Published online before print September 27, 2004, doi: 10.1161/01.CIR.0000143632.06471.93
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(Circulation. 2004;110:1980-1989.)
© 2004 American Heart Association, Inc.
Heart Failure |
Sphingosine Kinase Activation Mediates Ischemic Preconditioning in Murine Heart
From the Cardiology Section (Z.-Q.J., J.S.K.), VA Medical Center and Department of Medicine, University of California, San Francisco, and the Department of Medicine (E.J.G.), University of California, San Francisco.
Correspondence to Joel S. Karliner, MD, Cardiology Section (111C), 4150 Clement St, San Francisco, CA 94121. E-mail Joel.Karliner{at}med.va.gov
Received May 5, 2004; revision received July 22, 2004; accepted August 2, 2004.
Background— Phosphorylation of sphingosine by sphingosine kinase (SK) is the rate-limiting step in the cellular synthesis of sphingosine 1-phosphate (S1P). The monoganglioside GM1, which stimulates SK, is cardioprotective in part through increased generation of S1P that protects myocytes by diverse mechanisms. Because protein kinase C (PKC)
activation is necessary for myocardial ischemic preconditioning (IPC) and PKC activators increase SK activity, we tested the hypothesis that SK may be a central mediator of IPC.
Methods and Results— In adult murine hearts, IPC sufficient to reduce infarct size significantly increased cardiac SK activity, induced translocation of SK protein from the cytosol to membranes, and enhanced cardiac myocyte survival. IPC did not increase SK activity in PKC-null mice. The SK antagonist N,N-dimethylsphingosine inhibited PKC activation and directly abolished the protective effects of IPC and the enhanced SK activity induced by IPC.
Conclusions— These findings demonstrate that PKC is thus recruited by IPC and induces activation of SK that then mediates IPC-induced cardioprotection in murine heart.
Key Words: ischemia • myocardial infarction • enzymes • signal transduction
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