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Volume 272, Number 50, Issue of December 12, 1997
pp. 31285-31292
(Received for publication, August 18, 1997, and in revised form, October 3, 1997)
From the High density lipoprotein (HDL)
particles and HDL cholesteryl esters are taken up by both
receptor-mediated and non-receptor-mediated pathways. Here we show that
cell surface heparan sulfate proteoglycans (HSPG) participate in
hepatic lipase (HL)- and apolipoprotein (apo) E-mediated binding and
uptake of mouse and human HDL by cultured hepatocytes. The HL secreted
by HL-transfected McA-RH7777 cells enhanced both HDL binding at 4 °C
(~2-4-fold) and HDL uptake at 37 °C (~2-5-fold). The enhanced
binding and uptake of HDL were partially inhibited by the 39-kDa
protein, an inhibitor of low density lipoprotein receptor-related
protein (LRP), but were almost totally blocked by heparinase, which
removes the sulfated glycosaminoglycan chains from HSPG. Therefore, HL
may mediate the uptake of HDL by two pathways: an
HSPG-dependent LRP pathway and an
HSPG-dependent but LRP-independent pathway. The HL-mediated
binding and uptake of HDL were only minimally reduced when
catalytically inactive HL or LRP binding-defective HL was substituted
for wild-type HL, indicating that much of the HDL uptake required
neither HL binding to the LRP nor lipolytic processing. To study the
role of HL in facilitating the selective uptake of cholesteryl esters,
we used HDL into which radiolabeled cholesteryl ether had been
incorporated. HL increased the selective uptake of HDL cholesteryl
ether; this enhanced uptake was reduced by more than 80% by heparinase
but was unaffected by the 39-kDa protein. Like HL, apoE enhanced the binding and uptake of HDL (~2-fold) but had little effect on the selective uptake of HDL cholesteryl ether. In the presence of HL, apoE
did not further increase the uptake of HDL, and at a high concentration
apoE impaired or decreased the HL-mediated uptake of HDL. Therefore, HL
and apoE may utilize similar (but not identical) binding sites to
mediate HDL uptake. Although the relative importance of cell surface
HSPG in the overall metabolism of HDL in vivo remains to be
determined, cultured hepatocytes clearly displayed an
HSPG-dependent pathway that mediates the binding and uptake
of HDL. This study also demonstrates the importance of HL in enhancing
the binding and uptake of remnant and low density lipoproteins via an
HSPG-dependent pathway.
Heparan Sulfate Proteoglycans Participate in Hepatic Lipaseand Apolipoprotein E-mediated Binding and Uptake of Plasma
Lipoproteins, Including High Density Lipoproteins
§
,¶
,
and§
**
Gladstone Institute of Cardiovascular
Disease, § Cardiovascular Research Institute, and the
Departments of ¶ Pediatrics, 
Pathology, and ** Medicine,
University of California, San Francisco, California, 94141-9100
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