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Articles in PresS, published online ahead of print March 5, 2002
Am J Physiol Endocrinol Metab, 10.1152/ajpendo.00512.2001
Submitted on November 12, 2001
Accepted on January 3, 2002
1 Internal Medicine, Washington University School of Medicine, St. Louis, Missouri, USA
2 Physiology and Internal Medicine and Diabetes & Cardiovascular Biology Program, University of Missouri, Columbia, Columbia, Missouri, USA
* To whom correspondence should be addressed. E-mail: jhollosz{at}imgate.wustl.edu.
There is evidence suggesting that adaptive increases in GLUT4 and mitochondria in skeletal muscle occur in parallel. It has been reported that raising cytosolic Ca2+ in myocytes induces increases in mitochondrial enzymes. In this study, we tested the hypothesis that an increase in cytosolic Ca2+ induces an increase in GLUT4. We found that raising cytosolic Ca2+ by exposing L6 myotubes to 5 mM caffeine for 3h per day for 5 days induced increases in GLUT4 protein and in MEF2A and MEF2D, which are transcription factors involved in regulating GLUT4 expression. The caffeine-induced increases in GLUT4 and MEF2A and MEF2D were partially blocked by dantrolene, an inhibitor of sarcoplasmic reticulum (SR) Ca2+ release, and completely blocked by KN93, an inhibitor of Ca2+-calmodulin kinase (CAMK). Caffeine also induced increases in MEF2A, MEF2D and GLUT4 in rat epitrochlearis muscles incubated with caffeine in culture medium. AICAR, which activates AMP kinase, also induced ~2-fold increases in GLUT4, MEF2A and MEF2D in L6 myocytes. Our results provide evidence that increases in cytosolic Ca2+ and activation of AMPK, both of which occur in exercising muscle, increase GLUT4 protein in myocytes and skeletal muscle. The data suggest that this effect of Ca2+ is mediated by activation of CAMK, and indicate that MEF2A and MEF2D are involved in this adaptive response.
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