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pubmed-article:14982994pubmed:abstractTextPhospholamban (PLN) is a critical regulator of cardiac contractility through its binding to and regulation of the activity of the sarco(endo)plasmic reticulum Ca2+ ATPase. To uncover biochemical adaptations associated with extremes of cardiac muscle contractility, we used high-throughput gel-free tandem MS to monitor differences in the relative abundance of membrane proteins in standard microsomal fractions isolated from the hearts of PLN-null mice (PLN-KO) with high contractility and from transgenic mice overexpressing a superinhibitory PLN mutant in a PLN-null background (I40A-KO) with diminished contractility. Significant differential expression was detected for a subset of the 782 proteins identified, including known membrane-associated biomarkers, components of signaling pathways, and previously uninvestigated proteins. Proteins involved in fat and carbohydrate metabolism and proteins linked to G protein-signaling pathways activating protein kinase C were enriched in I40A-KO cardiac muscle, whereas proteins linked to enhanced contractile function were enriched in PLN-KO mutant hearts. These data demonstrate that Ca2+ dysregulation, leading to elevated or depressed cardiac contractility, induces compensatory biochemical responses.lld:pubmed
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pubmed-article:14982994pubmed:authorpubmed-author:EmiliAndrewAlld:pubmed
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pubmed-article:14982994pubmed:dateRevised2009-11-18lld:pubmed
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pubmed-article:14982994pubmed:articleTitleIdentification of biochemical adaptations in hyper- or hypocontractile hearts from phospholamban mutant mice by expression proteomics.lld:pubmed
pubmed-article:14982994pubmed:affiliationBanting and Best Department of Medical Research, University of Toronto, Toronto, ON, Canada M5G 1L6.lld:pubmed
pubmed-article:14982994pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:14982994pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
pubmed-article:14982994pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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