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Am J Physiol Regul Integr Comp Physiol 280: R1256-R1260, 2001;
0363-6119/01 $5.00
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Vol. 280, Issue 4, R1256-R1260, April 2001

RAPID COMMUNICATION
Skeletal muscle calcineurin: influence of phenotype adaptation and atrophy

Espen E. Spangenburg1, Jay H. Williams1, Roland R. Roy2, and Robert J. Talmadge1

1 Muscle Function Laboratory, Department of Human Nutrition, Foods, and Exercise, Virginia Polytechnic Institute and State University, Blacksburg, Virginia 24061; and 2 Brain Research Institute, University of California Los Angeles, Los Angeles, California 90095

Calcineurin (CaN) has been implicated as a signaling molecule that can transduce physiological stimuli (e.g., contractile activity) into molecular signals that initiate slow-fiber phenotypic gene expression and muscle growth. To determine the influence of muscle phenotype and atrophy on CaN levels in muscle, the levels of soluble CaN in rat muscles of varying phenotype, as assessed by myosin heavy chain (MHC)-isoform proportions, were determined by Western blotting. CaN levels were significantly greater in the plantaris muscle containing predominantly fast (IIx and IIb) MHC isoforms, compared with the soleus (predominantly type I MHC) or vastus intermedius (VI, contains all 4 adult MHC isoforms). Three months after a complete spinal cord transection (ST), the CaN levels in the VI muscle were significantly reduced, despite a significant increase in fast MHC isoforms. Surprisingly, the levels of CaN in the VI were highly correlated with muscle mass but not MHC isoform proportions in ST and control rats. These data demonstrate that CaN levels in skeletal muscle are highly correlated to muscle mass and that the normal relationship with phenotype is lost after ST.

calcium; calmodulin; myosin heavy chain; nuclear factor of activated T cells


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