Premium
Characterization of a cytosolic protein inhibiting lysosomal acid cholesteryl ester hydrolase
Author(s) -
Tanaka Mitsuo,
Yonekura Ryooji,
Iio Toshihiro,
Tabata Toshikazu
Publication year - 1984
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02534464
Subject(s) - biochemistry , cholesteryl ester , cytosol , chemistry , cathepsin d , hydrolase , trypsin , enzyme , chymotrypsin , lipase , acid phosphatase , hydrolysis , digestion (alchemy) , chromatography , cholesterol , lipoprotein
An inhibitor of lysosomal acid cholesteryl ester hydrolase (Acid CEH), (EC 3.1.1.13) was found in the cytosolic fraction of rat liver and various other tissues. The extent of the inhibitory effect was dependent on the concentration of the cytosolic protein. The Acid CEH inhibitor was heat‐labile, nondialyzable, and its inhibitory activity significantly decreased by trypsin or chymotrypsin digestion, but not by lipase digestion. The inhibitor had no effect on the activity of cathepsin D, β‐glucuronidase and acid phosphatase, which are other enzymes found in lysosomes. The present findings suggest that the inhibitor may be involved in the regulation of the hydrolysis of cholesteryl esters in lipoproteins that have been transferred into the liver.