缺血预处理
蛋白质组
蛋白质亚单位
蛋白质组学
磷酸化
重氮氧化物
线粒体
柠檬酸循环
蛋白激酶A
腺苷
生物化学
生物
蛋白质磷酸化
氧化磷酸化
ATP合酶
酶
化学
药理学
缺血
医学
内科学
内分泌学
基因
胰岛素
作者
D. Kent Arrell,Steven T. Elliott,Lesley A. Kane,Yurong Guo,Young Hee Ko,Pete L. Pedersen,John C. Robinson,Mitsushige Murata,Anne M. Murphy,Eduardo Marbán,Jennifer E. Van Eyk
出处
期刊:Circulation Research
[Ovid Technologies (Wolters Kluwer)]
日期:2006-09-29
卷期号:99 (7): 706-714
被引量:127
标识
DOI:10.1161/01.res.0000243995.74395.f8
摘要
Ischemic preconditioning is characterized by resistance to ischemia reperfusion injury in response to previous short ischemic episodes, a protective effect that can be mimicked pharmacologically. The underlying mechanism of protection remains controversial and requires greater understanding before it can be fully exploited therapeutically. To investigate the overall effect of preconditioning on the myocardial proteome, isolated rabbit ventricular myocytes were treated with drugs known to induce preconditioning, adenosine or diazoxide (each at 100 μmol/L for 60 minutes). Their protein profiles were then compared with vehicle-treated controls (n=4 animals per treatment) using a multitiered 2D gel electrophoresis approach. Of 28 significantly altered protein spots, 19 nonredundant proteins were identified (5 spots remained unidentified). The majority of these proteins are involved in mitochondrial energetics, including subunits of tricarboxylic acid cycle enzymes and oxidative phosphorylation complexes. These changes were not indiscriminate, with only a small number of enzymes or complex subunits altered, indicating a very specific and targeted affect of these 2 preconditioning mimetics. Among the changes were shifts in the extent of posttranslational modification of 4 proteins. One of these, the adenosine-induced phosphorylation of the ATP synthase β subunit, was fully characterized with the identification of 5 novel phosphorylation sites. This proteomics approach provides an overall assessment of the cellular response to pharmacological treatment with adenosine and diazoxide and identifies a distinct subset of enzymes and protein complex subunit that may underlie the preconditioned phenotype.
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