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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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

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.[1]


  1. Angiotensin II induces MMP-2 in a p47phox-dependent manner. Luchtefeld, M., Grote, K., Grothusen, C., Bley, S., Bandlow, N., Selle, T., Strüber, M., Haverich, A., Bavendiek, U., Drexler, H., Schieffer, B. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
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