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J. Biol. Chem., Vol. 275, Issue 43, 33409-33415, October 27, 2000
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From the The phospholipids of lipoproteins can be
transferred to cells by an endocytosis-independent uptake pathway. We
analyzed the role of scavenger receptor BI (SR-BI) for the selective
cellular phospholipid import. Human monocytes rapidly acquired the
pyrene (py)-labeled phospholipids sphingomyelin (SM),
phosphatidylcholine, and phosphatidylethanolamine from different donors
(low and high density lipoproteins (LDL, HDL), lipid vesicles). The
anti-SR-BI antibody directed against the extracellular loop of the
membrane protein lowered the cellular import of the phospholipids by
40-80%. The phospholipid transfer from the lipid vesicles into the
monocytes was suppressed by LDL, HDL, and apoprotein AI. Transfection
of BHK cells with the cDNA for human SR-BI enhanced the cellular import of the vesicle-derived py-phospholipids by 5-6-fold. In the
case of the LDL donors, transfer of py-SM to the transfected cells was
stimulated to a greater extent than the uptake of the other
py-phospholipids. Similar differences were not observed when the
vesicles and HDL were used as phospholipid donors. The concentration of
LDL required for the half-maximal phospholipid import was close to the
previously reported apparent dissociation constant for LDL binding to
SR-BI. The low activation energy of the SR-BI-mediated py-phospholipid
import indicated that the transfer occurs entirely in a hydrophobic
environment. Disruption of cell membrane caveolae by cyclodextrin
treatment reduced the SR-BI-catalyzed incorporation of py-SM,
suggesting that intact caveolae are necessary for the phospholipid
uptake. In conclusion, SR-BI mediates the selective import of the major
lipoprotein-associated phospholipids into the cells, the transfer
efficiency being dependent on the structure of the donor lipoprotein.
Scavenger Receptor BI Transfers Major Lipoprotein-associated
Phospholipids into the Cells*
,,
Physiologisches Institut der
Universität München, Schillerstrasse 44, 80336 München, Germany, the § Institut für
Biochemie, Eidgenössische Technische Hochschule Zürich,
8092 Zürich, Switzerland; and ¶ Boehringer Ingelheim Pharma
KG, 88397 Biberach, Germany
*
This work was supported by grants from the Deutsche
Forschungsgemeinschaft (to B. E.).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.:
49-89-5996-409; Fax: 49-89-5996-378; E-mail:
bernd.engelmann@physiol.med.uni-muenchen.de.
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