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Am J Physiol Regul Integr Comp Physiol 274: R494-R502, 1998;
0363-6119/98 $5.00
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Vol. 274, Issue 2, R494-R502, February 1998

Characterization of the ryanodine receptor/channel of invertebrate muscle

Kerry E. Quinn1, Loriana Castellani2,3, Karol Ondrias1, and Barbara E. Ehrlich1

1 Department of Physiology, University of Connecticut, Farmington, Connecticut 06030; 2 Rosenstiel Center, Brandeis University, Waltham 02254; and 3 Marine Biological Laboratory, Woods Hole, Massachusetts 02543

Electron-microscopic analysis was used to show that invertebrate muscle has feetlike structures on the sarcoplasmic reticulum (SR) displaying the typical four-subunit appearance of the calcium (Ca2+) release channel/ryanodine receptor (RyR) observed in vertebrate skeletal muscle (K. E. Loesser, L. Castellani, and C. Franzini-Armstrong. J. Muscle Res. Cell Motil. 13: 161-173, 1992). SR vesicles from invertebrate muscle exhibited specific ryanodine binding and single channel currents that were activated by Ca2+, caffeine, and ATP and inhibited by ruthenium red. The single channel conductance of this invertebrate RyR was lower than that of the vertebrate RyR (49 and 102 pS, respectively). Activation of lobster and scallop SR Ca2+ release channel, in response to cytoplasmic Ca2+ (1 nM-10 mM), reflected a bell-shaped curve, as is found with the mammalian RyR. In contrast to a previous report (J.-H. Seok, L. Xu, N. R. Kramarcy, R. Sealock, and G. Meissner. J. Biol. Chem. 267: 15893-15901, 1992), our results show that regulation of the invertebrate and vertebrate RyRs is quite similar and suggest remarkably similar paths in these diverse organisms.

intracellular calcium release; skeletal muscle; lobster; scallop


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Mol. Biol. Cell, July 1, 2000; 11(7): 2213 - 2219.
[Abstract] [Full Text]


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