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Titolo:
Characterization of the calcium-release channel/ryanodine receptor from zebrafish skeletal muscle
Autore:
Koulen, P; Janowitz, T; Johenning, FW; Ehrlich, BE;
Indirizzi:
Yale Univ, Dept Pharmacol & Cellular & Mol Physiol, New Haven, CT 06520 USA Yale Univ New Haven CT USA 06520 r & Mol Physiol, New Haven, CT 06520 USA Marine Biol Lab, Woods Hole, MA 02543 USA Marine Biol Lab Woods Hole MA USA 02543 iol Lab, Woods Hole, MA 02543 USA
Titolo Testata:
JOURNAL OF MEMBRANE BIOLOGY
fascicolo: 3, volume: 183, anno: 2001,
pagine: 155 - 163
SICI:
0022-2631(20011001)183:3<155:COTCCR>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
CARDIAC RYANODINE RECEPTOR; FOOT PROTEIN ISOFORMS; SARCOPLASMIC-RETICULUM; CA2+ RELEASE; CA2+-RELEASE CHANNELS; PURKINJE-CELLS; CA-2+ RELEASE; MICE LACKING; BINDING; MODULATION;
Keywords:
vertebrate; sarcoplasmic reticulum; caffeine; intracellular calcium signaling; ruthenium red; teleost;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
56
Recensione:
Indirizzi per estratti:
Indirizzo: Koulen, P Yale Univ, Dept Pharmacol & Cellular & Mol Physiol, POB 208066, New Haven,CT 06520 USA Yale Univ POB 208066 New Haven CT USA 06520 w Haven,CT 06520 USA
Citazione:
P. Koulen et al., "Characterization of the calcium-release channel/ryanodine receptor from zebrafish skeletal muscle", J MEMBR BIO, 183(3), 2001, pp. 155-163

Abstract

Calcium (Ca2+)-mediated signaling is fueled by two sources for Ca2+:Ca2+ can enter through Ca2+-channels located in the plasma membrane and can also be released from intracellular stores. In the present study the intracellular Ca2+ release channel/ryanodine receptor (RyR) from zebrafish skeletal muscle was characterized. Two RyR isoforms could be identified using immunoblotting and single-channel recordings. Biophysical properties as well as theregulation by modulators of RyR, ryanodine, ruthenium red and caffeine, were measured. Comparison with other RyRs showed that the zebrafish RyRs havefeatures observed with all RyRs described to date and thus, can serve as amodel system in future genetic and physiological studies. However, some differences in the biophysical properties were observed. The slope conductance for both isoforms was higher than that of the mammalian RyR type 1 (RyR1)measured with divalent ions. Also, inhibition by millimolar Ca2+ concentrations of the RyR isoform that is inhibited by high Ca2+ concentrations (teleost a RyR isoform) was attenuated when compared to mammalian RyRs. Due to the widespread expression of RyR these findings have important implicationsfor the interpretation of the role of the RyR in Ca2+ signaling when comparing zebrafish with mammalian physiology, especially when analyzing mutations underlying physiological changes in zebrafish.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 10/07/20 alle ore 15:23:12