AJP - Gastrointestinal and Liver Physiology, Vol 272, Issue 4 689-G697, Copyright © 1997 by American Physiological Society

ARTICLES

Colonic smooth muscle cells possess a different subtype of somatostatin receptor from gastric smooth muscle cells

V. D. Corleto, C. Severi, D. H. Coy, G. Delle Fave and R. T. Jensen
Digestive Diseases Branch, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.

Somatostatin (SS) alters colonic motility. To investigate whether SS has a direct effect on colonic smooth muscle cells, we prepared isolated muscle cells from the descending guinea pig colon and compared the effects of SS with those on isolated gastric smooth muscle cells. In gastric cells, SS had no effect on carbachol-induced contraction, whereas in colonic cells it caused inhibition. In colonic muscle cells, SS-28 caused >85% inhibition of contraction by cholecystokinin octapeptide (CCK-8), bombesin, 12-O-tetradecanoylphorbol-13-acetate, and ionomycin, whereas it had no effect on contraction by these agents in gastric cells. In gastric cells, SS inhibited relaxation. Three synthetic SS analogs had different relative affinities for causing effects in gastric and colonic cells. Pertussis toxin inhibited the action of SS-28 in each muscle cell type by 50-75%. SS-28 alone had a small contractile effect on cells from the circular layer of the colon. SS-28 inhibited carbachol-induced contraction in colonic cells from both the longitudinal and circular layers. These results demonstrate that the action of SS differs in colonic and gastric smooth muscle cells. SS inhibits contractants in colonic cells and relaxants in gastric cells. In colonic cells, SS has a weak contractile effect due to an effect on circular muscle cells and an inhibitory effect on cells from both longitudinal and circular layers. A different SS receptor subtype mediates the actions of SS in colonic and gastric muscle cells. In both cell types, the actions of SS are mediated by pertussis toxin-sensitive and -insensitive G proteins.

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