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Titolo:
FUNCTIONAL-ROLE FOR GLYCOSYLATED SUBTYPES OF RAT ENDOTHELIN RECEPTORS
Autore:
SHRAGALEVINE Z; SOKOLOVSKY M;
Indirizzi:
TEL AVIV UNIV,FAC LIFE SCI,DEPT NEUROBIOCHEM IL-69978 TEL AVIV ISRAEL TEL AVIV UNIV,FAC LIFE SCI,DEPT NEUROBIOCHEM IL-69978 TEL AVIV ISRAEL
Titolo Testata:
Biochemical and biophysical research communications
fascicolo: 2, volume: 246, anno: 1998,
pagine: 495 - 500
SICI:
0006-291X(1998)246:2<495:FFGSOR>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
LIGAND; SLICES; CELLS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
14
Recensione:
Indirizzi per estratti:
Citazione:
Z. Shragalevine e M. Sokolovsky, "FUNCTIONAL-ROLE FOR GLYCOSYLATED SUBTYPES OF RAT ENDOTHELIN RECEPTORS", Biochemical and biophysical research communications, 246(2), 1998, pp. 495-500

Abstract

Glycosylation of endothelin (ET) receptors was found to occur in rat cerebellar and atrial membranes. Specifically, we investigated whetherthe ETA and ETB receptor subtypes differed in their sensitivity to deglycosylation treatment and whether the two affinity states (nanomolarand picomolar) observed in each receptor subtype reflect differences in glycosylation states. Pretreatment of cerebellar or atrial membranes with endoglycosidase H (endo H) caused a marked decrease in the number of maximal binding sites that bind ligand with nanomolar affinity, whereas ligand affinity remained the same. The picomolar-affinity binding sites were not affected by endo H. The use of specific antagonistsindicated that the receptor subtype most likely to be influenced by glycosylation is ETA. We suggest that in both cerebellar and atrial membranes, the carbohydrate chains of the ETA receptor contribute to the binding of ligand to the nanomolar affinity binding sites, but not to the picomolar-affinity binding sites. (C) 1998 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 04:46:21