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Am J Physiol Regul Integr Comp Physiol 279: R1889-R1898, 2000;
0363-6119/00 $5.00
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Vol. 279, Issue 5, R1889-R1898, November 2000

Characterization of RyR1-slow, a ryanodine receptor specific to slow-twitch skeletal muscle

Jeffery Morrissette1,*, Le Xu2, Alexandra Nelson1, Gerhard Meissner2, and Barbara A. Block1

1 Hopkins Marine Station, Stanford University, Pacific Grove, California 93950; and 2 University of North Carolina, Chapel Hill, North Carolina 27599

Two distinct skeletal muscle ryanodine receptors (RyR1s) are expressed in a fiber type-specific manner in fish skeletal muscle (11). In this study, we compare [3H]ryanodine binding and single channel activity of RyR1-slow from fish slow-twitch skeletal muscle with RyR1-fast and RyR3 isolated from fast-twitch skeletal muscle. Scatchard plots indicate that RyR1-slow has a lower affinity for [3H]ryanodine when compared with RyR1-fast. In single channel recordings, RyR1-slow and RyR1-fast had similar slope conductances. However, the maximum open probability (Po) of RyR1-slow was threefold less than the maximum Po of RyR1-fast. Single channel studies also revealed the presence of two populations of RyRs in tuna fast-twitch muscle (RyR1-fast and RyR3). RyR3 had the highest Po of all the RyR channels and displayed less inhibition at millimolar Ca2+. The addition of 5 mM Mg-ATP or 2.5 mM beta ,gamma -methyleneadenosine 5'-triphosphate (AMP-PCP) to the channels increased the Po and [3H]ryanodine binding of both RyR1s but also caused a shift in the Ca2+ dependency curve of RyR1-slow such that Ca2+-dependent inactivation was attenuated. [3H]ryanodine binding data also showed that Mg2+-dependent inhibition of RyR1-slow was reduced in the presence of AMP-PCP. These results indicate differences in the physiological properties of RyRs in fish slow- and fast-twitch skeletal muscle, which may contribute to differences in the way intracellular Ca2+ is regulated in these muscle types.

sarcoplasmic reticulum; excitation-contraction coupling; calcium; muscle fiber types

* J. Morrissette and L. Xu contributed equally to this work.




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