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Titolo:
DUAL REGULATION OF THE SKELETAL-MUSCLE RYANODINE RECEPTOR BY TRIADIN AND CALSEQUESTRIN
Autore:
OHKURA M; FURUKAWA KI; FUJIMORI H; KURUMA A; KAWANO S; HIRAOKA M; KUNIYASU A; NAKAYAMA H; OHIZUMI Y;
Indirizzi:
HIROSAKI UNIV,SCH MED,DEPT PHARMACOL,5 ZAIFU CHO HIROSAKI AOMORI 0368562 JAPAN TOHOKU UNIV,FAC PHARMACEUT SCI,DEPT PHARMACEUT MOL BIOL,AOBA KU SENDAI MIYAGI 98077 JAPAN TOKYO MED & DENT UNIV,MED RES INST,DEPT CARDIOVASC DIS,BUNKYO KU TOKYO 113 JAPAN KUMAMOTO UNIV,FAC PHARMACEUT SCI,DEPT RADIOPHARMACEUT CHEM KUMAMOTO 862 JAPAN
Titolo Testata:
Biochemistry (Easton)
fascicolo: 37, volume: 37, anno: 1998,
pagine: 12987 - 12993
SICI:
0006-2960(1998)37:37<12987:DROTSR>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
CALCIUM-RELEASE CHANNEL; RETICULUM GLYCOPROTEIN TRIADIN; JUNCTIONAL TERMINAL CISTERNAE; SARCOPLASMIC-RETICULUM; CA2+ RELEASE; DIHYDROPYRIDINE RECEPTOR; MYOTOXIN-ALPHA; FACE MEMBRANE; FOOT PROTEIN; PURIFICATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
39
Recensione:
Indirizzi per estratti:
Citazione:
M. Ohkura et al., "DUAL REGULATION OF THE SKELETAL-MUSCLE RYANODINE RECEPTOR BY TRIADIN AND CALSEQUESTRIN", Biochemistry (Easton), 37(37), 1998, pp. 12987-12993

Abstract

Triadin, a calsequestrin-anchoring transmembrane protein of the sarcoplasmic reticulum (SR), was successfully purified from the heavy fraction of SR (HSR) of rabbit skeletal muscle with an antitriadin immunoaffinity column. Since depletion of triadin from solubilized HSR with the column increased the [H-3]ryanodine binding activity, we tested a possibility of triadin for a negative regulator of the ryanodine receptor/Ca2+ release channel (RyR). Purified triadin not only inhibited [H-3]ryanodine binding to the solubilized HSR but also reduced openings ofpurified RyR incorporated into the planar lipid bilayers. On the other hand, calsequestrin, an endogenous activator of RyR [Kawasaki and Kasai (1994) Biochem. Biophys. Res. Commun. 199. 1120-1127; Ohkura et al. (1995) Can. J. Physiol. Pharmacol. 73, 1181-1185] potentiated [H-3]ryanodine binding to the solubilized HSR. Ca2+ dependency of [H-3]ryanodine binding to the solubilized HSR was reduced by triadin, whereas that was enhanced by calsequestrin. Interestingly, [H-3]ryanodine binding to the solubilized HSR potentiated by calsequestrin was reduced by triadin. Immunostaining with anti-triadin antibody proved that calsequestrin inhibited the formation of oligomeric structure of triadin. These results suggest that triadin inhibits the RyR activity and that RyR is regulated by both triadin and calsequestrin, probably through an interaction between them, In this paper, triadin has been first demonstrated to have an inhibitory role in the regulatory mechanism of the RyR.

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Documento generato il 15/08/20 alle ore 19:47:45