gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 22 May 2015.

Matrix metallopeptidase 3

MMP-3, Matrix Metalloproteinase 3, stromelysin-1, MEF2
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. This gene encodes an enzyme which degrades fibronectin, laminin, collagens III, IV, IX, and X, and cartilage proteoglycans. The enzyme is thought to be involved in wound repair, progression of atherosclerosis, and tumor initiation. 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: matrix metalloproteinase, MMP-9, CAN, HAD, Interleukin-6
Papers using MMP-3 antibodies
Isolation and characterization of the cyanogen bromide peptides from the l(II) chain of chick cartilage collagen.
Buehler Markus J., In PLoS ONE, 1970
... mercuric acetate (APMA) for 1 hr at 37°C or by the recombinant active catalytic domain of MMP-3 (Merck-Calbiochem) at 1∶100 molar ratio ...
Papers on MMP-3
Activated human B cells induce inflammatory fibroblasts with cartilage-destructive properties and become functionally suppressed in return.
Tretter et al., Heidelberg, Germany. In Ann Rheum Dis, 18 Jun 2015
Besides cytokines, B-cell-activated SF also upregulated secretion of matrix metalloproteases such as MMP-3, thereby acquiring potential tissue destructive properties.
Functions of miR-1 and miR-133a during the postnatal development of masseter and gastrocnemius muscles.
Asada et al., Yokohama, Japan. In Mol Cell Biochem, 16 Jun 2015
The amounts of miR-1 and miR-133a were measured in mouse masseter and gastrocnemius muscles between 1 and 12 weeks after birth with real-time polymerase chain reaction and those of HDACs, MEF2, MyoD family, MCK, SRF, and Cyclin D1 were measured at 2 and 12 weeks with Western blotting.
Gastrin stimulates MMP-1 expression in gastric epithelial cells: putative role in gastric epithelial cell migration.
Dockray et al., Liverpool, United Kingdom. In Am J Physiol Gastrointest Liver Physiol, 14 Jun 2015
In human subjects with increased serum gastrin due to PPI usage, MMP-1 transcript abundance was increased 2-fold; there was also increased MMP-7 transcript abundance but not MMP-3.
Biological variation of established and novel biomarkers for atherosclerosis: Results from a prospective, parallel-group cohort study.
Baumgartner et al., Lausanne, Switzerland. In Clin Chim Acta, 13 Jun 2015
An ICC>0.5 (indicating moderate-to-good reliability) was found for hs-CRP, D-Dimer, E-selectin, IL-10, MCP-1, MMP-3, oxLDL, sICAM-1 and sP-selectin in both groups, for sVCAM in healthy controls and for MMP-9, PAI-1 and sCD40L in PAD patients.
Matrix metalloproteinases as therapeutic targets for stroke.
Rosenberg et al., Albuquerque, United States. In Brain Res, 24 May 2015
Normally the constitutive enzymes, MMP-2 and membrane type MMP (MMP-14), are activated in a spatially specific manner and act close to the site of activation, while the inducible enzymes, MMP-3 and MMP-9, become active through the action of free radicals and other enzymes during neuroinflammation.
Aberrant protein S-nitrosylation contributes to the pathophysiology of neurodegenerative diseases.
Lipton et al., San Diego, United States. In Neurobiol Dis, 18 Apr 2015
Specifically, we discuss the pathological consequences of S-nitrosylated parkin, myocyte enhancer factor 2 (MEF2), dynamin-related protein 1 (Drp1), protein disulfide isomerase (PDI), X-linked inhibitor of apoptosis protein (XIAP), and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) under neurodegenerative conditions.
Pathophysiological aspects of thyroid hormone disorders/thyroid peroxidase autoantibodies and reproduction.
Bisschop et al., Amsterdam, Netherlands. In Hum Reprod Update, Feb 2015
T3 increases the expression of matrix metalloproteinases (MMP), MMP-2, MMP-3, fetal fibronectin and integrin α5β1T3 in early placental extravillous trophoblasts.
S-Nitrosylation in neurogenesis and neuronal development.
Lipton et al., Los Angeles, United States. In Biochim Biophys Acta, Jan 2015
S-Nitrosylation modulates neuronal development by reaction with specific proteins, including the transcription factor MEF2.
Tyrosyl phosphorylated serine-threonine kinase PAK1 is a novel regulator of prolactin-dependent breast cancer cell motility and invasion.
Diakonova et al., Toledo, United States. In Adv Exp Med Biol, Dec 2014
Tyrosyl phosphorylated PAK1 also stimulates invasion of breast cancer cells in response to PRL and three-dimensional (3D) collagen IV via transcription and secretion of MMP-1 and MMP-3 in a MAPK-dependent manner.
[Changes in markers of proliferation, neoangiogenesis and plasminogen activation system in rectal cancer tissue].
Cheryarina et al., In Eksp Klin Gastroenterol, Dec 2014
AIM OF THE STUDY: determination of levelsofsometissuegrowth factors, fibrinolyticsystemindicesand MMP-3 for specifi- cation of the role of their changes in moderately differentiated adenocarcinoma of the rectum.
The Hippo transducer YAP1 transforms activated satellite cells and is a potent effector of embryonal rhabdomyosarcoma formation.
Camargo et al., Boston, United States. In Cancer Cell, Sep 2014
YAP1-TEAD1 upregulate pro-proliferative and oncogenic genes and maintain the ERMS differentiation block by interfering with MYOD1 and MEF2 pro-differentiation activities.
Isogenic human iPSC Parkinson's model shows nitrosative stress-induced dysfunction in MEF2-PGC1α transcription.
Lipton et al., Los Angeles, United States. In Cell, 2014
We report a pathway whereby basal and toxin-induced nitrosative/oxidative stress results in S-nitrosylation of transcription factor MEF2C in A53T hNs compared to corrected controls.
MEF2 is an in vivo immune-metabolic switch.
Dionne et al., London, United Kingdom. In Cell, 2013
We show that Mef2 is required in the fat body for anabolic function and the immune response.
A role for matrix metalloproteinases in regulating mammary stem cell function via the Wnt signaling pathway.
Werb et al., San Francisco, United States. In Cell Stem Cell, 2013
Here, we identify matrix metalloproteinase-3 (MMP3) as a regulator of Wnt signaling and mammary stem cell (MaSC) activity.
Exercise, GLUT4, and skeletal muscle glucose uptake.
Hargreaves et al., Copenhagen, Denmark. In Physiol Rev, 2013
AMPK and CaMKII are key signaling kinases that appear to regulate GLUT4 expression via the HDAC4/5-MEF2 axis and MEF2-GEF interactions resulting in nuclear export of HDAC4/5 in turn leading to histone hyperacetylation on the GLUT4 promoter and increased GLUT4 transcription.
Limited cleavage of tau with matrix-metalloproteinase MMP-9, but not MMP-3, enhances tau oligomer formation.
Giese et al., München, Germany. In Exp Neurol, 2012
In this study, we identify MMP-3 and MMP-9 as potential tau proteinases
miR-92b regulates Mef2 levels through a negative-feedback circuit during Drosophila muscle development.
Han et al., Ann Arbor, United States. In Development, 2012
The negative feedback circuit between miR-92b and Mef2 efficiently maintains the stable expression of both components that is required for homeostasis during Drosophila muscle development.
Zebrafish Mef2ca and Mef2cb are essential for both first and second heart field cardiomyocyte differentiation.
Hughes et al., London, United Kingdom. In Dev Biol, 2012
Mef2ca single mutants have delayed heart development, but form an apparently normal heart. Mef2cb single mutants have a functional heart and are viable adults.
Neurotoxin-induced selective ubiquitination and regulation of MEF2A isoform in neuronal stress response.
Mao et al., Atlanta, United States. In J Neurochem, 2012
MEF2A, but not MEF2C or MEF2D, is modified by ubiquitination in dopaminergic neuronal cell line SN4741 cells.
[Association of the MMP3, MMP9, ADAM33 and TIMP3 genes polymorphic markers with development and progression of chronic obstructive pulmonary disease].
Victorova et al., In Mol Biol (mosk), 2012
The MMP3 gene polymorphism may be an important risk factor for the development and progression of chronic obstructive pulmonary disease.
share on facebooktweetadd +1mail to friends