| Abstract: | The ingestion of glucose ad libitum (for 19 h to 3 days) decreased the levels of enzymes concerned with amino acid metabolism in liver and intestine (but not in kidney and brain) and raised those of hepatic glucokinase, pyruvate kinase and NADP-malate dehydrogenase.Glucose feeding inhibited the substrate and cortisol induction of tryptophan oxygenase; it did not diminish the induction of tyrosine aminotransferase by glucagon (in adrenalectomized rats) or of renal ornithine aminotransferase by estrogen and it enhanced the response of NADP-malate dehydrogenase to thyroxine. In hepatomas, as opposed to normal liver, 24 h of glucose feeding increased the basal and the cortisol-induced levels of tyrosine aminotransferase.The results obtained with endocrinectomized and hormone-treated rats led to the following conclusions: (1) the effects of glucose ingestion on the quantitative pattern of hepatic enzymes is not mediated through altered secretion of pituitary, adrenal or pancreatic hormones but presumably by metabolites of glucose; (2) glucose, ingested in large amounts over 1–3 days, is not an inhibitor of enzyme inductions in general: its effect varies with the enzyme, the inducer and the tissue in which the enzyme is located. |
