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Molecular Pharmacology, Vol 13, 60-69, Copyright © 1977 by the American Society for Pharmacology and Experimental Therapeutics

Pyridine Nucleotide-Dependent Electron Transport in Kidney Cortex Microsomes: Interaction with Desaturase and Other Microsomal Mixed-Function Oxidases

MARK R. MONTGOMERY 1 and DOMINICK L. CINTI 2

1 Pulmonary-Toxicology Laboratory and Research Service, Veterans Administration Hospital, and Departments of Pharmacology and Medicine, University of Minnesota, Minneapolis, Minnesota 55455
2 Department of Pharmacology, University of Connecticut Health Center, Farmington, Connecticut 06032

Rat kidney cortex microsomes contain both cytochrome b5 and its flavoprotein reductase, yet do not catalyze fatty acyl-CoA desaturation. This inactivity was unaltered by feeding a high-carbohydrate diet. However, supplementation of liver or lung microsomes with kidney microsomes produced a significant increase in desaturase activity. Kidney microsomes had no effect on liver N-demethylation or aromatic p-hydroxylation and only an additive effect on aryl hydrocarbon hydroxylase activity, suggesting specificity for the kidney-dependent synergism of desaturase. Although stearoyl-CoA is not desaturated by kidney microsomes, it did inhibit both kidney aryl hydrocarbon hydroxylase activity and NADH-cytochrome c reductase activity, which was restored to the control level by cyanide; stearic acid had no effect on reductase activity. These results suggest the presence of a desaturase electron transport system in kidney which may lack a factor(s) normally present in liver and lung.

Submitted on May 27, 1976
Accepted on August 19, 1976




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