Gtp[delta]s removal of d600 block of skeletal muscle excitation -contraction coupling. Carney-Anderson, Lisa, Ladora V. Thompson, Daniel A. Huetteman, and Sue K. Donaldson. University of Minnesota, Department of Physiology and Department of Physical Medicine and Rehabilitation, School of Medicine, and School of Nursing, Minneapolis, Minnesota 55455
APStracts 3:0181G, 1996.
G proteins interacting with dihydropyridine receptors (DHPR) in transverse tubules (TT) of skeletal muscle may have a role in skeletal excitation-contraction (EC) coupling. The aim of this study was to determine the effects of G protein-specific nucleotides (GTP[delta]S, GDP[beta]S) on the EC coupling mechanism in the presence of D600, an agent which blocks EC coupling by immobilizing the voltage-sensing subunit of the DHPR in its inactivated state. Using the mechanically peeled single fiber preparation from rabbit adductor magnus skeletal muscle, 50[mu]M GTP[delta]S and 500[mu]M GDP[beta]S were applied with the fiber in a D600-induced state of blocked EC coupling. Neither nucleotide served as an independent stimulus for sarcoplasmic reticulum (SR) Ca2+ release when added to the TT polarizing bath under conditions of D600 block. The presence of GTP[delta]S or GDP[beta]S during a complete EC coupling cycle removed the D600 block of EC coupling despite continuous bath D600. After the nucleotides were washed out, in the continued presence of D600, the D600 block of EC coupling was reestablished. In contrast, GTP[delta]S added only during the period of TT depolarization under D600 block did not remove the D600 block of EC coupling even though GTP[delta]S did stimulate SR Ca2+ release. GTP[delta]S had no effect on submaximum (0.5-1.0mM) caffeine contractures and thus is unlikely to be acting through the Ca2+-induced Ca2+ release mechanism of the SR. These data suggest that the molecular binding site for GTP[delta]S and GDP[beta]S is likely to be in the TT near the DHPR, perhaps on a G protein.

Received 10 May 1993; accepted in final form 12 September 1996.
APS Manuscript Number G210-3.
Article publication pending Am. J. Physiol. (Gastrointest. Liver
Physiology).
ISSN 1080-4757 Copyright 1996 The American Physiological Society.
Published in APStracts on 7 October 1996