Redox regulation of endogenous substrate oxidation by cardiac mitochondria

American Journal of Physiology. Heart and Circulatory Physiology
Paavo Korge, James N Weiss

Abstract

Reactive oxygen species (ROS) play important roles in regulating mitochondrial function, as well as in ischemia-reperfusion injury and cardioprotection. Here we show that, in the absence of exogenous substrates, cardiac mitochondria have a surprisingly large capacity to phosphorylate ADP by oxidizing endogenous substrates, provided that H2O2 is removed from the extramitochondrial environment and a reduced environment is maintained in the matrix. In isolated mitochondria without exogenous substrates, addition of catalase and the membrane-permeant reducing agent N-acetylcysteine (Nac) or the ROS scavenger mercaptopropionyl glycine significantly increased the ability to phosphorylate added ADP, as demonstrated by 1) full recovery of membrane potential (Deltapsi) and matrix volume from ADP-induced dissipation and shrinkage, 2) ADP-dependent increase in O2 consumption, and 3) enhanced rate of ATP synthesis. Removal of extramitochondrial H2O2 by catalase was required to stimulate endogenous substrate oxidation, as shown by the increase in O2 consumption and Deltapsi. This effect was greatly enhanced by addition of Nac or mercaptopropionyl glycine to suppress oxidation-induced ROS increases in the matrix. Theoretical considerations, a...Continue Reading

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Citations

Mar 31, 2012·Cell Death and Differentiation·J Boren, K M Brindle
Oct 7, 2009·Proceedings of the National Academy of Sciences of the United States of America·Kyle L HoehnDavid E James
Aug 17, 2010·Cardiovascular Pathology : the Official Journal of the Society for Cardiovascular Pathology·Vishnu UndyalaRichard S Vander Heide
Feb 24, 2010·Biochimica Et Biophysica Acta·M A AonB O'Rourke
Sep 25, 2012·Free Radical Biology & Medicine·Ranjana Kumari KanchanSmrati Bhadauria

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