Two cholesterol ester hydrolases. Distribution in rat tissues and in cultured human fibroblasts and monkey arterial smooth muscle cells.
Hydrolytic activity against acetone-dispersed [4-14C]cholesterol oleate has been assayed as a function of pH in seven parenchymal tissues, blood cells, and plasma of the rat, as well as in cultured human fibroblasts and monkey (Macaca nemestrina) arterial smooth muscle cells. Both acid and neutral hydrolytic activities were present in all of these except rat plasma. The pH optima were in all cases close to pH 4.5 and pH 6.8. Acid activity was quite constant from tissue to tissue, while neutral activity varied greatly, being greatest in adrenal, testis, and adipose tissue. Subcellular fractionation of human fibroblasts allowed demonstration that activities at pH 4.5 and pH 6.8 were concentrated in different fractions, apparently lysosomal and polysomal, respectively. It appears most cell types, including fibroblasts and smooth muscle cells, contain two separate enzymes capable of hydrolyzing cholesterol esters. The neutral pH polysomal enzyme, which is especially prominent in certain tissues, may have a function related to the specialized roles of these tissues.
D000818:Animals; D002265:Carboxylic Ester Hydrolases / Q000378:metabolism*; D002478:Cells, Cultured; D005347:Fibroblasts / Q000201:enzymology; D000882:Haplorhini; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008251:Macaca; D008297:Male; D009130:Muscle, Smooth / Q000201:enzymology; D051381:Rats; D002787:Sterol Esterase / Q000097:blood / Q000378:metabolism*; D013347:Subcellular Fractions / Q000201:enzymology; D014018:Tissue Distribution
D002265:Carboxylic Ester Hydrolases; D002787:Sterol Esterase