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Originally published In Press as doi:10.1074/jbc.M501484200 on May 31, 2005

J. Biol. Chem., Vol. 280, Issue 31, 28601-28609, August 5, 2005
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Triadins Are Not Triad-specific Proteins

TWO NEW SKELETAL MUSCLE TRIADINS POSSIBLY INVOLVED IN THE ARCHITECTURE OF SARCOPLASMIC RETICULUM*

Stéphane Vassilopoulos{ddagger}§, Dominique Thevenon{ddagger}§, Sophia Smida Rezgui{ddagger}§, Julie Brocard{ddagger}§, Agnès Chapel||, Alain Lacampagne**{ddagger}{ddagger}, Joël Lunardi{ddagger}§, Michel DeWaard{ddagger}§, and Isabelle Marty{ddagger}§§§

From the {ddagger}INSERM U607, Laboratoire Canaux Calciques, Fonctions et Pathologies, Grenoble F-38054, France, §CEA Grenoble, DRDC, Grenoble F-38000, France, University Joseph Fourier, Grenoble F-38000, France, ||CEA Grenoble, DRDC, Laboratoire Chimie des Protéines, Grenoble F-38054, France, **INSERM U637, IFR3, Physiopathologie Cardiovasculaire, Montpellier F-34095, France, and {ddagger}{ddagger}CHU Arnaud de Villeneuve, Montpellier F-3400, France

We have cloned two new triadin isoforms from rat skeletal muscle, Trisk 49 and Trisk 32, which were named according to their theoretical molecular masses (49 and 32 kDa, respectively). Specific antibodies directed against each protein were produced to characterize both new triadins. Both are expressed in adult rat skeletal muscle, and their expression in slow twitch muscle is lower than that in fast twitch muscle. Using double immunofluorescent labeling, the localization of these two triadins was studied in comparison to well-characterized proteins such as ryanodine receptor, calsequestrin, desmin, Ca2+-ATPase, and titin. None of these two triadins are localized within the rat skeletal muscle triad. Both are instead found in different parts of the longitudinal sarcoplasmic reticulum. We attempted to identify partners for each isoform: neither is associated with ryanodine receptor; Trisk 49 could be associated with titin or another sarcomeric protein; and Trisk 32 could be associated with IP3 receptor. These results open further fields of research concerning the functions of these two proteins; in particular, they could be involved in the set up and maintenance of a precise sarcoplasmic reticulum structure.


Received for publication, February 8, 2005 , and in revised form, May 2, 2005.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AJ812275 and AJ812276.

* This work was supported by grants from the Association Française contre les Myopathies and 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.

§§ To whom correspondence should be addressed: CCFP-INSERM U607, DRDC-CEA Grenoble, 17 rue des Martyrs, 38054 Grenoble Cedex 9, France. Tel.: 33-4-38-78-57-06; Fax: 33-4-38-78-50-41; E-mail: imarty{at}cea.fr.


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