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Biochem Biophys Res Commun. 2007 Dec 28;364(4):822-30. Epub 2007 Oct 25.

Oxidation of Prx2 and phosphorylation of GRP58 by angiotensin II in human coronary smooth muscle cells identified by 2D-DIGE analysis.

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Department of Pharmacology and Molecular Therapeutics, Kumamoto University Graduate School of Medical Sciences, Honjo 1-1-1, Kumamoto 860-8556, Japan.


To study early changes in angiotensin II (Ang II)-induced signaling with post-translational modifications, we analyzed proteins from cultured human coronary smooth muscle cells stimulated with Ang II, using two-dimensional difference gel electrophoresis (2D-DIGE) combined with ProQ Diamond and SYPRO Ruby staining, followed by mass spectrometry or Western blotting. Among 40 proteins identified, peroxiredoxin 2 (Prx2) was oxidized and 58 kDa glucose-regulated protein (GRP58) was phosphorylated after 5 min of Ang II (1 microM) stimulation. Valsartan, a selective Ang II type 1 (AT1) receptor blocker, and N-acetylcysteine, an antioxidant, inhibited both of these modifications, indicating the contribution of AT1 receptor and reactive oxygen species to oxidation of Prx2 and phosphorylation of GRP58 by Ang II.

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