Contractile activity of porcine neuromedin U-25 and various neuromedin U-related peptide fragments on isolated chicken crop smooth muscle.
Contractile activity of porcine neuromedin U-25 (p-NMU-25) and various neuromedin U (NMU) peptide fragment amides was examined on chicken crop smooth muscle preparation. The relative activity (expressed as RA value) of p-NMU-25 to porcine neuromedin U-8 (p-NMU-8) was 5.51 +/- 0.09, and p-NMU-25 (15-25) was the most potent fragment with an RA value of 7.78 +/- 0.05. All C-terminal 11-peptide amides of rat, rabbit, and frog NMU peptides retained activity about three-fold higher than the corresponding C-terminal 8-peptide amides. The peptide segment Asn15-Arg-Arg17 of p-NMU-25, as well as the corresponding positions of various NMU peptides: Ser13-Gly-Gly15 of rat NMU and Ser15-Arg-Gly17 of rabbit and frog NMUs, appeared to be involved in the structural requirements for increased contractile activity in the assay system.
Okimura
K
K
Faculty of Pharmaceutical Sciences, Hokuriku University, Kanazawa, Japan.
Sakura
N
N
Ohta
S
S
Kurosawa
K
K
Hashimoto
T
T
D000595:Amino Acid Sequence; D000818:Animals; D002645:Chickens; D003426:Crop, Avian / Q000187:drug effects*; D066298:In Vitro Techniques; D008969:Molecular Sequence Data; D009130:Muscle, Smooth / Q000187:drug effects; D009479:Neuropeptides / Q000494:pharmacology*; D010446:Peptide Fragments / Q000494:pharmacology*; D013329:Structure-Activity Relationship; D013552:Swine
D009479:Neuropeptides; D010446:Peptide Fragments; C046271:neuromedin U 25