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(Received for publication, February 29, 1996, and in revised form, April 14, 1996)
From the The enzyme hepatic lipase may play several roles
in lipoprotein metabolism. Recent investigation has suggested a role
for the enzyme in lipoprotein and/or lipoprotein lipid uptake. To study
this, a simple isolated system that mimics the in vivo
system would be desirable. The enzyme is secreted by the hepatic
parenchymal cell but exists, and presumably exerts its effects, while
bound to capillary endothelial cells in the liver, adrenal gland, and
the ovary. We constructed a cDNA that encodes the expression of a
chimeric protein composed of rat hepatic lipase and the signal sequence
for the addition of the glycophosphatidylinositol (GPI) anchor from
human decay-accelerating factor. When transfected into Chinese hamster
ovary (CHO) cells this gave rise to a cell population that had
immunoreactive hepatic lipase on the cell surface. Cloning of the
transfected cells produced several cell lines that expressed the
chimeric protein bound to the cell surface by a GPI anchor. This was
documented by demonstrating incorporation of
[3H]ethanolamine into anti-hepatic lipase
immunoprecipitable material; in addition, hepatic lipase was released
from the cells by phosphatidylinositol-specific phospholipase C but not
by heparin. Phosphatidylinositol-phospholipase C treatment of cells
expressing the anchored lipase released material that comigrated with
hepatic lipase on SDS-polyacrylamide gel electrophoresis and was
immunoreactive with antibody to the cross-reacting determinant of GPI
anchors. Cell lysates containing the anchored protein contained
salt-resistant lipase activity, a known feature of the secreted hepatic
lipase; thus it appears that these cells have a surface-anchored
hepatic lipase molecule. Although it was not possible to demonstrate
lipolysis by the enzyme while it was on the cell surface for technical
reasons, the protein produced by these cells was active when studied in
cell membranes. The ability of the cells to take up lipoproteins was
studied. The cells demonstrated an increased affinity for low density
lipoprotein (LDL) receptor mediated uptake of LDL. They did not,
however, demonstrate any enhanced binding or removal of chylomicron
remnants. With respect to LDL and remnants, the cells expressing
anchored lipase behaved similarly to CHO cell that expressed secreted
hepatic lipase. The cells expressing anchored hepatic lipase had a
marked increase in the uptake of high density lipoprotein and high
density lipoprotein cholesteryl ester when compared to that seen with
CHO cells secreting hepatic lipase. This increase occurred primarily
via the selective pathway, and was not reduced by addition of anti-LDL
receptor or anti-hepatic lipase antibodies or the receptor-associated
protein. Together the results suggest that hepatic lipase, when bound
to the cell surface by a GPI anchor, plays a role in enhancing
lipoprotein uptake. For LDL this may involve the provision of a second
foot for particle binding, thus enhancing affinity for the LDL
receptor. For chylomicron remnants an additional molecule or molecules
are necessary to mediate this effect. For HDL, the enzyme facilitates
uptake of cholesteryl ester primarily by the selective pathway.
Volume 271, Number 28,
Issue of July 12, 1996
pp. 16906-16914
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
CHARACTERIZATION OF LOW DENSITY LIPOPROTEIN AND CHYLOMICRON
REMNANT UPTAKE AND SELECTIVE UPTAKE OF HIGH DENSITY
LIPOPROTEIN-CHOLESTERYL ESTER
,¶
Research Institute, Palo Alto Medical
Foundation, ¶ Department of Medicine, Stanford University and
§ Geriatric Research, Education and Clinical Center,
Veterans Administration Palo Alto Health Care System,
Palo Alto, California 94301
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