Sarafotoxin, a novel vasoconstrictor peptide: Phosphoinositide hydrolysis in rat heart and brain

Y. Kloog, I. Ambar, M. Sokolovsky*, E. Kochva, Z. Wollberg, A. Bdolah

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

354 Scopus citations

Abstract

Sarafotoxins, a group of 21-residue cardiotoxic peptides from snake venom that induce coronary vasoconstriction, show high-affinity binding to rat atrial and brain membranes and activate the hydrolysis of phosphoinositides. Neither their binding nor their activity is affected by blockes or activators ofknown receptors and ion channels, suggesting that sarafotoxins act either directly on the phosphoinositide phosphodiesterase system or on a novel receptor. Their amino acid sequence shows a high degree of homology with that of endothein, a recently described 21-residue vasoconstrictor peptide found in porcine aortic endothelium. This is remarkable, since endothelin is a natural compound of the mammalian vascular system while sarafotoxins are highly toxic components of snake venom.

Original languageEnglish
Pages (from-to)268-270
Number of pages3
JournalScience
Volume242
Issue number4876
DOIs
StatePublished - 1988

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