Proteomics analysis on stressed myocardium injury-related proteins.
- Author:
Jing-bo GONG
1
;
Shu-qing WU
;
Ling-jia QIAN
Author Information
- Publication Type:Journal Article
- MeSH: Animals; Disease Models, Animal; Heat-Shock Proteins; metabolism; Male; Myocardium; metabolism; Proteomics; Rats; Rats, Wistar; Restraint, Physical; Stress, Physiological
- From: Chinese Journal of Applied Physiology 2005;21(2):171-174
- CountryChina
- Language:Chinese
-
Abstract:
AIMTo probe the related proteins to stress-induced myocardium injury.
METHODSAfter establishment of a myocardium injury model induced by restraint stress in rats, myocardium proteins of restraint stress-treated and untreated rats were extracted, and the two-dimensional polyacrylamide gel electrophoresis (2-DE) maps of the extracted proteins were established by using the immobilized pH gradient (IPG) and SDS-PAGE two-dimensional electrophoresis respectively. The alterative protein spots were analyzed by Image Master 3.01 software and identified with assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF-MS) and database searching.
RESULTSProteomics analysis showed that there were 10 proteins were significantly influenced by restraint stress in rat myocardium. After stress, proteins, including cardiac myosin heavy chain, dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex, similar to dihydrolipoamide S-succinyltransferase, mitochondrial aldehyde dehydrogenase, H (+)-transporting ATP synthase, albumin, myosin heavy chain and apolipoprotein A-I precursor showed increased expression. Mitochondrial aconitase and uncoupling protein UCP-3 showed decreased expression.
CONCLUSIONThese differential expressive proteins might be involved in stress-induced injury to myocardium.