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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 16 Apr 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, CAN, HAD, 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
Supplier
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
Osteopontin exacerbates pulmonary damage in influenzal lung injury.
New
Diao et al., In Jpn J Infect Dis, 10 May 2015
The epithelial sodium channel (ENaC) is the main mechanism of clearance of pulmonary edema fluid and matrix metalloproteinase7 (MMP7) is able to degrade extracellular matrix.
Matrix Metalloproteinase Expression in Contusional Traumatic Brain Injury: A Paired Microdialysis Study.
New
Hutchinson et al., Cambridge, United Kingdom. In J Neurotrauma, 09 May 2015
Overall, there was a gradual increase in MMP-7 concentrations in both 'normal' and injured brain over the monitoring period, although this was not consistent in every patient.
Association of MMP7-181A/G promoter polymorphism with gastric cancer risk: Influence of nicotine in differential allele-specific transcription via increased phosphorylation of CREB.
New
Swarnakar et al., India. In J Biol Chem, 06 May 2015
UNASSIGNED: Elevated expression of matrix metalloproteinase7 (MMP7) has been demonstrated to play a pivotal role in cancer invasion.
Matrix Remodeling by MMPs during Wound Repair.
Review
New
Parks et al., Los Angeles, United States. In Matrix Biol, 11 Apr 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.
Review
New
Lv et al., Changchun, China. In Cancer Epidemiol, 09 Mar 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).
Immunohistochemical Similarities between Lichen Sclerosus et Atrophicus and Morphea: A Case Study.
New
Aiba et al., Sendai, Japan. In Case Rep Dermatol, Jan 2015
In this report, we describe a case of LSA on the abdomen accompanied by morphea; we employed immunohistochemical staining for periostin as well as MMP-7 and MMP-28, both of which are reported to facilitate fibrosis in the development of various organs, including skin.
Imbalance of the nerve growth factor and its precursor as a potential biomarker for diabetic retinopathy.
New
El-Remessy et al., Augusta, United States. In Biomed Res Int, Dec 2014
MMP-7 activity was also assayed.
Alcohol consumption, Wnt/β-catenin signaling, and hepatocarcinogenesis.
Review
New
Ronis et al., Little Rock, United States. In Adv Exp Med Biol, Dec 2014
significant upregulation of soluble Wnts, Wnt2, and Wnt7a, and increased expression of several β-catenin targets involved in tumor promotion and progression, cyclin D1, c-myc, WISP1, and MMP7 (p<0.05).
Inflammation-related factors predicting prognosis of gastric cancer.
Review
New
Cao et al., Shanghai, China. In World J Gastroenterol, May 2014
Increased serum levels of matrix metalloproteinases (MMP)-3, MMP-7, and MMP-11 and increased levels of MMP-9, MMP-12, and MMP-21 in tumors are consistently associated with poor survival of GC.
A systematic review and meta-analysis of diagnostic and prognostic serum biomarkers of colorectal cancer.
Review
Gao et al., Luoyang, China. In Plos One, 2013
and MMP-7 with lowest (1.099, CI: 1.018-1.187))
Association between the MUC5B promoter polymorphism and survival in patients with idiopathic pulmonary fibrosis.
Impact
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.
GeneRIF
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.
GeneRIF
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.
GeneRIF
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.
GeneRIF
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.
GeneRIF
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.
Impact
GeneRIF
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.
Impact
GeneRIF
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.
Impact
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.
Impact
GeneRIF
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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