Phosphoproteome mapping of cardiomyocyte mitochondria in a rat model of heart failure.
Phosphoproteome mapping of cardiomyocyte mitochondria in a rat model of heart failure.
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DOI：
10.1007/s11010-013-1937-7
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发表时间：
2014-04
影响因子：
4.3
通讯作者：
Beranova-Giorgianni, Sarka
中科院分区：
文献类型：
--
作者：
Giorgianni, Francesco;Khan, M. Usman;Weber, Karl T.;Gerling, Ivan C.;Beranova-Giorgianni, Sarka
Mitochondria are complex organelles essential to cardiomyocyte survival. Protein phosphorylation is emerging as a key regulator of mitochondrial function. In the study reported here, we analyzed subsarcolemmal mitochondria harvested from rats who have received 4 weeks of aldosterone/salt treatment to simulate the neurohormonal profile of human congestive heart failure. Our objective was to obtain an initial qualitative inventory of the phosphoproteins in this biological system. Subsarcolemmal mitochondria were harvested and the phosphoproteome was analyzed with a gel-free bioanalytical platform. Mitochondrial proteins were digested with trypsin, and the digests were enriched for phosphopeptides with Immobilized Metal Ion Affinity Chromatography (IMAC). The phosphopeptides were analyzed by ion trap LC-MS/MS, and the phosphoproteins identified via database searches. Based on MS/MS and MS3 data, we characterized a set of 42 phosphopeptides that encompassed 39 phosphorylation sites. These peptides mapped to 26 proteins, for example long-chain specific acyl-CoA dehydrogenase (LCAD), Complex III subunit 6, and mitochondrial import receptor TOM70. Collectively, the characterized phosphoproteins belong to diverse functional modules, including bioenergetic pathways, protein import machinery, and calcium handling. The phosphoprotein panel discovered in this study provides a foundation for future differential phosphoproteome profiling towards an integrated understanding of the role of mitochondrial phosphorylation in heart failure.
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通讯作者：
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