Angiotensin II induces MMP-2 in a p47phox-dependent manner

Biochem Biophys Res Commun. 2005 Mar 4;328(1):183-8. doi: 10.1016/j.bbrc.2004.12.152.

Abstract

Activated matrix metalloproteinases (MMPs) in patients with acute coronary syndromes may contribute to plaque destabilization. Since reactive oxygen species (ROS) induce MMP-2 and angiotensin II (ANG II) enhances NADPH-oxidase-dependent ROS formation, we assessed whether ANG II induces MMP-2 in a NADPH-oxidase-dependent manner. MMP-2 mRNA expression and activity were analyzed in wildtype and p47phox-deficient (p47phox-/-) murine smooth muscle cells (SMC). To address a clinical implication, sections of human atherosclerotic arteries were stained for MMP-2, p47phox, ANG II, AT1-receptor, and alpha-smooth muscle cell actin (alpha-SMC actin). MMP-2 protein expression and activity from these arteries were compared to those without atherosclerosis. ANG II enhances mRNA synthesis and activity of MMP-2 in a p47phox-dependent manner. Immunohistochemical analyses revealed a co-localization of MMP-2 with p47phox, ANG II, AT1-receptor, and alpha-SMC actin. MMP-2 protein expression and gelatinolytic activity are increased in atherosclerotic arteries. Thus, activation of the renin-angiotensin system may contribute to plaque destabilization via ROS-dependent induction of MMP-2.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Angiotensin II / pharmacology*
  • Animals
  • Cardiomyopathies / metabolism*
  • Cells, Cultured
  • Coronary Artery Disease / metabolism*
  • Coronary Vessels / metabolism*
  • Dose-Response Relationship, Radiation
  • Humans
  • In Vitro Techniques
  • Matrix Metalloproteinase 2 / metabolism*
  • Mice
  • Mice, Inbred C57BL
  • Myocytes, Smooth Muscle / drug effects
  • Myocytes, Smooth Muscle / metabolism*
  • NADPH Oxidases
  • Phosphoproteins / deficiency
  • Phosphoproteins / metabolism*

Substances

  • Phosphoproteins
  • Angiotensin II
  • NADPH Oxidases
  • neutrophil cytosolic factor 1
  • Matrix Metalloproteinase 2