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Journal of Lipid Research, Vol 18, 154-163, Copyright © 1977 by Lipid Research, Inc.
P Brecher, HY Pyun and AV Chobanian
Radiolabeled cholesteryl oleate, when incorporated into phospholipid
vesicles, was hydrolyzed at acid pH by an enzyme present in rabbit aortic
homogenates. In contrast, cholesteryl oleate presented as an acetone
dispersion was not effectively hydrolyzed at acid pH under identical
conditions. Using the vesicle preparation as substrate, a sensitive assay
system for the acid hydrolase was developed in which hydrolysis was
proportional to protein concentration and incubation time, and was
independent of substrate concentration. The physical state of the vesicles
was apparently not altered by the assay conditions, and no hydrolysis of
the vesicle-associated phospholipid was detected. Acid cholesterol esterase
activity in atherosclerotic aortic tissue was 2.5-fold greater than that of
control tissue, and even greater increases were observed in the activities
of other lysosomal enzymes (N-acetyl-beta-d-glucosaminidase and beta-
glucuronidase). Glucose-6-phosphatase activity was also increased in aortas
from cholesterol-fed animals while 5' nucleotidase activity remained
unchanged. Labeled triolein also was incorporated into phospholipid
vesicles and was hydrolyzed by an acid lipase in aortic tissue.
Similarities between triolein and cholesteryl oleate hydrolysis existed
with respect to pH optimum and the effect of cholesterol feeding on
activity, suggesting that a single enzyme may hydrolyze both lipids.
ARTICLES
Effect of atherosclerosis on lysosomal cholesterol esterase activity in rabbit aorta
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