The defects in all classes of aryl hydrocarbon hydroxylase-deficient mutant of mouse hepatoma line, Hepa-1, are restricted to activities catalyzed by cytochrome P-450.
The extent of phenotypic derangement was investigated in representative aryl hydroxylase-deficient mutants of Hepa-1. One mutant is dominant while the others are recessive and are mutated in 3 different genes. All the mutants lacked ethoxyresorufin-O-deethylase activity as well as aryl hydrocarbon hydroxylase. However all had normal activities of NADPH-cytochrome P-450 reductase, epoxide hydrolase and ornithine decarboxylase. They also retained 2 liver-specific functions possessed by the parental line, namely albumin secretion and transferrin secretion. The phenotypic alterations in the mutants were therefore restricted to the cytochrome P-450 activities measured.
D000818:Animals; D001189:Aryl Hydrocarbon Hydroxylases / Q000172:deficiency*; D002460:Cell Line; D019363:Cytochrome P-450 CYP1A1; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D005799:Genes, Dominant; D005808:Genes, Recessive; D008114:Liver Neoplasms, Experimental / Q000235:genetics*; D051379:Mice; D009154:Mutation; D010088:Oxidoreductases / Q000172:deficiency; D010641:Phenotype
D003577:Cytochrome P-450 Enzyme System; D010088:Oxidoreductases; D001189:Aryl Hydrocarbon Hydroxylases; D019363:Cytochrome P-450 CYP1A1