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Journal of Histochemistry and Cytochemistry, Vol. 49, 857-866, July 2001, Copyright © 2001, The Histochemical Society, Inc.

ARTICLE

Variations in Dystrophin Complex in Red and White Caudal Muscles from Torpedo marmorata

Mar Royuelaa,b, Gérald Hugonb, François Rivierb, Jean Alain Fehrentzc, Jean Martinezc, Ricardo Paniaguaa, and Dominique Mornetb
a Department of Cell Biology and Genetics, University of Alcalá, Alcalá de Henares, Spain
b INSERM U.128, IFR 24, Groupe Muscles and Pathologies, Institut Bouisson-Bertrand, Montpellier, France
c Laboratoire des Amino-acides, Peptides et Protéines, UMR 5810, Faculté de pharmacie, Montpellier, France

Correspondence to: Mar Royuela, Dept. of Cell Biology and Genetics, Univ. of Alcalá de Henares (Madrid), Spain. E-mail: ricardo.paniagua@uah.es

We present an up-to-date study on the nature, at the protein level, of various members of the dystrophin complex at the muscle cell membrane by comparing red and white caudal muscles from Torpedo marmorata. Our investigations involved immunodetection approaches and Western blotting analysis. We determined the presence or absence of different molecules belonging to the dystrophin family complex by analyzing their localization and molecular weight. Specific antibodies directed against dystrophin, i.e., DRP2 {alpha}-dystrobrevin, ß-dystroglycan, {alpha}-syntrophin, {alpha}-, ß-, {gamma}-, and {delta}-sarcoglycan, and sarcospan, were used. The immunofluorescence study (confocal microscopy) showed differences in positive immunoreactions at the sarcolemmal membrane in these slow-type and fast-type skeletal muscle fibers. Protein extracts from T. marmorata red and white muscles were analyzed by Western blotting and confirmed the presence of dystrophin and associated proteins at the expected molecular weights. Differences were confirmed by comparative immunoprecipitation analysis of enriched membrane preparations with anti-ß-dystroglycan polyclonal antibody. These experiments revealed clear complex or non-complex formation between members of the dystrophin system, depending on the muscle type analyzed. Differences in the potential function of these various dystrophin complexes in fast or slow muscle fibers are discussed in relation to previous data obtained in corresponding mammalian tissues. (J Histochem Cytochem 49:857–865, 2001)

Key Words: dystrophin family, associated proteins, striated muscles


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