Inactivation of mitochondrial respiratory chain complex I leads mitochondrial nitric oxide synthase to become pro-oxidative |
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| Authors: | Parihar Mordhwaj S Parihar Arti Villamena Frederick A Vaccaro Patrick S Ghafourifar Pedram |
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| Affiliation: | Department of Surgery, Davis Heart and Lung Research Institute, and Institute of Mitochondrial Biology, The Ohio State University, Columbus, OH 43210, USA |
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| Abstract: | We recently demonstrated that mitochondrial nitric oxide synthase (mtNOS) functionally couples with mitochondrial respiratory chain complex I to produce nitric oxide [M.S. Parihar, R.R. Nazarewicz, E. Kincaid, U. Bringold, P. Ghafourifar, Association of mitochondrial nitric oxide synthase activity with respiratory chain complex I, Biochem. Biophys. Res. Commun. 366 (2008) 23-28] [1]. The present report shows that inactivation of complex I leads mtNOS to become pro-oxidative. Our findings suggest a crucial role for mtNOS in oxidative stress caused by mitochondrial complex I inactivation. |
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| Keywords: | RCC, respiratory chain complex NO, nitric oxide NOS, nitric oxide synthase mtNOS, mitochondrial nitric oxide synthase GSNO, S-nitrosoglutathione DMPO, (5,5-dimethylpyrroline-N-oxide) ROS, reactive oxygen species DTPA, diethylene triamine pentaacetic acid MnTBAP, Mn (III) porphyrin 5,10,15,20-tetrakis(benzoic acid) porphyrin FL, 2-{2-chloro-6-hydroxy-5-[(2-methyl-quinolin-8-ylamino)-methyl]-3-oxo-3H-xanthen-9-yl}-benzoic acid DCF-DA, chloromethyl-2,7-dichlorodihydrofluorescein diacetate smallcaps" >l-NMMA, smallcaps" >l-NG-monomethyl arginine |
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