SEX-RELATED DIFFERENCE IN THE EFFECT OF CLOFIBRIC ACID ON INDUCTION OF 2 NOVEL LONG-CHAIN ACYL-COA HYDROLASES IN RAT-LIVER

  • 1 January 1982
    • journal article
    • research article
    • Vol. 712  (1) , 48-56
Abstract
The sex difference in the induction of 2 novel long-chain acyl-CoA hydrolases in hepatic cytosol of rats by clofibric acid (p-chlorophenoxylisobutyric acid) [a hypolipidemic drug] feeding and the properties of the induced acyl-CoA hydrolases were investigated. Marked sex-related difference was observed in the induction of acyl-CoA hydrolase activity. The sex difference was mainly due to the difference in the induction of acyl-CoA hydrolase with higher MW (hydrolase I), but not to the difference in the induction of acyl-CoA hydrolase with lower MW (hydrolase II). The extent of the induction of the hydrolase I in hepatic cytosol of male rats was 3.5 times greater than that of female rats. Castration of male rats resulted in the marked depression of the ability to induce hydrolase I. The administration of testosterone to the castrated male rats stored completely the ability to induce hydrolase I. Unlike hydrolase I, the ability to induce hydrolase II did not respond to the changes in state of androgen. The administration of di-(2-ethylhexyl)phthalate also induced both hydrolase I and II, although the extent of the induction of hydrolase I was less compared to that by clofibric acid treatment. Marked sex difference was observed in the induction of the hydrolase I on di-(2-ethylhexyl)phthalate administration. These 2 hydrolases showed different kinetic properties and different substrate specificities to each other. Hydrolase I was inhibited by bovine serum albumin in vitro but was not affected by Mg2+. Hydrolase II was activated slightly in the presence of lower concentrations of bovine serum albumin, Mg2+ or Ca2+.

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