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A novel bradykinin-like peptide from skin secretions of the frog, Rana nigrovittata

✍ Scribed by Xiuhong Liu; Dewen You; Lihua Chen; Xu Wang; Keyun Zhang; Ren Lai

Publisher
John Wiley and Sons
Year
2008
Tongue
English
Weight
225 KB
Volume
14
Category
Article
ISSN
1075-2617

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✦ Synopsis

Abstract

A bradykinin‐like peptide has been isolated from the skin secretions of the frog Rana nigrovittata. This peptide was named ranakinin‐N. Its primary structure, RAEAVPPGFTPFR, was determined by Edman degradation and mass spectrometry. It is structurally related to bradykinin‐like peptides identified from skin secretions of other amphibians. Ranakinin‐N is composed of 13 amino acid residues and is related to the bradykinin identified from the skin secretions of Odorrana schmackeri, which is composed of 9 amino acid residues. Ranakinin‐N was found to exert concentration‐dependent contractile effects on isolated guinea pig ileum. cDNA sequence encoding the precursor of ranakinin‐N was isolated from a skin cDNA library of R. nigrovittata. The amino acid sequences deduced from the cDNA sequences match well with the results from Edman degradation. Analysis of different amphibian bradykinin cDNA structures revealed that the deficiency of a 15‐nucleotide fragment (agaatgatcagacgc in the cDNA encoding bradykinin from O. schmackeri) in the peptide‐coding region resulted in the absence of a dibasic site for trypsin‐like proteinases and an unusual ‐AEVA‐ insertion in the N‐terminal part of ranakinin‐N. The ‐AEAV‐ insertion resulted in neutral net charge at the N‐terminus of ranakinin‐N. Ranakinin‐N is the first reported bradykinin‐like peptide with a neutral net charge at the N‐terminus. Copyright © 2007 European Peptide Society and John Wiley & Sons, Ltd.

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