NDLI: Mechanism of action of des-His1-[Glu9]glucagon amide, a peptide antagonist of the glucagon receptor system.

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Mechanism of action of des-His1-[Glu9]glucagon amide, a peptide antagonist of the glucagon receptor system.

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Mechanism of action of des-His1-[Glu9]glucagon amide, a peptide antagonist of the glucagon receptor system.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Post, S. R. Rubinstein, P. G. Tager, H. S.
Description	Author Affiliation: Post SR ( Department of Biochemistry and Molecular Biology, University of Chicago, IL 60637.);
Abstract	We have investigated the mechanisms through which des-His1-[Glu9]glucagon amide functions as a peptide antagonist of the glucagon receptor/adenylyl cyclase system. Studies with radiolabeled peptides identified that (i) the antagonist bound to intact hepatocytes according to a single first-order process, whereas the rate of association of glucagon with the same preparation could be described only by the sum of two first-order processes; (ii) the interaction of the antagonist with saponin-permeabilized hepatocytes was not affected by the addition of GTP to the incubation medium or by the elimination of Mg2+, whereas the interaction of glucagon with the same cell preparation was modified significantly by the presence of the nucleotide or by the absence of the divalent metal ion; (iii) the dissociation of antagonist from intact hepatocytes incubated in buffer was complete, whereas that of agonist was not; and (iv) the antagonist bound to intact hepatocytes at steady state according to a single binding isotherm (as did both agonist and antagonist in permeabilized hepatocytes), whereas glucagon bound to the intact cell system with two clearly defined apparent dissociation constants. A model is presented for the mechanism of action of the glucagon antagonist in which the analog binds to glucagon receptors in a Mg(2+)- and GTP-independent fashion and in which resulting ligand-receptor complexes fail to undergo sequential adjustments necessary for the stimulation of adenylyl cyclase.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	5
Volume Number	90
Language	English
Publisher	National Academy of Sciences
Publisher Date	1993-04-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Glucagon Analogs & Derivatives Pharmacology Receptors, Gastrointestinal Hormone Antagonists & Inhibitors Adenylate Cyclase Metabolism Animals Binding, Competitive Cyclic AMP Physiology In Vitro Techniques Liver Receptors, Glucagon Signal Transduction Structure-Activity Relationship Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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