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Endocrinology, doi:10.1210/en.2002-0164
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Endocrinology Vol. 144, No. 8 3586-3597
Copyright © 2003 by The Endocrine Society

Testosterone Stimulates Intracellular Calcium Release and Mitogen-Activated Protein Kinases Via a G Protein-Coupled Receptor in Skeletal Muscle Cells

Manuel Estrada, Alejandra Espinosa, Marioly Müller and Enrique Jaimovich

Centro de Estudios Moleculares de la Célula and Instituto de Ciencias Biomédicas, Facultad de Medicina, Universidad de Chile, Casilla 70005, Santiago 6530499, Chile

Address all correspondence and requests for reprints to: Dr. Enrique Jaimovich, Instituto de Ciencias Biomédicas, Facultad de Medicina, Universidad de Chile, Independencia 1027, Casilla 70005, Santiago 6530499, Chile. E-mail: ejaimovi{at}machi.med.uchile.cl.

Involvement of intracellular Ca2+ and ERK1/2 phosphorylation in the fast nongenomic effects of androgens in myotubes was investigated. Testosterone or nandrolone produced fast (<1 min) and transient increases in intracellular Ca2+ with an oscillatory pattern. Calcium signals were slightly reduced in Ca2+-free medium, but lack of oscillations was evident. Signals were blocked by U-73122 and xestospongin B, inhibitors of inositol 1,4,5-trisphosphate (IP3) pathway. Furthermore, IP3 increased transiently 2- to 3-fold 45 sec after hormone addition. Cyproterone neither affected the fast Ca2+ signal nor the increase in IP3. Calcium increases could also be induced by the impermeant testosterone conjugated to BSA, and the effect of testosterone was abolished in cells incubated with guanosine 5'-O-(2-thiodiphosphate) or pertussis toxin. Stimulation of myotubes with testosterone, nandrolone, or testosterone conjugated to BSA increased immunodetectable phosphorylation of ERK1/2 within 5 min, and this effect was not inhibited by cyproterone. Phosphorylation was blocked by the use of 1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid-acetoxymethylester, U-73122, and xestospongin B as well as by dominant negative Ras, MAPK kinase (MEK), or the MEK inhibitor PD-98059. In addition, guanosine 5'-O-(2-thiodiphosphate) or pertussis toxin blocked ERK1/2 phosphorylation. These results are consistent with a fast effect of testosterone, involving a G protein-linked receptor at the plasma membrane, IP3-mediated Ca2+ signal, and the Ras/MEK/ERK pathway in muscle cells.




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