NDLI: Identification of distinct receptor complexes that account for high-and low-affinity glucagon binding to hepatic plasma membranes.

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Identification of distinct receptor complexes that account for high-and low-affinity glucagon binding to hepatic plasma membranes.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Mason, J. C. Tager, H. S.
Abstract	We have analyzed ligand-receptor complexes resulting from (i) the incubation of canine hepatic plasma membranes with [125I]iodoglucagon and (ii) subsequent gentle solubilization of receptor-bound ligand with digitonin. The complexes (molecular weight approximately equal to 500,000) retain the radiolabeled ligand during gel filtration and subsequent manipulation at 4 degrees C in the absence of covalent crosslinking. Affinity chromatography of the glucagon-receptor complexes on columns of wheat germ lectin linked to agarose resulted in two fractions, one of which was not bound by the column and the other of which was specifically eluted by N-acetylglucosamine. The presence of GTP during the incubation of plasma membranes with [125I]iodoglucagon caused about a 50% decrease in total ligand binding but affected only the ligand-receptor complexes that bound to wheat germ lectin. Moreover, it was found that the proportion of the two forms of ligand-receptor complexes identified by chromatography on wheat germ lectin depended on the degree of saturation of the membrane receptor. Thus, both the inhibition by glucagon of radiolabeled glucagon binding to membranes and the concomitantly decreased extent of association of the radiolabeled ligand with solubilized receptor complexes could be modeled in terms of two noninteracting receptor populations (having dissociation constants of about 0.35 and 4.94 X 10(-9) M). We conclude that (i) glucagon-receptor complexes formed on canine hepatic plasma membranes exist in two forms that differ after solubilization by digitonin in their avidities for wheat germ lectin, (ii) the high-and low-affinity binding of glucagon characteristic of hepatic plasma membranes arises from distinct receptor populations that probably differ in glycosylation, and (iii) the effect of GTP to decrease binding of glucagon to membranes arises from interactions of the nucleotide with the receptor complex that binds to wheat germ lectin.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	20
Volume Number	82
Language	English
Publisher	National Academy of Sciences
Publisher Date	1985-11-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Glucagon Metabolism Liver Receptors, Cell Surface Animals Cell Membrane Chromatography, Affinity Chromatography, Gel Guanosine Triphosphate Pharmacology Guanylyl Imidodiphosphate Kinetics Drug Effects Isolation & Purification Receptors, Glucagon Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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