Two tachykinin-like peptides from skin secretions of Danio rerio
✍ Scribed by Xuhua Mi; Haining Yu; Peng Jia; Zhenzhou Zhang; Luyong Zhang; Jingze Liu
- Book ID
- 105359828
- Publisher
- John Wiley and Sons
- Year
- 2010
- Tongue
- English
- Weight
- 160 KB
- Volume
- 16
- Category
- Article
- ISSN
- 1075-2617
- DOI
- 10.1002/psc.1194
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✦ Synopsis
Abstract
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.
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## Abstract Two novel antimicrobial peptides with similarity to brevinin‐2 family are purified and characterized from the skin secretions of the frog, __Rana nigrovittata__. Their amino acid sequences were determined as GAFGNFLKGVAKKAGLKILSIAQCKLSGTC (__brevinin‐2‐RN1__) and GAFGNFLKGVAKKAGLKILSIAQ