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Two tachykinin‐like peptides from skin secretions of Danio rerio
Author(s) -
Mi Xuhua,
Yu Haining,
Jia Peng,
Zhang Zhenzhou,
Zhang Luyong,
Liu Jingze
Publication year - 2010
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.1194
Subject(s) - tachykinin receptor , substance p , chemistry , danio , peptide , amino acid , cardiotoxin , urotensin ii , biochemistry , neuropeptide , receptor , zebrafish , gene , venom
Tachykinin perform multiple physiological functions such as smoothing muscle contraction, vasodilation, inflammation, the processing of nerve signal, neuroprotection and neurodegeneration. Two novel tachykinin‐like peptides named tachykinin‐DR1 and ‐DR2 were identified from skin secretions of Danio rerio in current work. Their amino acid sequences were determined as SKSQHFHGLM‐NH 2 and NKGEIFVGLM‐NH 2 , respectively. They share a conserved FXGLM‐NH 2 C ‐terminal consensus motif. By cDNA cloning, the precursor encoding both tachykinin‐DR1 and ‐DR2 was screened from the skin cDNA library of D. rerio . Tachykinin‐DR1 and ‐DR2 share the same precursor, which is composed of 108 amino acid (aa) residues. Regarding the biological activity, tachykinin‐DRs could induce the contraction of isolated strips of guinea pig ileum just like other tackykinins. To our best knowledge, this is the first report of tachykinin from fish skin. Copyright © 2009 European Peptide Society and John Wiley & Sons, Ltd.