Competitive interaction between endothelin and sarafotoxin: Binding and phosphoinositides hydrolysis in rat atria and brain.
Binding studies with the structurally similar vasoconstrictor peptides 125I-endothelin and 125I-sarafotoxin b, the former of mammalian origin and the latter derived from snake venom, reveal their mutually exclusive binding to rat atrium and various regions of the rat brain. In these tissues endothelin, like sarafotoxin, induces phosphoinositide hydrolysis which is in part Ca2+-independent. It is suggested that endothelins and sarafotoxins share common binding sites and mechanisms of action.
Ambar
I
I
Department of Biochemistry, The George S. Wise Faculty of Life Sciences, Tel Aviv University, Israel 69978.
Kloog
Y
Y
Schvartz
I
I
Hazum
E
E
Sokolovsky
M
M
D000818:Animals; D001665:Binding Sites; D001667:Binding, Competitive; D001921:Brain / Q000378:metabolism; D004305:Dose-Response Relationship, Drug; D016232:Endothelins; D006325:Heart Atria / Q000378:metabolism; D066298:In Vitro Techniques; D008297:Male; D010455:Peptides / Q000378:metabolism* / Q000494:pharmacology; D010716:Phosphatidylinositols / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains; D011956:Receptors, Cell Surface / Q000378:metabolism*; D011950:Receptors, Cholinergic / Q000378:metabolism*; D017466:Receptors, Endothelin; D018000:Receptors, Peptide; D014757:Viper Venoms / Q000378:metabolism* / Q000494:pharmacology
D016232:Endothelins; D010455:Peptides; D010716:Phosphatidylinositols; D011956:Receptors, Cell Surface; D011950:Receptors, Cholinergic; D017466:Receptors, Endothelin; D018000:Receptors, Peptide; D014757:Viper Venoms; C058085:sarafotoxin receptor; C057354:sarafotoxins s6