Kininase inhibition by glucagon.
In vitro glucagon (1-100 microgram/ml) has been shown to inhibit the degradation of bradykinin by kininases present in kidney microsomes and erythrocytes. Glucagon was less active on kininases present in plasma and was inactive on purified pancreatic carboxypeptidase B. In conscious dogs the intravenous infusion of glucagon (10 microgram/min) increased urine flow (160%) and urine kinin excretion (130%) and decreased urine kallikrein excretion (14%). It is suggested that in vivo inhibition of kininases might contribute to the biological effects of glucagon.
D000818:Animals; D001920:Bradykinin / Q000378:metabolism; D002268:Carboxypeptidases / Q000037:antagonists & inhibitors*; D004285:Dogs; D004912:Erythrocytes / Q000201:enzymology; D005934:Glucagon / Q000494:pharmacology*; D007610:Kallikreins / Q000652:urine; D007668:Kidney / Q000201:enzymology; D001121:Lysine Carboxypeptidase / Q000037:antagonists & inhibitors* / Q000097:blood; D008861:Microsomes / Q000201:enzymology
D005934:Glucagon; D002268:Carboxypeptidases; D001121:Lysine Carboxypeptidase; D007610:Kallikreins; D001920:Bradykinin