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

Biochem Biophys Res Commun. 2007 Dec 28;364(4):822-30. doi: 10.1016/j.bbrc.2007.10.095. Epub 2007 Oct 25.


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.

MeSH terms

  • Angiotensin II / administration & dosage*
  • Cells, Cultured
  • Coronary Vessels
  • Dose-Response Relationship, Drug
  • Electrophoresis, Gel, Two-Dimensional / methods*
  • Homeodomain Proteins / metabolism*
  • Humans
  • Myocytes, Smooth Muscle
  • Oxidation-Reduction / drug effects
  • Phosphorylation / drug effects
  • Protein Disulfide-Isomerases / metabolism*


  • Homeodomain Proteins
  • PRRX2 protein, human
  • Angiotensin II
  • Protein Disulfide-Isomerases
  • PDIA3 protein, human