期刊
AMERICAN JOURNAL OF PHYSIOLOGY-HEART AND CIRCULATORY PHYSIOLOGY
卷 303, 期 11, 页码 H1332-H1343出版社
AMER PHYSIOLOGICAL SOC
DOI: 10.1152/ajpheart.00145.2012
关键词
Na,K-ATPase; heart; hypoxia; S-nitrosylation; S-glutathionylation; redox stat; adaptation
资金
- Swiss National Academy of Sciences [112449, 310030_124970]
- Forschungskredit UZH Candoc [7082]
- United States-Israel Binational Science Foundation [2005346]
- Swiss National Science Foundation (SNF) [310030_124970] Funding Source: Swiss National Science Foundation (SNF)
- Division Of Behavioral and Cognitive Sci
- Direct For Social, Behav & Economic Scie [2005346] Funding Source: National Science Foundation
Yakushev S, Band M, van Patot MT, Gassmann M, Avivi A, Bogdanova A. Cross talk between S-nitrosylation and S-glutathionylation in control of the Na,K-ATPase regulation in hypoxic heart. Am J Physiol Heart Circ Physiol 303: H1332-H1343, 2012. First published September 14, 2012; doi: 10.1152/ajpheart.00145.2012.-Oxygen-induced regulation of Na, K-ATPase was studied in rat myocardium. In rat heart, Na, K-ATPase responded to hypoxia with a dose-dependent inhibition in hydrolytic activity. Inhibition of Na, K-ATPase in hypoxic rat heart was associated with decrease in nitric oxide (NO) production and progressive oxidative stress. Accumulation of oxidized glutathione (GSSG) and decrease in NO availability in hypoxic rat heart were followed by a decrease in S-nitrosylation and upregulation of S-glutathionylation of the catalytic alpha-subunit of the Na, K-ATPase. Induction of S-glutathionylation of the alpha-subunit by treatment of tissue homogenate with GSSG resulted in complete inhibition of the enzyme in rat a myocardial tissue homogenate. Inhibitory effect of GSSG in rat sarcolemma could be significantly decreased upon activation of NO synthases. We have further tested whether oxidative stress and suppression of the Na, K-ATPase activity are observed in hypoxic heart of two subterranean hypoxia-tolerant blind mole species (Spalax galili and Spalax judaei). In both hypoxia-tolerant Spalax species activity of the enzyme and tissue redox state were maintained under hypoxic conditions. However, localization of cysteines within the catalytic subunit of the Na, K-ATPase was preserved and induction of S-glutathionylation by GSSG in tissue homogenate inhibited the Spalax ATPase as efficiently as in rat heart. The obtained data indicate that oxygen-induced regulation of the Na, K-ATPase in the heart is mediated by a switch between S-glutathionylation and S-nitrosylation of the regulatory thiol groups localized at the catalytic subunit of the enzyme.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据