Reference : Oxidative stress activates MMP-2 in cultured human coronary smooth muscle cells
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/10993/5718
Oxidative stress activates MMP-2 in cultured human coronary smooth muscle cells
English
Valentin, F. [> >]
Bueb, Jean-Luc mailto [University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Life Science Research Unit >]
Kieffer, P. [> >]
Tschirhart, Eric mailto [University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Life Science Research Unit >]
Atkinson, J. [> >]
2005
Fundamental & Clinical Pharmacology
Blackwell Science
19
6
661-7
Yes (verified by ORBilu)
0767-3981
1472-8206
Oxford
United Kingdom
[en] enzymology ; Electrophoresis, Polyacrylamide Gel ; Enzyme Activation ; Enzyme Induction ; Enzyme-Linked Immunosorbent Assay ; Humans ; Matrix Metalloproteinase 2 ; Myocardium ; Oxidative Stress ; biosynthesis ; metabolism ; Cells, Cultured
[en] Oxidative stress is a cardinal feature of the inflammatory process and is involved in various pathologies including atherosclerosis. One of the important mechanisms in which oxidative stress may play a role is activation of matrix metalloproteinases such as MMP-2, which are involved in plaque destabilization. We investigated the mechanisms by which oxidative stress induces MMP-2 activation in cultured human coronary artery smooth muscle cells. Using zymography and Western blot analysis, we showed that oxidized low-density lipoproteins activate MMP-2 through up-regulation of the expression and activation of a membrane-type 1 matrix metalloproteinase (MT1-MMP). A second mechanism of MMP-2 activation involves oxidative radicals generated by the xanthine/xanthine oxidase complex (X/Xo). Research on these two mechanisms of MMP activation could lead to the elaboration of new vascular therapies for the treatment of atheroma based on interruption of a specific oxidative stress pathway.
http://hdl.handle.net/10993/5718
10.1111/j.1472-8206.2005.00371.x

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