Genetic Regulation of Hepatic Steroid 16α-Hydroxylase Activities in Inbred Strains of Mice*

Abstract

Steroid 16.alpha.-hydroxylase activities and properties were studied in C57BL/6J, 129/J, AKR/R, DBA/2J, C3H/I and BALB/c mouse liver using 4 different substrates. The highest enzymatic activities were measured in the female mice with the exception of the 129/J females. As in the rat liver, the sexual differentiation of the steroid 16.alpha.-hydroxylation observed in adult male and female mice took place at puberty. In the adult mouse layer, 2 steroid 16.alpha.-hydroxylase activities (forms I and II) could be differentiated on the basis of their relative affinities for the various steroid substrates and their relative proportions in male and female mouse livers. In the immature mouse liver, no sexual differences could be detected, and the mice of both sexes presented phenotypes identical to those of the adult female. The adult 129/J females appeared genetically deficient with respect to the form I of the steroid 16.alpha.-hydroxylase and presented a phenotype identical to that of the adult male mice of the various strains tested. Differences in hydroxylase activities between the C57Bl/6J and 129/J strains were investigated using standard genetic breeding protocols. Steroid 16.alpha.-hydroxylase seemed to be inherited additively in the liver of the female mice obtained by crossing the C57Bl/6J male and the 129/J female or the 129/J male and the C57Bl/6J female. In the male mice, regardless of genotype, the observed phenotype was always identical to the 2 male parental types. Both hormonal and genetic regulations were responsible for the different phenotypes occurring in adult male and female C57Bl/6J and 129/J mouse livers.