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Titolo:
Putative roles of type 3 ryanodine receptor isoforms (RyR3)
Autore:
Ogawa, Y; Kurebayashi, N; Murayama, T;
Indirizzi:
Juntendo Univ, Sch Med, Dept Pharmacol, Bunkyo Ku, Tokyo 1138421, Japan Juntendo Univ Tokyo Japan 1138421 macol, Bunkyo Ku, Tokyo 1138421, Japan
Titolo Testata:
TRENDS IN CARDIOVASCULAR MEDICINE
fascicolo: 2, volume: 10, anno: 2000,
pagine: 65 - 70
SICI:
1050-1738(200002)10:2<65:PROT3R>2.0.ZU;2-R
Fonte:
ISI
Lingua:
ENG
Soggetto:
CA2+ RELEASE CHANNELS; SKELETAL-MUSCLE; MICE LACKING; SARCOPLASMIC-RETICULUM; FROG; MG2+; DIAPHRAGM; MYOCYTES; CALCIUM; FIBERS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
35
Recensione:
Indirizzi per estratti:
Indirizzo: Ogawa, Y Juntendo Univ, Sch Med, Dept Pharmacol, Bunkyo Ku, Tokyo 1138421,Japan Juntendo Univ Tokyo Japan 1138421 nkyo Ku, Tokyo 1138421, Japan
Citazione:
Y. Ogawa et al., "Putative roles of type 3 ryanodine receptor isoforms (RyR3)", TREND CARD, 10(2), 2000, pp. 65-70

Abstract

Ca2+-release from the sarcoplasmic or endoplasmic reticulum, the intracellular Ca2+ store, is mediated by the ryanodine receptor (RyR) and/or the inositol trisphosphate receptor (IP3R). While IP3R. is a ligand(IP3)-operated channel RyR can be gated by a ligand (Ca2+) and/or mechanical coupling withthe voltage sensor There are three genetically distinct isoforms among RyRin mammals: RyR1-3. RyR1, the primary isoform in the skeletal muscle, can be gated by direct or indirect coupling with the conformation change of thealpha 1S subunit of dihydropyridine receptor (DHPR) on the T-tubules (transversely invaginated sarcolemma) upon depolarization of skeletal muscles orby the increased cytoplasmic Ca2+ (Ca2+-induced Ca2+ release, CICR). RyR2,the primary isoform in the cardiac ventricular muscle (and, in a lesser amount, the brain), can be gated by Ca2+ which flows in through DHPR, especially the alpha 1C subunit on depolarization. RyR3 is distributed ubiquitously in various tissues and may be coexpressed with RyR1 and RyR2. RyR3 is considered to be similar to RyR2 in the respect that it can be activated by Ca2+, in view of the lack of available evidence to show the activation by thealpha 1S subunit. Therefore, it is anticipated that RyR3 might take part through CICR in Ca2+ signaling in smooth muscle and other non-muscle cells. To address the possible involvement of the CICR mechanism in the Ca2+ signal transduction, it is critical to assess the effect of Mg2+ on the CICR activity and the cytoplasmic concentration of Mg2+. In this brief review our discussion focuses on the effects of Ca2+ and Mg2+ on the activity of RyR3. (Trends Cardiovasc Med 2000;10:65-70). (C) 2000 Elsevier Science Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/07/20 alle ore 08:35:15