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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 04 Sep 2015.

Matrix metallopeptidase 7

MMP-7, Matrix Metalloproteinase 7, Matrilysin
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. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: MMP-9, MMP-2, HAD, CAN, matrix metalloproteinase
Papers using MMP-7 antibodies
A simple and fast densitometric method for the analysis of tyrosine hydroxylase immunoreactivity in the substantia nigra pars compacta and in the ventral tegmental area
Mohanraj Rajesh, In PLoS ONE, 2004
... Antibodies against SPARC (Santa Cruz Biotechnology, Santa Cruz, CA, USA), (p-)SAPK/JNK, (p-)ERK1/2, (p-)p-38, MMP-7 (Cell signaling technology, Danvers, MA,USA), VEGF, ...
Papers on MMP-7
Associations of MMP-7 and OPN gene polymorphisms with risk of coal workers' pneumoconiosis in a Chinese population: a case-control study.
Ni et al., Nanjing, China. In Inhal Toxicol, 02 Oct 2015
BACKGROUND: The matrix metalloproteinase-7 (MMP-7) and osteopontin (OPN) are both multifunctional proteins with roles in inflammation, cell proliferation, tissue remodeling and so on, implicated in the pathogenesis of numerous conditions including pulmonary fibrosis.
Wnt/β-catenin signalling and podocyte dysfunction in proteinuric kidney disease.
Liu et al., Guangzhou, China. In Nat Rev Nephrol, 30 Sep 2015
Mechanistically, Wnt/β-catenin controls the expression of several key mediators implicated in podocytopathies, including Snail1, the renin-angiotensin system and matrix metalloproteinase 7. Wnt/β-catenin also negatively regulates Wilms tumour protein, a crucial transcription factor that safeguards podocyte integrity.
Resveratrol attenuates renal injury and fibrosis by inhibiting transforming growth factor-β pathway on matrix metalloproteinase 7.
Zhou et al., Changsha, China. In Exp Biol Med (maywood), 27 Sep 2015
Matrix metalloproteinase 7 (MMP7) was reported to reduce E-cadherin and induce EMT by up-regulation of β-catenin/lymphoid enhancer-binding factor 1 (LEF1) signaling.
MMP1, 2, 3, 7, and 9 Gene Polymorphisms and Urinary Cancer Risk: A Meta-Analysis.
Chuize et al., Shenyang, China. In Genet Test Mol Biomarkers, 24 Sep 2015
Many studies have been carried out on the association between polymorphisms in the MMP1, MMP2, MMP3, MMP7, and MMP9 genes and urinary cancer risk.
Matrix remodeling by MMPs during wound repair.
Parks et al., Los Angeles, United States. In Matrix Biol, May 2015
For wound closure, we discuss how two MMPs - MMP1 in human epidermis and MMP7 in mucosal epithelia - facilitate re-epithelialization by cleaving different ECM or ECM-associated proteins to affect similar integrin:matrix adhesion.
Prognostic significance of MMP-7 expression in colorectal cancer: a meta-analysis.
Lv et al., Changchun, China. In Cancer Epidemiol, Apr 2015
OBJECTIVE: Matrix metalloproteinase-7 (MMP-7) is a member of the family of matrix metalloproteinases (MMPs); it is associated with invasive tumor growth and distant metastasis in colorectal cancer (CRC).
[Genetic and environmental aspects of mathematical disabilities].
Khusnutdinova et al., In Genetika, Mar 2015
The results of the second approach demonstrates that the matrix metalloproteinase 7 gene (MMP7), the glutamate receptor ionotropic kainate 1 gene (GRIK1), and the dynein axonemal heavy chain 5 gene (DNA H5) are responsible for developing mathematical disabilities.
MicroRNA-203 Regulates Growth and Metastasis of Breast Cancer.
Lv et al., Shijiazhuang, China. In Cell Physiol Biochem, Dec 2014
MiR203 may also inhibit cell metastasis through suppressing matrix metalloproteinase 2 (MMP2), MMP7 and MMP9.
Wnt/β-catenin signaling and kidney fibrosis.
Liu et al., Pittsburgh, United States. In Kidney Int Suppl (2011), Nov 2014
In kidney cells, Wnt/β-catenin promotes the expression of numerous fibrosis-related genes such as Snail1, plasminogen activator inhibitor-1, and matrix metalloproteinase-7.
Gene expression in the chicken caecum in response to infections with non-typhoid Salmonella.
Kyrova et al., Brno, Czech Republic. In Vet Res, 2013
The highest induction in expression is observed for matrix metalloproteinase 7 (MMP7).
Association between the MUC5B promoter polymorphism and survival in patients with idiopathic pulmonary fibrosis.
Schwartz et al., Denver, United States. In Jama, 2013
The INSPIRE cohort was used to model the association of the MUC5B genotype with survival, accounting for the effect of matrix metalloproteinase 7 (MMP-7) blood concentration and other demographic and clinical covariates.
The forkhead box transcription factor FOXC1 promotes breast cancer invasion by inducing matrix metalloprotease 7 (MMP7) expression.
Keri et al., Cleveland, United States. In J Biol Chem, 2012
Findings identify MMP7 as a novel mechanism through which FOXC1 may regulate the basal-like breast cancer invasive phenotype and the propensity of these cancers to metastasize.
Is MMP-7 gene polymorphism a possible risk factor for chronic obstructive pulmonary disease in Turkish patients.
Eraltan et al., İstanbul, Turkey. In Genet Test Mol Biomarkers, 2012
These findings have suggested that MMP-7 polymorphism might be associated with the risk and progression of COPD in the Turkish population.
The transcription factor SOX18 regulates the expression of matrix metalloproteinase 7 and guidance molecules in human endothelial cells.
de Martin et al., Vienna, Austria. In Plos One, 2011
The identification of MMP7 as a direct SOX18 target gene as well as other potential candidates including guidance molecules provides a molecular basis for the proposed function of this transcription factor in the regulation of vessel formation.
Application of MMP-7 and MMP-10 in assisting the diagnosis of malignant pleural effusion.
Li et al., Shenyang, China. In Asian Pac J Cancer Prev, 2011
High MMP-7 is associated with malignant pleural effusion.
Expressions of MMPs and TIMP-1 in gastric ulcers may differentiate H. pylori-infected from NSAID-related ulcers.
Sheu et al., Tainan City, Taiwan. In Scientificworldjournal, 2011
H. pylori-infected gastric ulcers express higher MMP-7, MMP-9, and TIMP-1 than NSAID-related ulcers
Stat3 and MMP7 contribute to pancreatic ductal adenocarcinoma initiation and progression.
Hebrok et al., San Francisco, United States. In Cancer Cell, 2011
expression in pancreatic ductal adenocarcinoma cells and that MMP7 deletion limits tumor size and metastasis in mice
Divergent functions for airway epithelial matrix metalloproteinase 7 and retinoic acid in experimental asthma.
Kheradmand et al., Houston, United States. In Nat Immunol, 2009
MMP7 coordinates allergic lung inflammation by activating interleukin 25 while simultaneously inhibiting retinoid-dependent development of regulatory T cells.
Considering the critical interface between tumor cells and stromal cells in the search for targets for anticancer therapy.
Declerck et al., Los Angeles, United States. In Cancer Cell, 2005
In this issue of Cancer Cell, a paper by Lynch et al. demonstrates how the careful study of changes that occur at the interface between tumor cells and stromal cells led to the discovery of a new function for matrix metalloproteinase-7 (MMP-7) in the formation of osteolytic lesions in prostate cancer.
MMP-7 promotes prostate cancer-induced osteolysis via the solubilization of RANKL.
Futakuchi et al., Nashville, United States. In Cancer Cell, 2005
MMP-7, which was produced by osteoclasts at the tumor-bone interface, was capable of processing RANKL to a soluble form that promoted osteoclast activation.
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