NDLI: Matrix metalloproteinase-1-mediated up-regulation of vascular endothelial growth factor-2 in endothelial cells.

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Matrix metalloproteinase-1-mediated up-regulation of vascular endothelial growth factor-2 in endothelial cells.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Karin, Michael Schmid-schönbein, Geert W. Shaked, Helena Altshuler, Angelina E. Kistler, Erik B. Mazor, Rafi Alsaigh, Tom Pocock, Elizabeth S.
Description	Author Affiliation: Mazor R ( Department of Bioengineering, The Institute of Engineering in Medicine, Veterans Affairs Medical Center, San Diego, California, USA. rmazor@eng.ucsd.edu)
Abstract	Matrix metalloproteinase-1 (MMP-1) is a collagenase that is highly active in extracellular matrix and vascular remodeling, angiogenesis, and tumor progression. Vascular endothelial growth factor receptor-2 (VEGFR2), the main receptor for VEGF-A, is expressed on endothelial cells and promotes cell survival, proliferation, and other functions. Although MMP-1 and VEGFR2 co-exist in many normal and pathophysiological conditions, the effect of MMP-1 on cellular VEGFR2 that can promote the above processes is unknown. In this study we test the hypothesis that stimulation of endothelial cells with MMP-1 increases their levels of VEGFR2. The increased VEGFR2 is then available to bind VEGF-A, resulting in increased response. Indeed we found that endothelial cells incubated with active MMP-1 had higher mRNA and protein levels of VEGFR2. Furthermore, VEGF-A-dependent phosphorylation of intracellular signaling molecules and endothelial proliferation were elevated after MMP-1 treatment. MMP-1 caused activation of the nuclear factor-κB (NF-κB) pathway (p65/RelA) in endothelial cells, and this response was dependent upon activation of protease activated receptor-1 (PAR-1). Chromatin immunoprecipitation was used to confirm NF-κB-mediated active transcription of the VEGFR2 (KDR) gene. Elevation in VEGFR2 after MMP-1 stimulation was inhibited by PAR-1 knockdown and NF-κB specific inhibition. We conclude that MMP-1 promotes VEGFR2 expression and proliferation of endothelial cells through stimulation of PAR-1 and activation of NF-κB. These results suggest a mechanism by which MMP-1 may prime or sensitize endothelial cell functions.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	1
Volume Number	288
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2013-01-04
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Endothelial Cells Metabolism Endothelium, Vascular Cytology Gene Expression Regulation, Enzymologic Matrix Metalloproteinase 1 Vascular Endothelial Growth Factor A Vascular Endothelial Growth Factor Receptor-2 Biosynthesis Animals Cell Proliferation Microscopy, Fluorescence Models, Biological NF-kappa B Signal Transduction Up-Regulation Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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