Kinestatin: a novel bradykinin B2 receptor antagonist peptide from the skin secretion of the Chinese toad, Bombina maxima.
We have isolated a novel bradykinin B(2)-receptor antagonist peptide, kinestatin, from toad (Bombina maxima) defensive skin secretion. Mass spectroscopy established a molecular mass of 931.56 Da and a provisional structure: pGlu-Leu/Ile-Pro-Gly-Leu/Ile-Gly-Pro-Leu/Ile-Arg.amide. The unmodified sequence, -QIPGLGPLRG-, was located at the C-terminus of a 116-amino-acid residue open-reading frame following interrogation of a sequenced B. maxima skin cDNA library database. This confirmed the presence of appropriate primary structural attributes for the observed post-translational modifications present on the mature peptide and established residue 2 as Ile and residues 5/8 as Leu. Kinestatin represents a prototype novel peptide from amphibian skin.
Chen
Tianbao
T
School of Biomedical Sciences, University of Ulster, Coleraine BT52 1SA, Northern Ireland, UK.
O'Rourke
Martin
M
Orr
David F
DF
Coulter
Daniel J M
DJ
Hirst
David G
DG
Rao
Pingfan
P
Shaw
Chris
C
D000595:Amino Acid Sequence; D000818:Animals; D001001:Anura; D001483:Base Sequence; D001920:Bradykinin / Q000494:pharmacology; D065094:Bradykinin B2 Receptor Antagonists; D018076:DNA, Complementary / Q000032:analysis / Q000235:genetics; D008297:Male; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification* / Q000494:pharmacology*; D010656:Phenylephrine / Q000494:pharmacology; D051381:Rats; D017208:Rats, Wistar; D043782:Receptor, Bradykinin B2 / Q000378:metabolism; D016415:Sequence Alignment; D012867:Skin / Q000737:chemistry* / Q000378:metabolism; D014664:Vasodilation / Q000187:drug effects
D065094:Bradykinin B2 Receptor Antagonists; D018076:DNA, Complementary; D010455:Peptides; D043782:Receptor, Bradykinin B2; D010656:Phenylephrine; D001920:Bradykinin