Ewha Med J.  1983 Mar;6(1):3-15. 10.12771/emj.1983.6.1.3.

Effects of Chronic Ethanol Administration and Cold Exposure on Rabbit Adrenocorticoid 11beta-Hydroxylase and 18-Hydroxylase Activities

• Lee DY
• Sung NE

• KMID: 1967724
• DOI: http://doi.org/10.12771/emj.1983.6.1.3

Abstract

Rabbit adrenocrtical mitochondria contains cytochrome P-450 dependent hydrox-ylase system, capable of catalyzing the hydroxylation as well as other modifications of variety of lipids and foreign compounds, including drugs, pesticides, carcino-gens. Ethanol enhances the activity of the microsomal enzyme system, and cold exposure increases various enzyme activity. The present study investigated the effects of chronic ethanol administration and cold exposure on rabbit adrenocortical mitochondria 11beta-and 18-hydroxylase activity, cytochrome P-450 and b5 and AAF hydroxylation, serum cortisol level and lipid content of the adrenal cortex. The results obtained are : 1) When rabbits were administrated with 15% and 30% ethanol and were exp-osed to cold, the level of adrenocortical mitochondrial 11 beta-hydroxylase activity was increased, but 18-hydroxylase activity was slightly increased only in the cold exposure group. This result corresponded with an increase of serum cortisol level. 2) When rabbits were administrated with ethanol and were exposed to cold, the level of cytochrome P-450 in adrenocortical mitochondria was increased, but cytochrome b5 level did not change. Ring-hydroxylation of AAF did not change, but N-hydroxylation was increased. 3) When rabbits were administrated with ethanol and were exposed to cold, the levels of total cholesterol and triglyceride in adrenal cortex was remarkably incre-ased, but phospholipid level was reduced.

MeSH Terms

Adrenal Cortex
Cholesterol
Cytochrome P-450 Enzyme System
Cytochromes b5
Ethanol*
Hydrocortisone
Hydroxylation
Mitochondria
Pesticides
Rabbits
Steroid 11-beta-Hydroxylase
Triglycerides
Cholesterol
Cytochrome P-450 Enzyme System
Cytochromes b5
Ethanol
Hydrocortisone
Pesticides
Steroid 11-beta-Hydroxylase