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Am J Physiol Endocrinol Metab 273: E957-E964, 1997;
0193-1849/97 $5.00
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Vol. 273, Issue 5, E957-E964, November 1997

Structure and activity of uroguanylin and guanylin from the intestine and urine of rats

Xiaohui Fan1,2, F. Kent Hamra1,2, Roslyn M. London1,2, Sammy L. Eber1,2, William J. Krause2, Ronald H. Freeman2, Christine E. Smith3, Mark G. Currie3, and Leonard R. Forte1,2

1 Truman Veterans Affairs Medical Center and 2 Departments of Pharmacology, Pathology and Anatomical Sciences and Physiology, School of Medicine, Columbia 65212; and 3 Searle Research and Development, St. Louis, Missouri 63167

Uroguanylin and guanylin are related peptides that activate common guanylate cyclase signaling molecules in the intestine and kidney. Uroguanylin was isolated from urine and duodenum but was not detected in extracts from the colon of rats. Guanylin was identified in extracts from small and large intestine but was not detected in urine. Uroguanylin and guanylin have distinct biochemical and chromatographic properties that facilitated the separation, purification, and identification of these peptides. Northern assays revealed that mRNA transcripts for uroguanylin were more abundant in small intestine compared with large intestine, whereas guanylin mRNA levels were greater in large intestine relative to small intestine. Synthetic rat uroguanylin and guanylin had similar potencies in the activation of receptors in T84 intestinal cells. Production of uroguanylin and guanylin in the mucosa of duodenum is consistent with the postulate that both peptides influence the activity of an intracellular guanosine 3',5'-cyclic monophosphate signaling pathway that regulates the transepithelial secretion of chloride and bicarbonate in the intestinal epithelium.

guanylate cyclase; guanosine 3',5'-cyclic monophosphate; kidney; heat-stable enterotoxin; human T84 intestinal cells


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