One of the most widespread and abundant families of pharmacologically active
peptides in amphibian defensive skin secretions is the bradykinins and related
peptides. Despite retaining certain primary structural attributes that assign them to this
peptide family, bradykinins and related
peptides are unique among amphibian skin
peptides in that they exhibit a wide range of primary structural variations, post-translational modifications and/or N-terminal or C-terminal extensions. Initially it was believed that their high degree of primary structural heterogeneity was reflective of random gene mutations within species, but latterly, there is an increasing body of evidence that the spectrum of structural modifications found within this
peptide family is reflective of the vertebrate predator spectrum of individual species. Here we report the discovery of
ornithokinin (avian
bradykinin - Thr(6) , Leu(8) -
bradykinin) in the skin secretion of the Chinese bamboo odorous frog, Odorrana versabilis. Molecular cloning of its biosynthetic precursor-encoding
cDNA from a skin secretion-derived cDNA library revealed a deduced open-reading frame of 86
amino acid residues, encoding a single copy of
ornithokinin towards its C-terminus. The domain architecture of this
ornithokinin precursor
protein was consistent with that of a typical amphibian skin
peptide and quite different to that of the ornithokininogen from chicken plasma.
Ornithokinin was reported to induce
hypotension in the chicken and to contract the chicken oviduct but to have no obvious effect on the rat uterus. However, in this study, synthetic
ornithokinin was found to contract the rat ileum (EC50 = 539 nM) and to increase contraction frequency in the rat uterus (EC50 = 1.87 μM).