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An MRM-based workflow for quantifying cardiac mitochondrial protein phosphorylation in murine and human tissue.

Abstract：

:The regulation of mitochondrial function is essential for cardiomyocyte adaptation to cellular stress. While it has long been understood that phosphorylation regulates flux through metabolic pathways, novel phosphorylation sites are continually being discovered in all functionally distinct areas of the mitochondrial proteome. Extracting biologically meaningful information from these phosphorylation sites requires an adaptable, sensitive, specific and robust method for their quantification. Here we report a multiple reaction monitoring-based mass spectrometric workflow for quantifying site-specific phosphorylation of mitochondrial proteins. Specifically, chromatographic and mass spectrometric conditions for 68 transitions derived from 23 murine and human phosphopeptides, and their corresponding unmodified peptides, were optimized. These methods enabled the quantification of endogenous phosphopeptides from the outer mitochondrial membrane protein VDAC, and the inner membrane proteins ANT and ETC complexes I, III and V. The development of this quantitative workflow is a pivotal step for advancing our knowledge and understanding of the regulatory effects of mitochondrial protein phosphorylation in cardiac physiology and pathophysiology. This article is part of a Special Issue entitled: Translational Proteomics.

journal_name

J Proteomics

journal_title

Journal of proteomics

authors

Lam MP,Scruggs SB,Kim TY,Zong C,Lau E,Wang D,Ryan CM,Faull KF,Ping P

doi

10.1016/j.jprot.2012.02.014

subject

Has Abstract

pub_date

2012-08-03 00:00:00

pages

4602-9

issue

15

eissn

1874-3919

issn

1876-7737

pii

S1874-3919(12)00098-X

journal_volume

75

pub_type

杂志文章

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