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J. Biol. Chem., Vol. 277, Issue 29, 26565-26572, July 19, 2002
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From the The severe depletion of cholesteryl ester (CE) in
steroidogenic cells of apoA-I
Apolipoprotein A-I Is Necessary for the
in Vivo Formation of High Density Lipoprotein Competent for
Scavenger Receptor BI-mediated Cholesteryl Ester-selective Uptake*
,
Department of Pharmacological Sciences,
University Medical Center, State University of New York, Stony Brook,
New York 11794, the § Poultry Science Department, Texas A & M University, College Station, Texas 77843, and the ¶ Division of
Vascular Biology, La Jolla Institute for Molecular Medicine,
San Diego, California 92121
/ mice
suggests that apolipoprotein (apo) A-I plays a specific role in
the high density lipoprotein (HDL) CE-selective uptake process mediated
by scavenger receptor BI (SR-BI) in vivo. The nature of
this role, however, is unclear because a variety of apolipoproteins
bind to SR-BI expressed in transfected cells. In this study the role of
apoA-I in SR-BI-mediated HDL CE-selective uptake was tested via
analyses of the biochemical properties of apoA-I/ HDL and its interaction with SR-BI
on adrenocortical cells, hepatoma cells, and cells expressing a
transfected SR-BI. apoA-I/ HDL are large
heterogeneous particles with a core consisting predominantly of CE and
a surface enriched in phospholipid, free cholesterol, apoA-II, and
apoE. Functional analysis showed apoA-I/
HDL to bind to SR-BI with the same or higher affinity as compared with
apoA-I+/+ HDL, but
apoA-I/ HDL showed a 2-3-fold decrease in
the Vmax for CE transfer from the HDL particle
to adrenal cells. These results indicate that the absence of apoA-I
results in HDL particles with a reduced capacity for SR-BI-mediated
CE-selective uptake. The reduced Vmax illustrates that HDL properties necessary for binding to SR-BI are
distinct from those properties necessary for the transfer of HDL CE
from the core of the HDL particle to the plasma membrane. The
reduced Vmax for HDL CE-selective uptake
likely contributes to the severe reduction in CE accumulation in
steroidogenic cells of apoA-I/ mice.
*
This work was supported by National Institutes of Health
Grants HL 58012 and HL 60844.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.:
631-444-9685; Fax: 631-444-3218; E-mail:
dave@pharm.sunysb.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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