Degradation of glucagon receptors by dispase treatment of isolated intact rat hepatocytes.
Collagenase-isolated rat hepatocytes were treated with dispase II, a neutral proteolytic enzyme which is often used for the disintegration of neonatal cells. The treatment of hepatocytes with dispase II caused a significant reduction of glucagon binding to the intact cells. The deleterious effect of this enzyme on the specific glucagon binding site is accompanied by a reduction of the maximum intracellular cyclic AMP production.
D000818:Animals; D000242:Cyclic AMP / Q000378:metabolism; D010450:Endopeptidases / Q000494:pharmacology*; D005934:Glucagon / Q000378:metabolism*; D007700:Kinetics; D008099:Liver / Q000378:metabolism*; D008297:Male; D003012:Microbial Collagenase / Q000494:pharmacology; D051381:Rats; D011956:Receptors, Cell Surface / Q000187:drug effects / Q000378:metabolism*; D018027:Receptors, Glucagon
D011956:Receptors, Cell Surface; D018027:Receptors, Glucagon; D005934:Glucagon; D000242:Cyclic AMP; D010450:Endopeptidases; D003012:Microbial Collagenase; C023139:dispase