Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Ryanodine-sensitive Ca2+ release mechanism in non-excitable cells (Review)
Autore:
Ozawa, T;
Indirizzi:
Tohoku Univ, Grad Sch Med, Dept Physiol, Aoba Ku, Sendai, Miyagi 9808575, Japan Tohoku Univ Sendai Miyagi Japan 9808575 Ku, Sendai, Miyagi 9808575, Japan
Titolo Testata:
INTERNATIONAL JOURNAL OF MOLECULAR MEDICINE
fascicolo: 1, volume: 7, anno: 2001,
pagine: 21 - 25
SICI:
1107-3756(200101)7:1<21:RCRMIN>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
MUSCLE SARCOPLASMIC-RETICULUM; CYCLIC ADP-RIBOSE; JUNCTIONAL TERMINAL CISTERNAE; LIVER ENDOPLASMIC-RETICULUM; BRAIN MICROSOMAL-MEMBRANES; INDUCED CALCIUM-RELEASE; PAROTID ACINAR-CELLS; FAST SKELETAL-MUSCLE; CA-2+ RELEASE; BINDING-SITES;
Keywords:
ryanodine receptor; microsomal Ca2+ release; [H-3]ryanodine binding; non-excitable cells;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
71
Recensione:
Indirizzi per estratti:
Indirizzo: Ozawa, T Tohoku Univ, Grad Sch Med, Dept Physiol, Aoba Ku, Sendai, Miyagi 9808575, Japan Tohoku Univ Sendai Miyagi Japan 9808575 i, Miyagi 9808575, Japan
Citazione:
T. Ozawa, "Ryanodine-sensitive Ca2+ release mechanism in non-excitable cells (Review)", INT J MOL M, 7(1), 2001, pp. 21-25

Abstract

The properties of a ryanodine-sensitive Ca2+ release channel (receptor) innon-excitable cells like exocrine cells or epithelial cells are described in this review. The ryanodine-sensitive Ca2+ release from the microsomal vesicles is activated by Ca2+, caffeine, ryanodine or cyclic ADP-ribose (cADPR) and is inhibited by ruthenium red or higher concentrations (greater thanor equal to 100 muM) of ryanodine. The properties are similar to those of excitable cells such as muscle cells or neuronal tissues. In some non-excitable cells, the Ca2+ release induced by caffeine, ryanodine or cADPR is stimulated by calmodulin (CaM) or FK506. K-d values of [H-3]ryanodine binding to the receptor protein range from 6 to 17 nM and are similar to those of ahigh-affinity binding site in skeletal or cardiac muscle. Maximum binding capacities (B-max) range from 40 to 620 fmol/ mg protein and are 10 similarto 200-fold lower than those for a high-affinity binding site in skeletal muscle. Caffeine, adenine nucleotide AMP-PCP, Mg2+, ruthenium red or FK506 affects the binding. In some non-excitable cells, the ryanodine receptor (RyR) isoform RyR2 or RyR3 is expressed and has been identified. However, unlike for excitable cells, information concerning the RyR proteins, includingbinding sites for modulators like CaM and phosphorylation sites has not yet been obtained.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/01/20 alle ore 03:13:53