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Matrix metallopeptidase 10

MMP-10, Matrix Metalloproteinase 10, stromelysin-2
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 and fibronectin. 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-3, MMP-9, matrix metalloproteinase, MMP-2, MMP-7
Papers using MMP-10 antibodies
Th2-predominant inflammation and blockade of IFN-gamma signaling induce aneurysms in allografted aortas
Kirchmair Rudolf, In PLoS ONE, 2003
... and the following antibodies; CD68, Dako M0876; MMP-1, Millipore MAB3307; MMP10, R& D MAB9101; COX-2, Abcam AB15191 and NF-κB, Abcam, ...
Papers on MMP-10
Comparative Characterization of Vaginal Cells Derived From Premenopausal Women With and Without Severe Pelvic Organ Prolapse.
Shynlova et al., Toronto, Canada. In Reprod Sci, Feb 2016
increased transcript levels of collagen VII, multiple matrix metalloproteinases (MMP3, MMP7, MMP10, MMP12, MMP13, and MMP14), integrins (ITGA1, ITGA4, ITGA6, ITGA8, ITGB1, ITGB2, and ITGB3), and cell adhesion molecules as compared to control-HVCs.
Body Water Status and Short-term Maximal Power Output during a Multistage Road Bicycle Race (Giro d'Italia 2014).
Gatterer et al., Monza, Italy. In Int J Sports Med, Jan 2016
The shortening of the vector was negatively related to MMP10 (r=- 0.749, p=0.032) and MMP15 (r=- 0.735, p=0.038) during stage 16 (heavy mountain-stage) and MMP60 (r=- 0.751, p=0.032),
Over expression of p21-activated kinase 7 associates with lymph node metastasis in esophageal squamous cell cancers.
Zhu et al., In Cancer Biomark, Jan 2016
PAK7 could enhance the protein levels of Vimentin and MMP10, but reduce E-cadherin, TIMP1 and TIMP2.
miRNA and target gene expression in menstrual endometria and early pregnancy decidua.
Wang et al., Hohhot, China. In Eur J Obstet Gynecol Reprod Biol, Dec 2015
METHODS: Quantitative reverse transcription-polymerase chain reaction (qRT-PCR) was used to measure the expression of the miR-146b-5p, miR-181b-5p, miR-424, miR-532, miR-199a-3p, miR-423, miR-22-3p, let-7i-5p, and miR-1 and the predicted target genes IGF2R, LEPR, SGK1, MMP2, MMP10, LIF, IL6, and STAT3 in menstrual endometria and early pregnancy decidua.
Orally administered extract from Prunella vulgaris attenuates spontaneous colitis in mdr1a(-/-) mice.
Wannemuehler et al., Ames, United States. In World J Gastrointest Pharmacol Ther, Dec 2015
Oral administration of the P. vulgaris extract resulted in reduced (P < 0.05) serum levels of IL-10 (4.6 ± 2 vs 19.4 ± 4), CXCL9 (1319.0 ± 277 vs 3901.0 ± 858), and TNFα (9.9 ± 3 vs 14.8 ± 1) as well as reduced gene expression by more than two-fold for Ccl2, Ccl20, Cxcl1, Cxcl9, IL-1α, Mmp10, VCAM-1, ICAM, IL-2, and TNFα in the colonic mucosa of mdr1a(-/-) mice compared to vehicle-treated mdr1a(-/-) mice.
Matrix metalloproteinase genes on chromosome 11q22 and risk of carpal tunnel syndrome.
Collins et al., Cape Town, South Africa. In Rheumatol Int, Dec 2015
Variants within the MMP10, MMP1, MMP3 and MMP12 gene cluster on chromosome 11q22 have been associated with connective tissue injuries.
Matrix Metalloproteinases as Therapeutic Targets for Idiopathic Pulmonary Fibrosis.
Owen et al., Albuquerque, United States. In Am J Respir Cell Mol Biol, Nov 2015
These mechanisms include MMPs: (1) promoting epithelial-to-mesenchymal transition (MMP-3 and MMP-7); (2) increasing lung levels or activity of profibrotic mediators or reducing lung levels of antifibrotic mediators (MMP-3, MMP-7, and MMP-8); (3) promoting abnormal epithelial cell migration and other aberrant repair processes (MMP-3 and MMP-9); (4) inducing the switching of lung macrophage phenotypes from M1 to M2 types (MMP-10 and MMP-28); and (5) promoting fibrocyte migration (MMP-8).
Normal and Cystic Fibrosis Human Bronchial Epithelial Cells Infected with Pseudomonas aeruginosa Exhibit Distinct Gene Activation Patterns.
Guillot et al., Paris, France. In Plos One, 2014
Finally, we established that the protein products of the genes exhibiting the greatest differential upregulation (CSF2, CCL2, TNF, CSF3, MMP1, and MMP10) between CF patients and CTRL were produced in higher amounts by infected cells from CF patients versus CTRL.
Protein Expression of Stromelysin-2 in Head and Neck Squamous Cell Carcinomas.
Ghodsi et al., Zāhedān, Iran. In Asian Pac J Cancer Prev, 2014
However, there are few studies on association between stromelysin-2 (ST-2) and invasive behavior of HNSCC.
Proteinases and plaque rupture: unblocking the road to translation.
Newby, Bristol, United Kingdom. In Curr Opin Lipidol, 2014
Novel targets, including MMP-8, MMP-10, MMP-14, MMP-19, MMP-25 and MMP-28, are also being considered.
Proteases and small intestinal barrier function in health and disease.
MacDonald et al., London, United Kingdom. In Curr Opin Gastroenterol, 2014
RECENT FINDINGS: It is now well established that intestinal proteases, such as matrix metalloproteinase (MMP)-1, MMP-3, MMP-10 and MMP-12, are key players in the development of ulcers in inflammatory bowel disease, have direct effects on epithelial barrier function and are involved in epithelial restitution.
The association of genetic variants of matrix metalloproteinases with abdominal aortic aneurysm: a systematic review and meta-analysis.
Golledge et al., Townsville, Australia. In Heart, 2014
No associations with AAA were identified for other SNPs assessed in this study including rs1799750 (MMP1), rs3918242 (MMP9), rs486055 (MMP10), rs2276109 (MMP12), rs2252070 (MMP13), rs4898 (TIMP1) or rs9619311 (TIMP3).
Effects of diabetes on the eye.
Lutty, Baltimore, United States. In Invest Ophthalmol Vis Sci, 2013
Gene therapies upregulating MNNG HOS transforming gene (cMet) and/or downregulating MMP10 and cathepsin S are potential future therapies for diabetic keratopathy.
Synergistic effect of thrombin and CD40 ligand on endothelial matrix metalloproteinase-10 expression and microparticle generation in vitro and in vivo.
Orbe et al., Pamplona, Spain. In Arterioscler Thromb Vasc Biol, 2012
Thrombin/CD40L elicited a strong synergistic effect on endothelial MMP-10 expression and microparticles containing MMP-10 in vitro and in vivo, which may represent a new link between inflammation/thrombosis with prognostic implications.
Matrix metalloproteinase-10 (MMP-10) interaction with tissue inhibitors of metalloproteinases TIMP-1 and TIMP-2: binding studies and crystal structure.
Radisky et al., Jacksonville, United States. In J Biol Chem, 2012
Data show that TIMP-1 inhibits the MMP-10 with a K(i) of 1.1 x 10(-9) M, and TIMP-2 inhibits the MMP-10 with a K(i) of 5.8 x 10(-9) M.
Matrix metalloproteinase-10 effectively reduces infarct size in experimental stroke by enhancing fibrinolysis via a thrombin-activatable fibrinolysis inhibitor-mediated mechanism.
Páramo et al., Pamplona, Spain. In Circulation, 2012
MMP-10 was capable of enhancing tissue plasminogen activator-induced fibrinolysis via a thrombin-activatable fibrinolysis inhibitor inactivation-mediated mechanism.
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-10 is associated with malignant pleural effusion.
Matrix metalloproteinase-10 is required for lung cancer stem cell maintenance, tumor initiation and metastatic potential.
Fields et al., Jacksonville, United States. In Plos One, 2011
Mmp10 is required for maintenance of a highly tumorigenic, cancer-initiating, metastatic stem-like cell population in lung cancer.
Histone deacetylase 7 maintains vascular integrity by repressing matrix metalloproteinase 10.
Olson et al., Dallas, United States. In Cell, 2006
HDAC7 represses MMP10 gene transcription by associating with myocyte enhancer factor-2 (MEF2), a direct activator of MMP10 transcription and essential regulator of blood vessel development.
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