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Endocrinology, Vol 124, 1235-1238, Copyright © 1989 by Endocrine Society


ARTICLES

Inhibition of glucose-stimulated insulin release in the perfused rat pancreas by parathyroid secretory protein-I (chromogranin-A)

GH Greeley Jr, JC Thompson, J Ishizuka, CW Cooper, MA Levine, SU Gorr and DV Cohn
Department of Surgery, University of Texas Medical Branch, Galveston 77550.

The effect of graded doses (10(-10)-10(8) M) of highly purified bovine parathyroid secretory protein-I (SP-I; chromogranin-A) or synthetic porcine pancreastatin on glucose-stimulated insulin release in the perfused rat pancreas was examined. SP-I (10(-9) M) inhibited the first phase of glucose-stimulated insulin release, and 10(-8) M SP-I inhibited both the first and second phases of glucose-stimulated insulin release; 10(-10) M SP-I was inactive. In comparison, pancreastatin at 10(-10) M inhibited the first phase of insulin release, and at 10(-9) and 10(-8) M, pancreastatin inhibited both phases of insulin release. The inhibition by SP-I was achieved at concentrations that normally exist in the general circulation of man. These and other data suggest that circulating SP-I plays a physiological role in the regulation of insulin secretion.


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G. Wang, Y. Anini, W. Wei, X. Qi, A.-M. O'Carroll, T. Mochizuki, H.-Q. Wang, M. R. Hellmich, E. W. Englander, and G. H. Greeley Jr.
Apelin, a New Enteric Peptide: Localization in the Gastrointestinal Tract, Ontogeny, and Stimulation of Gastric Cell Proliferation and of Cholecystokinin Secretion
Endocrinology, March 1, 2004; 145(3): 1342 - 1348.
[Abstract] [Full Text] [PDF]




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