EFFECT OF GLUCAGON ON PHENYLALANINE METABOLISM AND PHENYLALANINE-DEGRADING ENZYMES IN RAT
EFFECT OF GLUCAGON ON PHENYLALANINE METABOLISM AND PHENYLALANINE-DEGRADING ENZYMES IN RAT
复制标题
DOI:
10.1042/bj1420231
复制
发表时间:
1974-01-01
影响因子:
4.1
通讯作者:
HARPER, AE
中科院分区:
文献类型:
--
作者:
BRAND, LM;HARPER, AE
Glucagon administered subcutaneously to rats for 10 days had no significant effect on liver phenylalanine hydroxylase activity, but induced liver dihydropteridine reductase more than twofold. In rats administered a phenylalanine load orally, glucagon treatment stimulated oxidation and depressed urinary phenylalanine excretion. These responses could not be related to an effect of glucagon on hepatic tyrosine–α-oxoglutarate aminotransferase activity. Even in rats with phenylalanine hydroxylase activity depressed to 50% of control values byp-chlorophenylalanine administration, glucagon treatment increased the phenylalanine-oxidation rate substantially. Although hepatic phenylalanine–pyruvate aminotransferase was increased tenfold in glucagon-treated rats, glucagon treatment did not increase urinary excretion of phenylalanine transamination products by rats given a phenylalanine load. Glucagon treatment did not affect phenylalanine uptake by the gut or liver, or the liver content of phenylalanine hydroxylase cofactor. It is suggested that dihydropteridine reductase is the rate-limiting enzyme in phenylalanine degradation in the rat, and that glucagon may regulate the rate of oxidative phenylalanine metabolismin vivoby promoting indirectly the maintenance of the phenylalanine hydroxylase cofactor in its active, reduced state.