TAILIEUCHUNG - Báo cáo khoa học: Modulation of F0F1-ATP synthase activity by cyclophilin D regulates matrix adenine nucleotide levels

Cyclophilin D was recently shown to bind to and decrease the activity of F0F1 -ATP synthase in submitochondrial particles and permeabilized mito-chondria [Giorgio Vet al. (2009) J Biol Chem, 284, 33982–33988]. Cyclo-philin D binding decreased both ATP synthesis and hydrolysis rates. | IFEBS Journal Modulation of F0F1-ATP synthase activity by cyclophilin D regulates matrix adenine nucleotide levels Christos Chinopoulos1 2 Csaba Konrad2 Gergely Kiss2 Eugeniy Metelkin3 Beata Torocsik2 Steven F. Zhang1 and Anatoly A. Starkov1 1 WeillMedicalCollege of CornellUniversity New York NY USA 2 Department of MedicalBiochemistry Semmelweis University Budapest Hungary 3 Institute for Systems Biology SPb Moscow Russia Keywords adenine nucleotide carrier control strength metabolic control analysis permeability transition pore phosphate carrier Correspondence A. A. Starkov WeillMedicalCollege of CornellUniversity 585 68th Street A501 New York NY 10021 USA Fax 212 000 0000 Tel 212 746 4534 E-mail ans2024@ Received 9 June 2010 revised 22 January 2011 accepted 25 January 2011 doi Cyclophilin D was recently shown to bind to and decrease the activity of F0F1-ATP synthase in submitochondrial particles and permeabilized mitochondria Giorgio V et al. 2009 J Biol Chem 284 33982-33988 . Cyclo-philin D binding decreased both ATP synthesis and hydrolysis rates. In the present study we reaffirm these findings by demonstrating that in intact mouse liver mitochondria energized by ATP the absence of cyclophilin D or the presence of cyclosporin a led to a decrease in the extent of uncoupler-induced depolarization. Accordingly in substrate-energized mitochondria an increase in F0Fi-ATP synthase activity mediated by a relief of inhibition by cyclophilin D was evident in the form of slightly increased respiration rates during arsenolysis. However the modulation of F0F1-ATP synthase by cyclophilin D did not increase the adenine nucleotide translocase ANT -mediated ATP efflux rate in energized mitochondria or the ATP influx rate in de-energized mitochondria. The lack of an effect of cyclophilin D on the ANT-mediated adenine nucleotide exchange rate was attributed to the lower flux control coefficient of the F0F1-ATP synthase .

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