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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 26 Nov 2014.

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
Simultaneous Consideration of Multiple Candidate Protein Biomarkers for Long-Term Risk for Cardiovascular Events.
Newby et al., Durham, United States. In Circ Cardiovasc Genet, 24 Dec 2014
Model 1 identified 6 biomarkers strongly associated with death/MI: ICAM-1, MMP-3, NT-proBNP, IL-6, sCD40L, and IGFBP2.
MEF2 Transcription Factors Regulate Distinct Gene Programs in Mammalian Skeletal Muscle Differentiation.
Naya et al., Boston, United States. In J Biol Chem, 21 Dec 2014
By contrast, vertebrate MEF2 is encoded by four distinct genes, Mef2a, b, c, and d, making it far more challenging to link this transcription factor to the regulation of specific muscle gene programs.
Osteoactivin attenuates skeletal muscle fibrosis after distraction osteogenesis by promoting extracellular matrix degradation/remodeling.
Sairyo et al., Tokushima, Japan. In J Pediatr Orthop B, 17 Dec 2014
Transcript levels of matrix metalloprotease (mmp)-3 and MMP-9 were upregulated, and MMP-3 and MMP-9 proteins were increased in the OA-Tg group.
Alternative Splicing of MEF2C Controls its Activity in Normal Myogenesis and Promotes Tumorigenicity in Rhabdomyosarcoma Cells.
Davie et al., United States. In J Biol Chem, 17 Dec 2014
The MEF2 family of transcription factors regulates many developmental programs, including myogenesis.
Comparison of the Effects of Matrix Metalloproteinase Inhibitors on TNF-α Release from Activated Microglia and TNF-α Converting Enzyme Activity.
Kim et al., Taegu, South Korea. In Biomol Ther (seoul), Sep 2014
Our group recently reported that MMP-3, -8, and -9 are upregulated during microglial activation and play a role as proinflammatory mediators (Lee et al., 2010, 2014).
Towards a better understanding of cognitive behaviors regulated by gene expression downstream of activity-dependent transcription factors.
Bito et al., Tokyo, Japan. In Neurobiol Learn Mem, Sep 2014
Here, we will first summarize our current knowledge on essential activity-dependent transcription factors (TFs) such as CREB, MEF2, Npas4 and SRF, then examine how various transcription cofactors (TcoFs) also contribute to defining the transcriptional outputs during learning and memory.
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.
Proteases and small intestinal barrier function in health and disease.
MacDonald et al., London, United Kingdom. In Curr Opin Gastroenterol, Mar 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.
Immune-metabolic interaction in Drosophila.
Dionne, London, United Kingdom. In Fly (austin), Mar 2014
We have recently identified the transcription factor MEF2 as a critical switch between anabolic and immune function in the adult Drosophila fat body.
Hemorrhagic transformation after ischemic stroke in animals and humans.
Sharp et al., Sacramento, United States. In J Cereb Blood Flow Metab, Feb 2014
This contrasts to delayed HT (>18 to 24 hours after stroke) that relates to ischemia activation of brain proteases (MMP-2, MMP-3, MMP-9, and endogenous tissue plasminogen activator), neuroinflammation, and factors that promote vascular remodeling (vascular endothelial growth factor and high-moblity-group-box-1). Processes that mediate BBB repair and reduce HT risk are discussed, including transforming growth factor beta signaling in monocytes, Src kinase signaling, MMP inhibitors, and inhibitors of reactive oxygen species.
Isogenic human iPSC Parkinson's model shows nitrosative stress-induced dysfunction in MEF2-PGC1α transcription.
Lipton et al., Los Angeles, United States. In Cell, Jan 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.
Matrix metalloproteinases in coronary artery disease.
Garg et al., In Adv Clin Chem, Dec 2013
Although results thus far are inconsistent, meta-analysis has demonstrated that MMP-3 Glu45Lys and MMP-9 1562C/T gene polymorphisms were associated with CAD risk.
MEF2 is an in vivo immune-metabolic switch.
Dionne et al., London, United Kingdom. In Cell, Nov 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, Oct 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, Jul 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.
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