Glucagon binding to purified liver plasma membranes from growing rats undergoing energy restriction.
The purpose of this work was to investigate liver glucagon receptors in growing rats fed a control diet (11.8% crude protein) or a high-protein diet (19.8% crude protein) given in restricted amounts. The animals were fed every 4 hours. 125I-glucagon binding to purified liver plasma membranes was studied. Membrane purity was analysed with marker enzymes. The alteration of glucagon during incubation was measured. The results show that specific 125I-glucagon binding increased with time at 30 degrees C, reaching a maximal value within 120 min. The increasing level of unlabelled glucagon inhibited 125I-glucagon binding at steady state. Apparent specific 125I-glucagon binding at steady state was lower in experimental animals than in controls. This correlated with the increase in glucagon breakdown and decrease in membrane purity. Alternatively, glucagon binding to its receptors could drop. Unlabelled glucagon excess produced a time-dependent dissociation of glucagon-receptor complexes (half-life: up to 1 h). Feeding the experimental diet increased the dissociation of labelled glucagon-receptor complexes.
D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D004044:Dietary Proteins / Q000008:administration & dosage*; D005934:Glucagon / Q000378:metabolism*; D007700:Kinetics; D008099:Liver / Q000378:metabolism*; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains; D011956:Receptors, Cell Surface / Q000378:metabolism*; D018027:Receptors, Glucagon
D004044:Dietary Proteins; D011956:Receptors, Cell Surface; D018027:Receptors, Glucagon; D005934:Glucagon