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The authors show that the antimicrobial peptide alpha-defensin is functionally sustained during nutrient deprivation because of regulation of the defensin-processing enzyme MMP7 by microbiota- and host-derived factors. Sustained Mmp7 expression requires the microbiota and is mediated by de-repression of the transcription activator Atoh1 upon attenuation of the transcriptional repressor Hes1 in intestinal epithelial cells.
Combined Mmp-7 Deletion and N-cadherin Mimetic (EC4-Fc) Over-Expression is associated with Aneurysm Severity.
upregulating MMP7 levels may be key to remove remyelination-impairing fibronectin aggregates in multiple sclerosis lesions
MMP7 shedding of syndecan-1/CXCL1 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-induced intestinal permeability and lethality.
regulator of beta-catenin function in injured lung epithelium
Angiotensin II suppresses RECK, but induces matrix metalloproteinases both in vivo and in vitro.
MMP7 regulated ciliated cell formation.
SPARC suppresses angiogenesis of gastric cancer by down-regulating the expression of VEGF 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/beta-catenin activity.
STAT3 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.
expression in pancreatic ductal adenocarcinoma cells and that MMP7 deletion limits tumor size and metastasis in mice
MMP-2 mediates Ang II-induced hypertension and is transcriptionally controlled by 2 other metalloproteinases, MMP-7 and TACE.
MMP-7 is involved in the cleavage of N-cadherin and modulates vascular smooth muscle cell apoptosis, and may contribute to atherosclerotic plaque development and rupture.
matrilysin regulates pulmonary localization of dendritic cells that express CD103
H. pylori-mediated induction of MMP-7 may serve to protect the gastric mucosa from pathophysiologic processes that promote carcinogenesis.
MMP7 shedding of syndecan-1 facilitates wound closure by causing the alpha(2)beta(1) integrin to assume a less active conformation thereby removing restrictions to migration
Gene expression analysis reveals matrilysin as a key regulator of pulmonary fibrosis in mice and humans.
Knockdown of Sema3A prevented Domain IV-3-induced tumoroid formation and Sema3A was sensitive to MMP-7 proteolysis. The perlecan-Sema3A complex abrogates FAK activity and stabilizes PCa cell interactions.
Increased MMP7 expression is associated with membrane rupture at parturition.
High serum level of MMP-7 was associated with increased risk of incident spontaneous subarachnoid hemorrhage, independently of the main risk factors for subarachnoid hemorrhage.
Plasma OPN + MMP7 + PSG9 elevation in combination was a prognostic factor for overall survival in hepatocellular carcinoma
we compared the expression of MMP1, MMP2, MMP7, and MMP9, well known as secreted MMPs, and found that MMP expression varied in lesions with different histological grade,histological subtype, and type of invasion.
MMP7 expression is regulated by Hes3 in lung cancer cells.
Blood concentrations of MMP2 and MMP7 did not distinguish between different types of endocarditis
This study shows expression of matrix metalloproteinase7 is associated with the progressive epithelial changes that characterize the transformation of normal squamous epithelium through the preneoplastic condition of Barrett's esophagus to esophageal adenocarcinoma.
Low level of MMP2 and high level of MMP7 in the plasma of gastric adenocarcinoma patients correlated with poor overall survival.
MMP1 rs1799750 1G/2G genotype was found to play a significant role in the development of exudative AMD at the age of less than 65 years. IL-1beta concentration was significantly higher in exudative AMD patients for MMP1 rs1799750 1G/1G genotype and MMP7 rs11568818 A/G genotype compared with control group subjects.
Comparatively lower expression of MMP-7 in gastric mucosal inflammation and imbalanced expression of TIMP-1 might be two of the pathogeneses of chronic stomach disease
EGFR-mediated matrix metalloproteinase-7 up-regulation promotes epithelial-mesenchymal transition via ERK1-AP1 axis during ovarian endometriosis progression.
PRL-3 promotes glioblastoma progression by enhancing MMP7 through the ERK and JNK pathways.
The results of this study suggest that the two MMP-7 polymorphisms, - A-181G and C-153T, do not play a major role in determining personal susceptibility to bladder cancer in Taiwan.
Results suggest a significant correlation of higher serum zinc levels with the diagnosis of prostate cancer. The polymorphism rs11568818 in MMP-7 gene was also associated with an increased prostate cancer risk in Poland.
the results indicated that changes in MMP7 sensitivity, attributable to mutant AA, have the potential of identifying patients with distinct survival outcomes as well as patients with cancer specimen immune activity.
CTHRC1 serves as a pro-metastatic gene that contributes to NSCLC invasion and metastasis, which are mediated by upregulated MMP7 and MMP9 expression. Targeting CTHRC1 may be beneficial for inhibiting NSCLC metastasis.
no difference in the expression of MMP-7 and TIMP-1 in the endometrium in relation to hormone levels and menstrual cycle phases were observed
MMP-7 A-181G may play an indirect role in determining personal susceptibility to Colorectal Cancer.
Results provide evidence that MMP7 expression is regulated by leptin through ERK and JNK pathways to modulate cell invasion of ovarian neoplasm.
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