scholarly journals Isolation and Structure of a New Active Peptide "Xenopsin"on the Smooth Muscle, especially on a Strip of Fundus from a Rat Stomach, from the Skin of Xenopus laevis

1973 ◽  
Vol 21 (12) ◽  
pp. 2801-2804 ◽  
Author(s):  
KENGO ARAKI ◽  
SHINRO TACHIBANA ◽  
MIKIO UCHIYAMA ◽  
TERUMI NAKAJIMA ◽  
TADASHI YASUHARA
1975 ◽  
Vol 23 (12) ◽  
pp. 3132-3140 ◽  
Author(s):  
KENGO ARAKI ◽  
SHINRO TACHIBANA ◽  
MIKIO UCHIYAMA ◽  
TERUMI NAKAJIMA ◽  
TADASHI YASUHARA

1979 ◽  
Vol 27 (2) ◽  
pp. 486-491 ◽  
Author(s):  
TADASHI YASUHARA ◽  
OSAMU ISHIKAWA ◽  
TERUMI NAKAJIMA ◽  
KENGO ARAKI ◽  
SHINRO TACHIBANA
Keyword(s):  

2015 ◽  
Vol 93 (6) ◽  
pp. 405-411 ◽  
Author(s):  
Othman Al-Shboul ◽  
Ayman Mustafa

Recent studies have shown that both Rho kinase signaling and oxidative stress are involved in the pathogenesis of a number of human diseases, such as diabetes mellitus, hypertension, and atherosclerosis. However, very little is known about the effect of oxidative stress on the gastrointestinal (GI) smooth muscle Rho kinase pathway. The aim of the current study was to investigate the effect of oxidative stress on Rho kinase II and muscle contraction in rat stomach. The peroxynitrite donor 3-morpholinosydnonimine (SIN-1), hydrogen peroxide (H2O2), and peroxynitrite were used to induce oxidative stress. Rho kinase II expression and ACh-induced activity were measured in control and oxidant-treated cells via specifically designed enzyme-linked immunosorbent assay (ELISA) and activity assay kits, respectively. Single smooth muscle cell contraction was measured via scanning micrometry in the presence or absence of the Rho kinase blocker, Y-27632 dihydrochloride. All oxidant agents significantly increased ACh-induced Rho kinase II activity without affecting its expression level. Most important, oxidative stress induced by all three agents augmented ACh-stimulated muscle cell contraction, which was significantly inhibited by Y-27632. In conclusion, oxidative stress activates Rho kinase II and enhances contraction in rat gastric muscle, suggesting an important role in GI motility disorders associated with oxidative stress.


1998 ◽  
Vol 342 (1) ◽  
pp. 119-122 ◽  
Author(s):  
Soraya S Smaili ◽  
Paulo M Cavalcanti ◽  
Maria Etsuko M Oshiro ◽  
Alice T Ferreira ◽  
Aron Jurkiewicz

2001 ◽  
Vol 281 (3) ◽  
pp. R902-R908 ◽  
Author(s):  
Joseph B. Kim ◽  
Ågot Johansson ◽  
Susanne Holmgren ◽  
J. Michael Conlon

Two molecular forms of gastrin-releasing peptide (GRP) were isolated from an extract of the intestine of the tetraploid frog Xenopus laevis. The primary structure of GRP-1 (APTSQQHTEQ10LSRSNINTRG20 SHWAVGHLM.NH2) differs from that of GRP-2 by a single amino acid substitution (Asn15→ Thr15). GRP-(20–29) peptide (neuromedin C) was also isolated from the extract. Synthetic GRP-1 produced concentration-dependent contractions of longitudinal smooth muscle strips from Xenopus cardiac stomach (pD2 = 8.93 ± 0.32; n = 6). The responses were unaffected by tetrodotoxin, atropine, and methysergide, indicating a direct action of the peptide on smooth muscle cells. GRP-1 elicited concentration-dependent relaxations of precontracted (5 μM carbachol) circular smooth muscle strips from the same region (pD2 = 8.96 ± 0.21; n = 8). The responses were significantly ( P < 0.05) attenuated (71 ± 24% decrease in maximum response; n = 6) by indomethacin, indicating mediation, at least in part, by prostanoids. Despite the fact that Xenopus GRP-1 differs from pig GRP at 15 amino acid sites, both peptides are equipotent and equally effective for both contractile and relaxant responses, demonstrating that selective evolutionary pressure has acted to conserve the functional COOH-terminal domain in the peptide. The data suggest a physiologically important role for GRP in the regulation of gastric motility in X. laevis.


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