Studies on Human Hepatic Cholesterol Ester Hydrolase in Liver Disease

1978 ◽  
Vol 38 (sup150) ◽  
pp. 218-222 ◽  
Author(s):  
J. B. Simon ◽  
R. W. M. Poon
1977 ◽  
Vol 75 (2) ◽  
pp. 235-243 ◽  
Author(s):  
J. P. RENSTON ◽  
T. J. IHRIG ◽  
R. H. RENSTON ◽  
B. GONDOS ◽  
R. J. MORIN

The characteristics and localization of a cholesterol ester hydrolase enzyme in homogenates of whole testis and in isolated seminiferous tubules and interstitial cells of mature rats have been investigated. Hydrolysis of cholesteryl [1-14C]oleate occurred at an optimum pH of 7·0 was linearly related to time up to 5–6 h of incubation and increased linearly up to 0·25 mg protein/incubation. Hydrolytic activity was inhibited by increasing the incubation temperature from 29 to 41 °C and by sonication. Cholesterol ester hydrolase activity/mg protein was three times greater in homogenates of seminiferous tubules than in interstitial cells. Cholesterol ester hydrolase may function to provide precursors for use in seminiferous tubular steroid hormone biosynthesis or germ cell maturation.


FEBS Letters ◽  
1986 ◽  
Vol 201 (2) ◽  
pp. 257-261 ◽  
Author(s):  
Roger J. Colbran ◽  
Andrew J. Garton ◽  
Susan R. Cordle ◽  
Stephen J. Yeaman

PEDIATRICS ◽  
1989 ◽  
Vol 83 (6) ◽  
pp. 1074-1075
Author(s):  
MOSHE WOLMAN

Presently available information indicates that Wolman disease is due to a defect in a single lysosomal enzyme molecule, called acid lipase, esterase, or cholesterol ester hydrolase (EC3.1.1.13). Cells of the reticuloendothelial system, hepatocytes, adrenocortical, and presumably many other cells normally, contain a neutral esterase associated with their microsomes, which is not deficient in Wolman disease. Theoretically, catabolism of intracellular hydrophobic cholesterol (esters and triglycerides) should proceed normally in Wolman disease cells whenever the metabolic chain does not depend on lysosomal hydrolysis.


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