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Glucagon receptor signaling is not required for L-carbamoyl glutamate and L-citrulline induced ureagenesis in mice.

Glucagon regulates hepatic amino acid metabolism and increases ureagenesis. Ureagenesis is activated by N-acetylglutamate (NAG), formed via activation of N-acetylglutamate synthase (NAGS). Aiming to identify the steps whereby glucagon both acutely and chronically regulates ureagenesis, we investigated whether glucagon receptor mediated activation of ureagenesis is required in a situation where NAGS activity and/or NAG levels are sufficient to activate the first step of the urea cycle in vivo. Female C57Bl/6JRj mice, treated with a glucagon receptor antagonist (GRA), glucagon receptor knockout (Gcgr-/- ) mice, and wild-type (Gcgr+/+ ) littermates received an intraperitoneal injection of N-carbamoyl glutamate (a stable variant of NAG) (Car), L-citrulline (Cit), Car and Cit (Car+Cit), or PBS. In separate experiments, Gcgr-/- and Gcgr+/+ mice were administered N-carbamoyl glutamate and L-citrulline (w Car+w Cit) in the drinking water for eight weeks. Car, Cit, and Car+Cit significantly (P<0.05) increased plasma urea concentrations, independently of pharmacological and genetic disruption of glucagon receptor signaling (P=0.9). Car increased blood glucose concentrations equally in GRA and vehicle treated mice (P=0.9), whereas the increase upon Car+Cit was impaired in GRA treated mice (P=0.008). Blood glucose concentrations remained unchanged in Gcgr-/- mice upon Car (P=0.2) and Car+Cit (P=0.9). Eight weeks administration of w Car+w Cit did not change blood glucose (P>0.2), plasma amino acid (P>0.4) and urea concentrations (P>0.3), or the area of glucagon positive cells (P>0.3) in Gcgr-/- and Gcgr+/+ mice. Our data suggest that glucagon mediated activation of ureagenesis is not required when NAGS activity and/or NAG levels are sufficient to activate the first step of the urea cycle.

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