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J Proteomics. 2013 Apr 9;81:15-23. doi: 10.1016/j.jprot.2012.09.015. Epub 2012 Sep 25.

Site-specific quantitative analysis of cardiac mitochondrial protein phosphorylation.

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1
Department of Physiology, Division of Cardiology, David Geffen School of Medicine at UCLA, Los Angeles, CA 90095, USA.

Abstract

We report the development of a multiple-reaction monitoring (MRM) strategy specifically tailored to the detection and quantification of mitochondrial protein phosphorylation. We recently derived 68 MRM transitions specific to protein modifications in the respiratory chain, voltage-dependent anion channel, and adenine nucleotide translocase. Here, we have now expanded the total number of MRM transitions to 176 to cover proteins from the tricarboxylic acid cycle, pyruvate dehydrogenase complex, and branched-chain alpha-keto acid dehydrogenase complex. We utilized the transition set to analyze endogenous protein phosphorylation in human heart, mouse heart, and mouse liver. The data demonstrate the potential utility of the MRM workflow for studying the functional details of mitochondrial phosphorylation signaling. This article is part of a Special Issue entitled: From protein structures to clinical applications.

PMID:
23022582
PMCID:
PMC3593810
DOI:
10.1016/j.jprot.2012.09.015
[Indexed for MEDLINE]
Free PMC Article
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