Primary structure and pharmacological activity of a nonapeptide related to neuromedin U isolated from chicken intestine
| Autor: | J. Michael Conlon, Steven Harvey, Wanyun Zeng, Peter W. Abel, Charles S. Bockman, Finbarr O'Harte |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
medicine.medical_specialty
Physiology Molecular Sequence Data Radioimmunoassay Neuropeptide Peptide In Vitro Techniques Biology Biochemistry Guinea pig Uterine Contraction Cellular and Molecular Neuroscience Endocrinology Internal medicine medicine Animals Amino Acid Sequence Amino Acids Intestinal Mucosa Peptide sequence Chromatography High Pressure Liquid chemistry.chemical_classification Neuropeptides Protein primary structure Rats Inbred Strains Biological activity Rats chemistry Female Neuromedin S Chickens Neuromedin U |
| Zdroj: | Peptides. 12:809-812 |
| ISSN: | 0196-9781 |
| Popis: | An extract of chicken intestine contained neuromedin U-like immunoreactivity (36 pmol/g wet tissue weight). The primary structure of the predominant molecular form (NMU-9), comprising 94% of the total immunoreactivity, was established as: Gly-Tyr-Phe-Phe-Phe-Arg-Pro-Arg- Asn-NH2. This sequence differs from that of pig neuromedin U-8 (NMU-8) by the substitution of Leu3 by Phe and, like the corresponding peptide from the guinea pig, is extended from the NH2-terminus by a Gly residue. A minor component of neuromedin U comprised 25 amino acid residues. An extract of chicken whole brain contained much less NMU-like immunoreactivity (1.5 pmol/g) and the nonpeptide was the only molecular form detected. Synthetic chicken NMU-9 produced a concentration-dependent contraction of smooth muscle from the rat uterus and its effect was unchanged in the presence of tetrodotoxin, atropine and indomethacin. The potency of chicken NMU-9 (EC50 360 +/- 60 nM; mean +/- S.E., n = 6) was approximately 8-fold less than that of pig NMU-8 (EC50 46 +/- 8 nM) but the maximum contraction produced by both agonists was not significantly different. |
| Databáze: | OpenAIRE |
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