Elsevier

Regulatory Peptides

Volume 41, Issue 1, 3 September 1992, Pages 1-8
Regulatory Peptides

The purification and sequence analysis of an avian neuromedin U

https://doi.org/10.1016/0167-0115(92)90508-RGet rights and content

Abstract

In this study we have purified an avian homologue of neuromedin U from the chicken. Each step of the purification process was followed by a specific radioimmunoassay developed using porcine neuromedin U. Microsequence analysis characterised the peptide to be 25 amino acid residues long with the following sequence: Y-K-V-D-E-D-L-Q-G-A-G-G-I-Q-S-R-G-Y-F-F-F-R-P-R-N. Chicken neuromedin U has marked sequence similarity with the porcine peptide at its bioactive C-terminal region. Our findings demonstrate that the amino acid sequence of neuromedin U is markedly conserved in species which have diverged millions of years ago in evolutionary terms.

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  • Cloning and expression patterns of neuromedin U and its receptors in pigs

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    Neuromedin U (NMU) is a highly conserved neuropeptide first isolated from porcine spinal cord that facilitates uterine smooth muscle contraction and increases blood pressure in rats (Minamino et al., 1985). NMU has been studied in several species, including guinea pigs (Domin et al., 1986), rats (Domin et al., 1986), Australasian tree frogs (Salmon et al., 2000), rabbits (Kage et al., 1991), chickens (O'Harte et al., 1991), goldfish (Maruyama et al., 2008), avian species (Domin et al., 1992), and humans (Austin et al., 1995; Domin et al., 1986). It must be noted that there may be differences in gene expression between species.

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1

Present address: Department of Growth Regulation, Imperial Cancer Research Fund, Lincoln's Inn Fields, London WC2A 3PX, UK.

2

Present address: Laboratory of Protein Structure, National Institute For Medical Research, Mill Hill, London NW7 1AA, UK.

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