An MRM-based workflow for quantifying cardiac mitochondrial protein phosphorylation in murine and human tissue.
An MRM-based workflow for quantifying cardiac mitochondrial protein phosphorylation in murine and human tissue.
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DOI：
10.1016/j.jprot.2012.02.014
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发表时间：
2012-08-03
影响因子：
3.3
通讯作者：
Ping P
中科院分区：
文献类型：
--
作者：
Lam MP;Scruggs SB;Kim TY;Zong C;Lau E;Wang D;Ryan CM;Faull KF;Ping P
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.
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影响因子：
9.9
作者：
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通讯作者：
Aebersold, Ruedi
影响因子：
4.4
作者：
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通讯作者：
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通讯作者：
Zaugg, Michael
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7
作者：
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通讯作者：
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影响因子：
20.1
作者：
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通讯作者：
Van Eyk JE