3-Hydroxy-3-methylglutaryl coenzyme a reductase activity in liver of athymic mice with or without an implanted human carcinoma.
Hydroxymethylglutaryl coenzyme A (HMG-CoA) reductase activities and cholesterol content in the liver of athymic mice either bearing or not an implanted human lung mucoepidormoid carcinoma (HLMC) and in the neoplasic tissue, were analyzed. The properties of the HMG-CoA reductase of HLMC grown in nude mice and those ones found in the liver of these animals, sacrificed either at mid-light or mid-dark, were similar. The hepatic reductase activity was found to be four- to five-fold greater at mid-dark than at mid-light (462 +/- 141 vs. 123 +/- 22 pmol min-1 mg protein-1). Since the Km value was not modified, the mid-dark activity could be due to an increase in the amount of enzyme. In contrast, HLMC reductase activity and cholesterol content showed similar values at mid-light and mid-dark points. HLMC reductase does not appear to have any diurnal variation and the cholesterol synthesis and content seems to be independent of food intake. HLMC-bearing nude mice undergo several alterations in the biosynthesis and homeostasis of cholesterol. Hypocholesterolemia, lower hepatic cholesterol content and higher HMG-CoA reductase activity are characteristic of host mice.
Polo
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Instituto de Investigaciones Bioquímicas de La Plata (INIBIOLP), Facultad de Cs. Médicas, UNLP-CONICET, Argentina.
de Bravo
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Carbone
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D000818:Animals; D018277:Carcinoma, Mucoepidermoid / Q000378:metabolism; D002784:Cholesterol / Q000032:analysis / Q000097:blood; D005260:Female; D006801:Humans; D006903:Hydroxymethylglutaryl CoA Reductases / Q000378:metabolism*; D025782:Hydroxymethylglutaryl-CoA-Reductases, NADP-dependent; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008175:Lung Neoplasms / Q000378:metabolism; D051379:Mice; D008819:Mice, Nude; D008862:Microsomes, Liver / Q000201:enzymology; D009368:Neoplasm Transplantation
D002784:Cholesterol; D006903:Hydroxymethylglutaryl CoA Reductases; D025782:Hydroxymethylglutaryl-CoA-Reductases, NADP-dependent