Biochemical properties of liver peroxisomes from rat, guinea pig and human species and the influence of hormonal status on rat liver acyl-CoA oxidase mRNA content

Abstract

Liver peroxisomes from three different species, rat, guinea pig and man, have been purified by ultracentrifugation on a discontinous Nycodenz gradient. Several biochemical parameters were tested in order to compare the basic peroxisomal properties of liver from rat, a species strongly responsive to peroxisome proliferators, and guinea pig and man, two weakly responsive species. Polypeptide patterns were compared and the bands in guinea pig and man comigrating with the two major bands in rat, catalase at 66 kDa and urate oxidase at 35 kDa, appeared in low amounts. However, other polypeptides are similar througout these species especially in guinea pig as revealed by cross-immunoreactivity using an anti-rat peroxisomal protein rabbit immuneserum. Specific activities of peroxisome acyl-CoA oxidase and microsome ω-lauryl hydroxylase have comparable rates in rat and guinea pig liver, but in human liver the activities are much lower. There is a cross-hybridization between acyl-CoA oxidase mRNA probed by rat liver acyl-CoA oxidase cDNA among the three species at a medium stringency. But interestingly, acyl-CoA oxidase mRNA from guinea pig and man appear to be larger in size. On the other hand, the hormonal status does not seem to have a significant effect on the rat liver acyl-CoA oxidase mRNA level suggesting at most that insulin, corticosterone and estradiol have no direct effect on acyl-CoA oxidase gene expression, which contrasts with the well-known effect of peroxisome proliferators.