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MMP7 shedding of syndecan-1 (show SDC1 Proteins)/CXCL1 (show CXCL1 Proteins) complexes functions as a checkpoint that restricts neutrophil activation at sites of epithelial injury.
MMP7 exerts a restrictive role on H. pylori-induced gastric injury and the development of premalignant lesions by suppressing M1 macrophage polarization.
absence of MMP7 protects mice from LPS (show TLR4 Proteins)-induced intestinal permeability and lethality.
regulator of beta-catenin (show CTNNB1 Proteins) function in injured lung epithelium
Angiotensin II suppresses RECK (show RECK Proteins), but induces matrix metalloproteinases both in vivo and in vitro.
MMP7 regulated ciliated cell formation.
SPARC (show SPARC Proteins) suppresses angiogenesis of gastric cancer by down-regulating the expression of VEGF (show VEGFA Proteins) and MMP-7
Protein expression levels of MMP-7, MMP-14 and ERK1/2 phosphorylation level were all elevated with the increasing pathological grades in brain glioma tissues.
levels of renal MMP-7 correlate with Wnt (show WNT2 Proteins)/beta-catenin (show CTNNB1 Proteins) activity.
STAT3 (show STAT3 Proteins) plays an important role in regulation of tumor growth, invasion, and angiogenesis, which could be act by reducing MMP-7 expression in pancreatic cancer cells.
Matrix Metalloproteinase-7 Promoter polymorphism is associated with breast Cancer.
Data suggest that the cytoplasmic domain of Sdc2 (show SDC2 Proteins) is involved in regulation of expression of MMP7 in colon carcinoma/adenocarcinoma cells; induction of MMP7 involves protein kinase C gamma (show PRKCG Proteins)-mediated FAK (show PTK2 Proteins)/ERK (show EPHB2 Proteins) signaling. (Sdc2 (show SDC2 Proteins) = syndecan-2 (show SDC2 Proteins); MMP7 = matrix metalloproteinase-7; FAK (show PTK2 Proteins) = focal adhesion kinase 1 (show PTK2 Proteins))
We conclude that in the resected esophageal cancer an increased mRNA expression of MMP-7, MMP-10 (show MMP10 Proteins) and TIMP-1 (show TIMP1 Proteins) correlated with clinicopathologic features. We suggest that these genes may play a role during progression of the disease MMP-10 (show MMP10 Proteins), MMP-7, TIMP-1 (show TIMP1 Proteins), TIMP-2 (show TIMP2 Proteins) were overexpressed in 73%, 85%, 55% and 42% of esophageal cancer samples, respectively.
plasma concentrations of MMP-7, MMP-8 (show MMP8 Proteins), -9 and TIMP-1 (show TIMP1 Proteins) within 96 h from the onset of acute pancreatitis symptoms are elevated in acute pancreatitis patients compared with healthy controls
ZnCo-heterobimetallic analog of cdMMP7 with Co(II) bound in the catalytic site was prepared and characterized. This study describes a well-characterized analog of MMP7 that is available for future inhibitor design efforts.
data suggest that syndecan-2 (show SDC2 Proteins) induces extracellular shedding of E-cadherin (show CDH1 Proteins) and supports the acquisition of a fibroblast-like morphology by regulating MMP-7 expression in a colon cancer cell line
There were no statistically significant differences in the distribution of MMP7 -181 A/G and MMP12 (show MMP12 Proteins) -82 A/G genotype, allele, or haplotype frequencies between IRSA patients and controls, as well as patients' primary and secondary idiopathic recurrent spontaneous abortion
No significant differences were found between MMP-7 A-181G, C-115T, and TIMP-2 (show TIMP2 Proteins) G-418C polymorphism and coronary artery disease and myocardial infarction in a Turkish population.
In summary, our study demonstrates that IL-7 (show IL7 Proteins)/IL-7R axis promotes the invasion and migration of prostate cancer cells, through activation of AKT (show AKT1 Proteins)/NF-kappaB (show NFKB1 Proteins) pathway and upregulation of MMP-3 (show MMP3 Proteins) and MMP-7 expression
MMP-7 is a stable neutral hydrophilic secreted protein, and it may play a vital role in the invasion and metastasis of cancer cells.
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades proteoglycans, fibronectin, elastin and casein and differs from most MMP family members in that it lacks a conserved C-terminal protein domain. The enzyme is involved in wound healing, and studies in mice suggest that it regulates the activity of defensins in intestinal mucosa. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.
, matrilysin, uterine
, matrix metalloproteinase 7
, matrix metalloproteinase-7
, pump-1 protease
, uterine metalloproteinase
, Matrix metalloproteinase 7 (matrilysin)
, matrix metalloproteinase 7 (matrilysin, uterine)
, uterine matrilysin
, matrilysin-related protein