Cholesterol esterase activity of human intestinal mucosa.

It has been suggested that cholesterol absorption in humans is dependent on bile acid pool composition and that expansion of the cholic acid pool size is followed by an increase of the absorption values. Similar observations were reported in rats, where the increase of cholesterol absorption, after trihydroxy bile acid feeding, seems to be due to the stimulatory effect of cholic acid on the intestinal cholesterol esterase. In the present study, therefore, we investigated some general properties of human intestinal cholesterol esterase, with particular emphasis to the effect of bile acids on this enzymatic activity. Twenty-nine segments of small intestine were taken during operations; the enzymatic activity was studied by using mucosal homogenate as a source of enzyme and oleic acid, cholesterol, and 14C-labeled cholesterol as substrates. The time-activity relationship was linear within the first two hours; optimal pH for esterification ranged between 5 and 6.2. There was little difference between the esterifying activity of the jejunal and ileal mucosa. Esterification of cholesterol was observed with all the investigated fatty acids but was maximal with oleic acid. Bile acids did not affect cholesterol esterase activity when present in the incubation mixture at 0.1 and 1.0 mM; the enzymatic activity, however, was significantly inhibited when bile acids were added at 20 mM. In conclusion, this study has shown that the human intestinal mucosa possesses a cholesterol esterase activity; at variance with the rat, however, the human enzyme does not seem to be stimulated by trihydroxy bile acids. Thus, the stimulatory effect of cholic acid on cholesterol absorption induced by the administration of this bile acid does not seem to be simply due to changes of cholesterol esterase activity of the small bowel mucosa.