Endothelin.
Endothelin (ET) belongs to a family of 21 amino acid peptides comprising at least three isoforms in man. Originally identified as an endothelium-derived vasoconstrictive substance, ET arises from a precursor peptide which is cleaved and released by a specific ET-converting enzyme. ET exerts multiple pharmacological effects through its own receptors. Among them, ET evokes the sustained and poorly reversible contraction of isolated vascular preparations and induces in vivo a long-lasting pressor effect preceded by transient hypotension. The mechanism of action of ET is not yet clarified although ET has been shown to stimulate phospholipase C and protein kinase C. It seems probable that this peptide acts more as a paracrine or autocrine signal than a circulating hormone. The availability of specific receptor antagonists and inhibitors of its biosynthesis will allow to understand the biological relevance of this novel family of peptides.
Chabrier
P E
PE
Institut Henri-Beaufour, Les Ulis, France.
Braquet
P
P
D000595:Amino Acid Sequence; D000818:Animals; D016232:Endothelins / Q000737:chemistry / Q000502:physiology*; D006801:Humans; D008969:Molecular Sequence Data; D011956:Receptors, Cell Surface / Q000378:metabolism; D017466:Receptors, Endothelin; D012689:Sequence Homology, Nucleic Acid; D014662:Vasoconstrictor Agents / Q000737:chemistry; D014757:Viper Venoms / Q000737:chemistry
D016232:Endothelins; D011956:Receptors, Cell Surface; D017466:Receptors, Endothelin; D014662:Vasoconstrictor Agents; D014757:Viper Venoms; C057354:sarafotoxins s6