Journal
PEPTIDES
Volume 31, Issue 5, Pages 979-982Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.peptides.2010.01.016
Keywords
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Funding
- Queen's University
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Skin kininogens from bombinid toads encode an array of bradykinin-related peptides and one such kininogen from Bombina maxima also encodes the potent bradykinin B2-receptor antagonist, kinestatin. In order to determine if the skin secretion of the closely-related toad, Bombina orientalis, contained a bradykinin inhibitory peptide related to kinestatin, we screened reverse phase HPLC fractions of defensive skin secretion using a rat tail artery smooth muscle preparation. A fraction was located that inhibited bradykinin-induced relaxation of the preparation and this contained a peptide of 3198.5 Da as determined by MALDI-TOF MS. Automated Edman degradation of this peptide established the identity of a 28-mer as: DMYEIKGFKSAHGRPRVCPPGEQCPIWV, with a disulfide-bridge between Cys(18) and Cys(24) and an amidated C-terminal Val residue. Peptide DV-28 was found to correspond to residues 133-160 of skin pre-kininogen-2 of B. orientalis that also encodes two copies of (Thr(6))-bradykinin. The C-terminal residue, Gly-161, of the precursor open-reading frame, acts as the C-terminal amide donor of mature DV-28. DV-28 amide thus represents a new class of bradykinin inhibitor peptide from amphibian skin secretion. (C) 2010 Elsevier Inc. All rights reserved.
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