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Am J Physiol Cell Physiol (February 25, 2004). doi:10.1152/ajpcell.00395.2003
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Submitted on September 16, 2003
Accepted on February 10, 2004

RyR1 exhibits lower gain of Ca2+-induced Ca2+ release activity than RyR3 in the sarcoplasmic reticulum: evidence for selective stabilization of RyR1 channel

Takashi Murayama1* and Yasuo Ogawa1

1 Department of Pharmacology, Juntendo University School of Medicine, Tokyo, Japan

* To whom correspondence should be addressed. E-mail: takashim{at}med.juntendo.ac.jp.

We showed that frog {alpha}-ryanodine receptor ({alpha}-RyR, the homologue of mammalian RyR1) had a lowered gain of Ca2+-induced Ca2+ release (CICR) activity than {beta}-RyR, the homologue of mammalian RyR3, in the sarcoplasmic reticulum (SR) vesicles, indicating selective "stabilization" of the former isoform (Murayama, T and Ogawa, Y. (2001) J. Biol. Chem. 276, 2953-2960). To know whether this is also the case with mammalian RyR1, we determined [3H]ryanodine binding of RyR1 and RyR3 in bovine diaphragm SR vesicles, advancing further understanding of the mechanism underlying stabilization. The value of [3H]ryanodine binding (B) was normalized by its maximal binding site (Bmax) which was determined by Scatchard plot analysis, whereby the specific activity of each isoform was expressed. This B/Bmax expression demonstrated that the ryanodine binding of the individual RyR1 channels was less than 15 % that of the RyR3 channels. Responses to CICR ligands such as Ca2+, Mg2+, adenine nucleotides, and caffeine of RyR1 and RyR3 were not substantially different between in situ and purified isoforms. These results suggest that the gain of CICR activity of RyR1 is markedly lower than that of RyR3 in mammalian skeletal muscle SR, indicating selective stabilization of RyR1 as is true of frog {alpha}-RyR. The stabilization was partly eliminated by treatment with FK506 and partly by solubilization of the vesicles with 3-[(3-cholamidopropyl) dimethylammonio]-1-propanesulfonic acid (CHAPS), each of which was additive to the other, accounting for the destabilized activity. In contrast, high salt which greatly enhances the [3H]ryanodine binding caused only minor change in the gain factors of RyR1 on these treatments. None of the T-tubule components, coexisting RyR3, or calmodulin was the cause of the stabilization. Isoform-specific inhibitions by FKBP12 and by CHAPS-sensitive protein-protein or protein-lipid interactions may be involved in the selective stabilization of CICR activity of RyR1 in the SR. The CHAPS-sensitive process is common between mammalian and frog skeletal muscle and may be the primary underlying mechanism for stabilization of the RyR1 homologues.




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