Linked Life Data

17438143

Source:http://linkedlifedata.com/resource/pubmed/id/17438143

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pubmed-article:17438143pubmed:abstractTextS100A1, a Ca(2+)-sensing protein of the EF-hand family that is expressed predominantly in cardiac muscle, plays a pivotal role in cardiac contractility in vitro and in vivo. It has recently been demonstrated that by restoring Ca(2+) homeostasis, S100A1 was able to rescue contractile dysfunction in failing rat hearts. Myocardial contractility is regulated not only by Ca(2+) homeostasis but also by energy metabolism, in particular the production of ATP. Here, we report a novel interaction of S100A1 with mitochondrial F(1)-ATPase, which affects F(1)-ATPase activity and cellular ATP production. In particular, cardiomyocytes that overexpress S100A1 exhibited a higher ATP content than control cells, whereas knockdown of S100A1 expression decreased ATP levels. In pull-down experiments, we identified the alpha- and beta-chain of F(1)-ATPase to interact with S100A1 in a Ca(2+)-dependent manner. The interaction was confirmed by colocalization studies of S100A1 and F(1)-ATPase and the analysis of the S100A1-F(1)-ATPase complex by gel filtration chromatography. The functional impact of this association is highlighted by an S100A1-mediated increase of F(1)-ATPase activity. Consistently, ATP synthase activity is reduced in cardiomyocytes from S100A1 knockout mice. Our data indicate that S100A1 might play a key role in cardiac energy metabolism.lld:pubmed
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pubmed-article:17438143pubmed:articleTitleCa2+ -dependent interaction of S100A1 with F1-ATPase leads to an increased ATP content in cardiomyocytes.lld:pubmed
pubmed-article:17438143pubmed:affiliationMaurice E Mueller Institute for Structural Biology, Biozentrum, University of Basel, Basel, Switzerland.lld:pubmed
pubmed-article:17438143pubmed:publicationTypeJournal Articlelld:pubmed
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