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J. Biol. Chem., Vol. 275, Issue 26, 19653-19660, June 30, 2000
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From the Activation of the transcription factor nuclear
factor of activated T cells by the calcium-sensitive serine/threonine
phosphatase calcineurin has been proposed as one of the molecular
mechanisms by which motor nerve activity establishes the slow muscle
phenotype. To investigate whether the calcineurin pathway can regulate
the large spectrum of slow muscle characteristics in vivo,
we treated rats for three weeks with cyclosporin A (an inhibitor of
calcineurin). In soleus (slow muscle), but not in plantaris (fast
muscle), the proportion of slow myosin heavy chain (MHC-1) and slow
sarcoplasmic reticulum ATPase (SERCA2a) was decreased, whereas that of
fast MHC (MHC-2A) and fast SERCA1 increased, indicating a slow to fast contractile phenotype transition. Cytosolic isoforms of creatine kinase
and lactate dehydrogenase (most abundant in fast fibers), as well as
mitochondrial creatine kinase and citrate synthase activities (elevated
in fast/oxidative fibers) were dose dependently increased by
cyclosporin A treatment in soleus muscle, with no change in plantaris.
Calcineurin catalytic subunit was more abundant in soleus muscle fibers
compared with plantaris. Taken together these results suggest that the
calcineurin pathway co-regulates a set of multigenic protein families
involved in the transition between slow oxidative (type I) to fast
oxidative (type IIa) phenotype in soleus muscle.
Calcineurin Co-regulates Contractile and Metabolic Components of
Slow Muscle Phenotype*
,,,
Unité de Bioénergétique et
Environnement, Centre de Recherches du Service de Santé des
Armées, Avenue du Maquis du Grésivaudan,
38702, La Tronche Cedex, France, the ¶ U-446 INSERM,
Cardiologie Cellulaire et Moléculaire, Université
Paris-Sud, 92296 Châtenay-Malabry, France, and
§ Service de Physiologie Clinique et des Explorations
Fonctionnelles, Hôpitaux Universitaires de Strasbourg,
67091 Strasbourg Cedex, France
*
This work was supported by Association Française
contre les Myopathies and by the PROGRES program from INSERM.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Supported by Centre National de la Recherche Scientifique. To
whom correspondence should be addressed: U-446 INSERM, Cardiologie Cellulaire et Moléculaire, Université Paris-Sud, 5 rue J-B
Clément, 92296 Châtenay-Malabry, France. Tel.: 33 1 46 83 57 62; Fax: 33 1 46 83 54 75; E-mail:
Renee.Ventura@cep.u-psud.fr.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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