Functional nonequality of the cardiac and skeletal ryanodine receptors

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dc.contributor.authorNakai, Junichi
dc.contributor.authorOgura, Tatsuya
dc.contributor.authorProtasi, Feliciano
dc.contributor.authorFranzini-Armstrong, Clara
dc.contributor.authorAllen, Paul D.
dc.contributor.authorBeam, Kurt G.
dc.date.accessioned2021-02-24T17:56:34Z
dc.date.available2021-02-24T17:56:34Z
dc.date.issued1997-02-04
dc.descriptionUMBC Weihong Lin Laben_US
dc.description.abstractDihydropyridine receptors (DHPRs), which are voltage-gated Ca2+ channels, and ryanodine receptors (RyRs), which are intracellular Ca2+ release channels, are expressed in diverse cell types, including skeletal and cardiac muscle. In skeletal muscle, there appears to be reciprocal signaling between the skeletal isoforms of both the DHPR and the RyR (RyR-1), such that Ca2+ release activity of RyR-1 is controlled by the DHPR and Ca2+ channel activity of the DHPR is controlled by RyR-1. Dyspedic skeletal muscle cells, which do not express RyR-1, lack excitation–contraction coupling and have an ≈30-fold reduction in L-type Ca2+ current density. Here we have examined the ability of the predominant cardiac and brain RyR isoform, RyR-2, to substitute for RyR-1 in interacting with the skeletal DHPR. When RyR-2 is expressed in dyspedic muscle cells, it gives rise to spontaneous intracellular Ca2+ oscillations and supports Ca2+ entry-induced Ca2+ release. However, unlike RyR-1, the expressed RyR-2 does not increase the Ca2+ channel activity of the DHPR, nor is the gating of RyR-2 controlled by the skeletal DHPR. Thus, the ability to participate in skeletal-type reciprocal signaling appears to be a unique feature of RyR-1.en_US
dc.description.sponsorshipWe thank N. Sekiguchi, R. Morris, and S. Mukherjee for technical help. This research was supported by a grant from the Japan Ministry of Education, Science, Culture and Sports to J.N., grants from Muscular Dystrophy Association and the Brigham and Women’s Hospital Anesthesia Foundation (P.D.A.), and National Institutes of Health Grants HL48093 (C.F.-A.) and NS24444 (K.G.B.). T.O. was supported by National Institutes of Health Grants DC00244 and DC00766 (to S. C. Kinnamon).en_US
dc.description.urihttps://www.pnas.org/content/94/3/1019en_US
dc.format.extent4 pagesen_US
dc.genrejournal articlesen_US
dc.identifierdoi:10.13016/m22idu-oqxz
dc.identifier.citationJunichi Nakai, Tatsuya Ogura, Feliciano Protasi, Clara Franzini-Armstrong, Paul D. Allen, and Kurt G. Beam, Functional nonequality of the cardiac and skeletal ryanodine receptors, PNAS (1997), 94 (3) 1019-1022; https://doi.org/10.1073/pnas.94.3.1019en_US
dc.identifier.urihttps://doi.org/10.1073/pnas.94.3.1019
dc.identifier.urihttp://hdl.handle.net/11603/21078
dc.language.isoen_USen_US
dc.relation.isAvailableAtThe University of Maryland, Baltimore County (UMBC)
dc.relation.ispartofUMBC Biological Sciences Department Collection
dc.rightsThis item is likely protected under Title 17 of the U.S. Copyright Law. Unless on a Creative Commons license, for uses protected by Copyright Law, contact the copyright holder or the author.
dc.subjectryanodine receptorsen_US
dc.subjectskeletal muscleen_US
dc.subjectdihydropyridine receptors (DHPRs)en_US
dc.subjectcardiac muscleen_US
dc.subjectcouplingen_US
dc.titleFunctional nonequality of the cardiac and skeletal ryanodine receptorsen_US
dc.typeTexten_US

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