期刊
NITRIC OXIDE-BIOLOGY AND CHEMISTRY
卷 26, 期 2, 页码 95-101出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.niox.2011.12.007
关键词
Nitric oxide; Mitochondrial permeability transition pore; Thiol; Nitrosylation; Disulfide bonds formation
资金
- Japanese Ministry of Education, Culture, Sports, Science, and Technology [20590858]
- Grants-in-Aid for Scientific Research [21590926, 20590858] Funding Source: KAKEN
Nitric oxide (NO) alters the opening of mitochondrial permeability transition pore (mPTP). However, the signaling pathways of NO on mPTP remain elusive. We aimed to clarify the contribution of thiol-mediated responses to the effects of NO on mPTP in permeabilized myocytes. We found that (1) a high concentration of spermine NONOate (an NO donor; 500 mu M) opened mPTP and depolarized Delta Psi(m). (2) A low concentration of NONOate (5 mu M) prevented atractyloside (an mPTP opener)-induced mPTP opening. (3) Mn(III) tetrakis (4-benzoic acid) porphyrin (Mn-TBAP, ONOO- scavenger) attenuated the effect of high-concentration NONOate on mPTP opening, but did not inhibited the preventive effects of low-concentration NONOate. (4) When the interaction of NO with thiol was inhibited by N-ethylmaleimide, the opening (by high-concentration NONOate) and preventive effects (by low-concentration NONOate) of NONOate on mPTP were blocked. (5) Dithiothreitol (an inhibitor of disulfide bonds formation) prevented high-concentration NONOate-induced mPTP opening. (6) Ascorbic acid (an inhibitor of S-nitrosylation) prevented the preventive effects of low-concentration NONOate on mPTP. We conclude that opening of mPTP by high-concentration NO is related to disulfide bonds formation and oxidizing effects of ONOO-. In contrast, the inhibitory effect of physiological concentrations of NO on mPTP is related to S-nitrosylation. (c) 2012 Elsevier Inc. All rights reserved.
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