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Originally published In Press as doi:10.1074/jbc.M209649200 on October 9, 2002

J. Biol. Chem., Vol. 277, Issue 51, 49982-49988, December 20, 2002
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Scavenger Receptors Class A-I/II and CD36 Are the Principal Receptors Responsible for the Uptake of Modified Low Density Lipoprotein Leading to Lipid Loading in Macrophages*

Vidya V. KunjathoorDagger , Maria Febbraio§, Eugene A. Podrez, Kathryn J. MooreDagger , Lorna AnderssonDagger , Stephanie KoehnDagger , Jeongmi S. RheeDagger , Roy Silverstein§, Henry F. Hoff, and Mason W. FreemanDagger ||

From the Dagger  Lipid Metabolism Unit, Department of Medicine, Massachusetts General Hospital, Boston, Massachusetts 02114, § Department of Medicine, Division of Hematology and Medical Oncology and Center for Vascular Biology, Weill Medical College of Cornell University, New York, New York 10021, and the  Department of Cell Biology, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, Ohio 44195

Modification of low density lipoprotein (LDL) can result in the avid uptake of these lipoproteins via a family of macrophage transmembrane proteins referred to as scavenger receptors (SRs). The genetic inactivation of either of two SR family members, SR-A or CD36, has been shown previously to reduce oxidized LDL uptake in vitro and atherosclerotic lesions in mice. Several other SRs are reported to bind modified LDL, but their contribution to macrophage lipid accumulation is uncertain. We generated mice lacking both SR-A and CD36 to determine their combined impact on macrophage lipid uptake and to assess the contribution of other SRs to this process. We show that SR-A and CD36 account for 75-90% of degradation of LDL modified by acetylation or oxidation. Cholesteryl ester derived from modified lipoproteins fails to accumulate in macrophages taken from the double null mice, as assessed by histochemistry and gas chromatography-mass spectrometry. These results demonstrate that SR-A and CD36 are responsible for the preponderance of modified LDL uptake in macrophages and that other scavenger receptors do not compensate for their absence.

* This work was supported by Grant HL53315 (to H. F. H.) from the National Institutes of Health, a Scientist Development grant from the American Heart Association (to E. A. P.), Grant F32HL10366 from the National Institutes of Health (to V. V. K.), and Grants HL45098 and HL66678 from the National Institutes of Health (to M. W. F.).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.: 617-726-5906; Fax: 617-726-2879; E-mail: freeman@frodo.mgh.harvard.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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