Abstract
An endothelium-derived 21-residue vasoconstrictor peptide, endothelin, has been isolated, and shown to be one of the most potent vasoconstrictors known. Cloning and sequencing of preproendothelin complementary DNA shows that mature endothelin is generated through an unusual proteolytic processing, and regional homologies to a group of neurotoxins suggest that endothelin is an endogenous modulator of voltage-dependent ion channels. Expression of the endothelin gene is regulated by several vasoactive agents, indicating the existence of a novel cardiovascular control system.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Aorta
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Arteries / drug effects
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Base Sequence
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Calcimycin / pharmacology
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Cells, Cultured
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DNA / genetics
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Endothelins
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Endothelium, Vascular / metabolism*
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Epinephrine / pharmacology
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Gene Expression Regulation / drug effects
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Ion Channels / drug effects
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Molecular Sequence Data
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Peptides / genetics
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Peptides / isolation & purification*
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Peptides / physiology
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Protein Conformation
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Protein Precursors / metabolism
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Protein Processing, Post-Translational
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RNA, Messenger / biosynthesis
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Recombinant Proteins / genetics
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Swine
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Vasoconstriction* / drug effects
Substances
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Endothelins
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Ion Channels
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Peptides
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Protein Precursors
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RNA, Messenger
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Recombinant Proteins
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Calcimycin
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DNA
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Epinephrine