Competitive interaction between endothelin and sarafotoxin: Binding and phosphoinositides hydrolysis in rat atria and brain
Biochemical and Biophysical Research CommunicationsPublished 1 January 1989
I. Ambar, Yoel Kloog, Iris Schvartz, Eli Hazum, Mordechai Sokolovsky
Citations144
SJR quartileQ2
SJR score0.75
SNIP0.56
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TL;DR
Binding studies with the structurally similar vasoconstrictor peptides125I-endothelin and 125I-sarafotoxin b reveal their mutually exclusive binding to rat atrium and various regions of the rat brain, suggesting that endothelins and sarafotoxins share common binding sites and mechanisms of action.
Abstract
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.
Keywords
MedicineNeuroscienceBiochemistry, Genetics and Molecular Biology
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