient mice and wild-type littermates (exp
66 rences in corneal neovascularization between matrilysin-deficient mice and wild-type littermates seem
67 orneal epithelial cells were not elevated in matrilysin-deficient mice compared with the wild-type mi
68 ation after excimer laser keratectomy in the matrilysin-deficient mice measured 21.3% +/- 5.2% and 18
70 The area of corneal neovascularization in matrilysin-deficient mice was not significantly differen
75 Mmp7-/-, and Mmp10-/- mice identified 2,091 matrilysin-dependent and 1,628 stromelysin-2-dependent g
81 basement membrane disruption was detected in matrilysin-expressing mice, which could account for the
82 factors secreted from monocytes could induce matrilysin expression in a human prostatic cell line.
84 , flagellin-null mutants failed to stimulate matrilysin expression in cultured cells or in lungs infe
86 e assessed if relevant CF pathogens regulate matrilysin expression in human lung epithelial cells.
88 specifically flagellin) potently stimulates matrilysin expression in lung epithelial cells and may m
95 MPs with simple domain constituents, such as matrilysin, from the larger and more elaborate enzymes.
98 tumors, leads to coordinate upregulation of matrilysin gene transcription, contributing to gastroint
100 and cell-associated FasL to sFasL, and that matrilysin-generated sFasL was effective at inducing apo
101 d expression of Bcl-2, Bcl-XL, survivin, and matrilysin, genes associated with a poor prognosis in ad
102 ence of kcat/K(m) for Dns-PLALWAR shows that matrilysin has a broad pH optimum (5.0-9.0) and the pKa
103 icity, the amino acids at these positions in matrilysin have been replaced by those found in stromely
105 tochemistry revealed prominent expression of matrilysin in cells confined to the border between acell
107 otential mechanism for the overexpression of matrilysin in inflamed ducts and glands of the prostate.
108 e of this study was to determine the role of matrilysin in maintaining corneal avascularity during wo
112 tivity of matrix metalloproteinase-7 (MMP-7, matrilysin) in vitro, suggesting that this oxidant activ
113 of stromelysin (HFS:L214Y/V215A) to resemble matrilysin increases activity (i.e., higher kcat/KM) tow
115 ls coexpressing Fas and Fas ligand (FasL) to matrilysin induces apoptosis, whereas chronic exposure t
118 use model peptides that mimic the region of matrilysin involved in this reaction, VVWGTA, VVWATA, an
122 Based on these findings, we conclude that matrilysin is a suppressor of the Min phenotype, possibl
127 ave demonstrated that one MMP family member, matrilysin, is expressed in a high percentage of early-s
128 entactin with the matrix metalloproteinase, matrilysin, liberates peptides that retain E domain-medi
129 epithelial specific matrix metalloproteinase matrilysin (MAT) has been correlated with enhanced tumor
132 elial transcriptional responses dependent on matrilysin (matrix metalloproteinase 7 [MMP-7]) and stro
133 erexpression of the matrix metalloproteinase matrilysin (matrix metalloproteinase-7) in the mouse mam
142 latinase (MMP 9), stromelysin 1 (MMP 3), and matrilysin (MMP 7) all processed this substrate efficien
143 A or B), stromelysins (MMP-3 and MMP-11), or matrilysin (MMP-7) affected SF/HGF-induced responses.
146 human matrix metalloproteinase (MMP) family, matrilysin (MMP-7) and gelatinase B/type IV collagenase
148 ate that HOCl inhibits the activity of human matrilysin (MMP-7) in vitro, suggesting that it might li
150 einases (MMPs) are tightly bound to tissues; matrilysin (MMP-7), although the smallest of the MMPs, i
151 ct of Brij-35 on human gelatinase B (MMP-9), matrilysin (MMP-7), and membrane-type 1 MMP (MT1-MMP) wa
152 pproach for rapid and sensitive detection of matrilysin (MMP-7, a biomarker involved in the degradati
153 lytically active matrix metalloproteinase 7 (matrilysin, MMP-7) and heparin-binding epidermal growth
160 s C, values closely similar to those for the matrilysin produced by activation of the Chinese hamster
161 ia (Min) mice, we propose that regulation of matrilysin production by beta-catenin accumulation is a
163 f factor, LEF-1, significantly downregulated matrilysin promoter activity, suggesting that beta-caten
164 iously observed coordinate regulation of the matrilysin promoter by beta-catenin and Ets family trans
165 gesting that beta-catenin transactivates the matrilysin promoter by virtue of its ability to abrogate
168 transfection analyses with a chimeric human matrilysin promoter-chloramphenicol acetyltransferase re
172 lysaccharide treatment substantially induced matrilysin protein and mRNA expression in LNCaP prostate
177 epithelial cells, transfection of activated matrilysin resulted in shedding of E-cadherin and accele
179 helial cells have been repeatedly exposed to matrilysin, show a significant decrease in apoptosis.
181 lation was found between mRNA expression for matrilysin, stromelysins 1-3, TIMP-1, or TIMP-3 and secr
182 ne products, a secreted phospholipase A2 and matrilysin, that has been implicated as modifiers of ade
183 omatrilysin and the activity of fully active matrilysin to cleave specific physiologic substrates.
190 s and cell culture studies demonstrated that matrilysin was secreted lumenally by lung epithelium, bu
191 teady-state reaction of wild type and mutant matrilysin with substrates with Leu and Tyr residues in
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