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01.03.2012 | Original Article | Ausgabe 3/2012

European Journal of Applied Physiology 3/2012

Proteomic analysis of mitochondrial proteins in cardiomyocytes from rats subjected to intermittent hypoxia

European Journal of Applied Physiology > Ausgabe 3/2012
Wei-Zhong Zhu, Xiu-Feng Wu, Yi Zhang, Zhao-Nian Zhou
Wichtige Hinweise
Communicated by Keith Phillip George.


Intermittent hypoxia (IH) markedly enhances cardiac tolerance against ischemia/reperfusion injury, but its mechanism and molecular basis remain unclear. For exploring the expression of mitochondrial proteins induced by IH, two-dimensional electrophoresis and Thermo Finnigan LTQ mass spectrometer (MS) were applied. After comparing the protein profiles of myocardial mitochondria between IH and normoxic hearts, 14 protein spots were found to be altered more than threefold between the two groups, 11 of which were identified by Finnigan LTQ MS. Among these 11 proteins, 9 were involved in energy metabolism, including 7 that were increased after IH. The latter were identified as aldehyde dehydrogenase, methylmalonate-semialdehyde dehydrogenase, ATP synthase β chain, mitochondrial aconitase, malate dehydrogenase, electron transfer flavoprotein α subunit and sirtuin 5. Two other proteins, ubiquinol-cytochrome C reductase iron-sulfur subunit and aspartate aminotransferase, were decreased after IH. Biochemical tests for energy metabolism in mitochondria supported the proteomic results. IH exposure also increased the expression of a molecular chaperone—heat shock protein 60 and an antioxidant protein, peroxiredoxin 5. These findings will provide clues for understanding the mechanism of IH-induced cardiac protection and may lead to the development of interventional strategies designed to utilize the advantages of IH clinically.

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