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Am J Physiol Gastrointest Liver Physiol 252: G178-G181, 1987;
0193-1857/87 $5.00
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AJP - Gastrointestinal and Liver Physiology, Vol 252, Issue 2 178-G181, Copyright © 1987 by American Physiological Society

ARTICLES

Role of sulfate ester in influencing biologic activity of cholecystokinin-related peptides

R. Vinayek, R. T. Jensen and J. D. Gardner

In dispersed acini from guinea pig, mouse, or rat pancreas cholecystokinin-(27-33) is a full agonist, and removing the sulfate ester from the tyrosine residue in position 27 caused a 100- to 300-fold decrease in potency with no change in efficacy. In dispersed acini from mouse or rat pancreas, cholecystokinin-(27-32)-NH2 is a partial agonist, and removing the sulfate ester from the tyrosine in position 27 abolished the efficacy. The desulfated peptide was able, however, to interact with CCK receptors with a potency that was threefold less than that of cholecystokinin-(27-32)-NH2 and therefore functioned as a cholecystokinin receptor antagonist. In dispersed acini from guinea pig pancreas cholecystokinin-(27-32)-NH2 is a cholecystokinin receptor antagonist. Removing the sulfate ester from the tyrosine residue in position 27 of cholecystokinin(27-32)-NH2 caused a fourfold decrease in potency but did not abolish the ability of the peptide to interact with cholecystokinin receptors; therefore, desulfated cholecystokinin-(27-32)-NH2 functioned as a cholecystokinin receptor antagonist.


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Z. Ji, E. M. Hadac, R. M. Henne, S. A. Patel, T. P. Lybrand, and L. J. Miller
Direct Identification of a Distinct Site of Interaction between the Carboxyl-terminal Residue of Cholecystokinin and the Type A Cholecystokinin Receptor Using Photoaffinity Labeling
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