Similar Ca2+ dependences of [3H]ryanodine binding to alpha- and beta-ryanodine receptors purified from bullfrog skeletal muscle in an isotonic medium

FEBS Letters
T Murayama, Y Ogawa

Abstract

To understand the functions of the two ryanodine receptor isoforms (alpha- and beta-RyRs) in nonmammalian skeletal muscles, we determined [3H]ryanodine binding to these isoforms purified from bullfrog skeletal muscle. In 0.17 M-NaCl medium both isoforms demonstrated similar Ca2+ dependent ryanodine binding activities, while the Ca2+ sensitivity for activation of beta-RyR was increased in 1 M-NaCl medium. This enhancement in Ca2+ sensitivity depended on the kinds of salts used. These results imply that alpha- and beta-RyRs may have similar properties as Ca2+-induced Ca2+ release channels in bullfrog skeletal muscle.

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Citations

Nov 30, 2002·Trends in Cardiovascular Medicine·Takashi Murayama, Yasuo Ogawa
Dec 11, 2007·Biochemical and Biophysical Research Communications·Yasuo Ogawa
Sep 15, 2006·American Journal of Physiology. Cell Physiology·Akihito ChugunYasuo Ogawa
Dec 22, 2007·Biochemical and Biophysical Research Communications·Andrew A VossClaudio F Perez

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