Modulation of sarcoplasmic reticulum Ca release in skeletal muscle expressing ryanodine receptor impaired in regulation by calmodulin and S100A1
نویسندگان
چکیده
Naohiro Yamaguchi,* Benjamin L. Prosser,* Farshid Ghassemi,* Le Xu, Daniel A. Pasek, Jerry P. Eu, Erick O. Hernández-Ochoa, Brian R. Cannon, Paul T. Wilder, Richard M. Lovering, David Weber, Werner Melzer, Martin F. Schneider, and Gerhard Meissner Department of Biochemistry and Biophysics, School of Medicine, University of North Carolina, Chapel Hill, North Carolina; Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, Maryland; Department of Medicine, Division of Pulmonary, Allergy and Critical Care, Duke University, Durham, North Carolina; Department of Orthopaedics, University of Maryland School of Medicine, Baltimore, Maryland; and Institute of Applied Physiology, Ulm University, Ulm, Germany
منابع مشابه
Modulation of sarcoplasmic reticulum Ca2+ release in skeletal muscle expressing ryanodine receptor impaired in regulation by calmodulin and S100A1.
In vitro, calmodulin (CaM) and S100A1 activate the skeletal muscle ryanodine receptor ion channel (RyR1) at submicromolar Ca(2+) concentrations, whereas at micromolar Ca(2+) concentrations, CaM inhibits RyR1. One amino acid substitution (RyR1-L3625D) has previously been demonstrated to impair CaM binding and regulation of RyR1. Here we show that the RyR1-L3625D substitution also abolishes S100A...
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The role of S100A1 in skeletal muscle is just beginning to be elucidated. We have previously shown that skeletal muscle fibers from S100A1 knockout (KO) mice exhibit decreased action potential (AP)-evoked Ca(2+) transients, and that S100A1 binds competitively with calmodulin to a canonical S100 binding sequence within the calmodulin-binding domain of the skeletal muscle ryanodine receptor. Usin...
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The skeletal muscle relaxant dantrolene inhibits the release of Ca from the sarcoplasmic reticulum during excitation-contraction coupling and suppresses the uncontrolled Ca release that underlies the skeletal muscle pharmacogenetic disorder malignant hyperthermia; however, the molecular mechanism by which dantrolene selectively affects skeletal muscle Ca regulation remains to be defined. Here w...
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Rodney George G. Calmodulin in adult mammalian skeletal muscle: localization and effect on sarcoplasmic reticulum Ca release. Am J Physiol Cell Physiol 294: C1288–C1297, 2008. First published March 5, 2008; doi:10.1152/ajpcell.00033.2008.—Calmodulin is a ubiquitous Ca binding protein that binds to ryanodine rectors (RyR) and is thought to modulate its activity. Here we evaluated the effects of ...
متن کاملS100A1 Protein Does Not Compete with Calmodulin for Ryanodine Receptor Binding but Structurally Alters the Ryanodine Receptor·Calmodulin Complex.
S100A1 has been suggested as a therapeutic agent to enhance myocyte Ca(2+) cycling in heart failure, but its molecular mode of action is poorly understood. Using FRET, we tested the hypothesis that S100A1 directly competes with calmodulin (CaM) for binding to intact, functional ryanodine receptors type I (RyR1) and II (RyR2) from skeletal and cardiac muscle, respectively. Our FRET readout provi...
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