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Journal of Lipid Research, Vol 24, 869-876, Copyright © 1983 by Lipid Research, Inc.
M Bamberger, JM Glick and GH Rothblat
The objective of this study was to determine whether high density
lipoproteins (HDL) that have been treated with hepatic lipase have an
enhanced ability to deliver cholesterol to cells. Human HDL was incubated
with rat hepatic lipase, reisolated, and subjected to compositional
analysis. Approximately 28% of the HDL phosphatidylcholine was hydrolyzed
by the hepatic lipase but no change was detected in the cholesterol or
apoprotein content of the HDL compared to HDL incubated with
heat-inactivated hepatic lipase. Cultured rat hepatoma cells exposed to
hepatic lipase-modified HDL showed an increased uptake of HDL free
cholesterol relative to cells exposed to control HDL. This increased
delivery of HDL free cholesterol was demonstrated by both isotopic and mass
determinations and it contributed to a 1.6-fold increase in total cellular
cholesterol content relative to cells treated with control HDL. The free
cholesterol delivered by the HDL is functionally available to the cell as
evidenced by the conversion of radiolabeled free cholesterol to cholesteryl
ester. The stimulation of free cholesterol delivery was dose-dependent up
to a level of 100 micrograms of HDL free cholesterol/ml of extracellular
medium, and was directly related to the extent of phosphatidylcholine
hydrolysis. The enhanced cellular accumulation of HDL free cholesterol
observed with hepatic lipase appears to be due to the phospholipase
activity of this enzyme, since similar results were obtained with HDL that
had been modified by snake venom phospholipase A2.(ABSTRACT TRUNCATED AT
250 WORDS)
ARTICLES
Hepatic lipase stimulates the uptake of high density lipoprotein cholesterol by hepatoma cells
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