HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 280, Issue 47, 39302-39308, November 25, 2005

This Article Full Text Full Text (PDF) All Versions of this Article: 280/47/39302    most recent M506566200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Rezgui, S. S. Articles by Marty, I. Search for Related Content PubMed PubMed Citation Articles by Rezgui, S. S. Articles by Marty, I. Social Bookmarking                      What's this?

Triadin (Trisk 95) Overexpression Blocks Excitation-Contraction Coupling in Rat Skeletal Myotubes^*

Sophia Smida Rezgui¶, Stéphane Vassilopoulos¶, Julie Brocard¶, Jean Claude Platel¶, Alexandre Bouron¶, Christophe Arnoult¶, Sarah Oddoux¶, Luis Garcia¶||, Michel De Waard¶, and Isabelle Marty¶1

From the INSERM U607, Laboratoire Canaux Calciques, Fonctions et Pathologies, CEA Grenoble, DRDC, 17 rue des Martyrs, F38054 Grenoble, France, the University of Grenoble, Grenoble, F38000 France, and ^||Genethon, 1, rue de l'Internationale, Evry, 91002 France

To identify the function of triadin in skeletal muscle, adenovirus-mediated overexpression of Trisk 95 or Trisk 51, the two major skeletal muscle isoforms, was induced in rat skeletal muscle primary cultures, and the physiological behavior of the modified cells was analyzed. Overexpression did not modify the expression level of their protein partners ryanodine receptor, dihydropyridine receptor, and the other triadin. Caffeine-induced calcium release was also unaffected by triadin overexpression. Nevertheless, in the absence of extracellular calcium, depolarization-induced calcium release was almost abolished in Trisk 95 overexpressing myotubes (T95 myotubes), and not modified in Trisk 51 overexpressing myotubes (T51 myotubes). This was not because of a modification of dihydropyridine receptors, as depolarization in presence of external calcium still induced a calcium release, and the activation curve of dihydropyridine receptor was unchanged, in both T95 and T51 myotubes. The calcium release complex was also maintained in T95 myotubes as Trisk 95, ryanodine receptor, dihydropyridine receptor, and Trisk 51 were still co-localized. The effect of Trisk 95 overexpression on depolarization-induced calcium release was reversed by a simultaneous infection with an antisense Trisk 95 adenovirus, indicating the specificity of this effect. Thus, the level of Trisk 95 and not Trisk 51 is important on regulating the calcium release complex, and an excess of this protein can lead to an inhibition of the physiological function of the complex.

Received for publication, June 16, 2005 , and in revised form, September 20, 2005.

^* This work was supported by grants from the Association Française contre les Myopathies (AFM), by grants from the GIS-Institut des Maladies Rares, and financial support from INSERM, CEA, and the French ministry of research. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: CCFP-INSERM U607, DRDC-CEA Grenoble, 17 rue des Martyrs, 38054 Grenoble Cedex 9, France. Tel.: 33-4-38-78-5706; Fax: 33-4-38-78-5041; E-mail: imarty{at}cea.fr.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				X. Shen, C. Franzini-Armstrong, J. R. Lopez, L. R. Jones, Y. M. Kobayashi, Y. Wang, W. G. L. Kerrick, A. H. Caswell, J. D. Potter, T. Miller, et al. Triadins Modulate Intracellular Ca2+ Homeostasis but Are Not Essential for Excitation-Contraction Coupling in Skeletal Muscle J. Biol. Chem., December 28, 2007; 282(52): 37864 - 37874. [Abstract] [Full Text] [PDF]

				S. A. Goonasekera, N. A. Beard, L. Groom, T. Kimura, A. D. Lyfenko, A. Rosenfeld, I. Marty, A. F. Dulhunty, and R. T. Dirksen Triadin Binding to the C-Terminal Luminal Loop of the Ryanodine Receptor is Important for Skeletal Muscle Excitation Contraction Coupling J. Gen. Physiol., September 24, 2007; 130(4): 365 - 378. [Abstract] [Full Text] [PDF]

				A. J. Rose, T. J. Alsted, J. B. Kobbero, and E. A. Richter Regulation and function of Ca2+-calmodulin-dependent protein kinase II of fast-twitch rat skeletal muscle J. Physiol., May 1, 2007; 580(3): 993 - 1005. [Abstract] [Full Text] [PDF]

				E. J. Jaehnig, A. B. Heidt, S. B. Greene, I. Cornelissen, and B. L. Black Increased Susceptibility to Isoproterenol-Induced Cardiac Hypertrophy and Impaired Weight Gain in Mice Lacking the Histidine-Rich Calcium-Binding Protein Mol. Cell. Biol., December 15, 2006; 26(24): 9315 - 9326. [Abstract] [Full Text] [PDF]

				E. H. Lee, G. Cherednichenko, I. N. Pessah, and P. D. Allen Functional Coupling between TRPC3 and RyR1 Regulates the Expressions of Key Triadic Proteins J. Biol. Chem., April 14, 2006; 281(15): 10042 - 10048. [Abstract] [Full Text] [PDF]