Abstract
The defensive skin secretions of amphibians are a rich resource for the discovery of novel, bioactive peptides. Here we report the identification of a novel vascular smooth muscle-relaxing peptide, named vasorelaxin, from the skin secretion of the Chinese piebald odorous frog, Odorrana schmackeri. Vasorelaxin consists of 20 amino acid residues, SRVVKCSGFRPGSPDSREFC, with a disulfide-bridge between Cys-6 and Cys-20. The structure of its biosynthetic precursor was deduced from cloned skin cDNA and consists of 67 amino acid residues encoding a single copy of vasorelaxin (vasorelaxin, accession number: HE860494). Synthetic vasorelaxin caused a profound relaxation of rat arterial smooth muscle with an EC(50) of 6.76 nM.
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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Arteries / cytology
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Arteries / drug effects*
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Arteries / metabolism
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Base Sequence
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Cloning, Molecular
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Gene Library
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Male
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Molecular Sequence Data
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Muscle, Smooth / cytology
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Muscle, Smooth / drug effects*
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Muscle, Smooth / metabolism
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Odorants
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Peptide Fragments / chemistry
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Peptide Fragments / genetics
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Peptide Fragments / pharmacology*
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Peptides / chemistry
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Peptides / genetics
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Peptides / pharmacology*
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Ranidae
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Rats
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Rats, Wistar
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Skin / chemistry
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Skin / metabolism*
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Vasodilation / drug effects*
Substances
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Peptide Fragments
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Peptides
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vasorelaxin protein, Odorrana schmackeri
Grants and funding
These authors have no support or funding to report.