© 1995 American Heart Association, Inc.
Articles |
Oxidized LDL Binds to CD36 on Human Monocyte-Derived Macrophages and Transfected Cell Lines
Evidence Implicating the Lipid Moiety of the Lipoprotein as the Binding Site
From the Departments of Pathology (A.C.N.) and Medicine (S.F.A.P., R.L.S.), Cornell University Medical College, New York, NY.
Correspondence to Andrew C. Nicholson, Cornell University Medical College, Department of Pathology, Room A-626, New York, NY 10021.
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Abstract |
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Abstract Accumulating evidence strongly implicates oxidized LDL (Ox-LDL) in the pathogenesis of atherosclerosis. Several receptors have been identified that bind and internalize Ox-LDL, but their relative importance in vivo is unclear. CD36 is an 88-kD transmembrane glycoprotein expressed on monocytes/macrophages, platelets, and microvascular endothelium that has been implicated as a putative receptor for Ox-LDL. We demonstrate that an anti-CD36 monoclonal antibody inhibited 50% of the specific binding and 26% of the specific degradation of Ox-LDL by human monocyte–derived macrophages. To characterize more completely this binding we evaluated interactions between CD36 and Ox-LDL in murine NIH-3T3 cells stably transfected with human CD36 cDNA. Ox-LDL bound to CD36-transfected 3T3 cells in a saturable manner. Specific binding, internalization, and degradation of Ox-LDL were increased fourfold in CD36-transfected cell lines compared with 3T3 cells transfected with vector alone. Binding of Ox-LDL to CD36-transfected 3T3 cells was inhibited by a panel of anti-CD36 antibodies and by soluble CD36 but not by thrombospondin. Specificity of binding was demonstrated by the equivalent binding of LDL and acetylated LDL to control and CD36-transfected 3T3 cells. The epitope or epitopes on Ox-LDL recognized by CD36 are undefined. Two observations suggest that CD36 recognizes a lipid moiety or that the lipid portion of the lipoprotein is essential for apoprotein recognition. The first is that the increased binding of Ox-LDL to CD36-transfected 3T3 cells is abrogated by delipidation of the lipoprotein, and the second is that oleic acid competes for the binding of Ox-LDL to CD36-transfected 3T3 cells. These data demonstrate that CD36 functions as an Ox-LDL receptor and suggest that CD36 may play a functional role in lipid accumulation by human macrophages and subsequent foam cell development during atherosclerosis.
Key Words: CD36 • oxidized LDL • macrophage • scavenger receptor • atherosclerosis
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Introduction |
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Macrophage-derived cholesteryl ester–laden foam cells are a characteristic feature of the atherosclerotic lesion.1 Accumulating evidence suggests that oxidized LDL (Ox-LDL) is the source of this lipid and that scavenger receptors—receptors that recognize, bind, and internalize modified forms of LDL such as acetylated LDL (Ac-LDL) and Ox-LDL—mediate foam cell development.2 3 Scavenger receptors were initially identified in patients with familial hypercholesterolemia.4 It was observed that these patients accumulate cholesteryl ester within macrophages of atherosclerotic plaques, but they lack LDL receptors. A macrophage scavenger receptor that mediates the binding and internalization of Ac-LDL has been isolated.5 6 Two macrophage scavenger receptor genes, type I and type II, have recently been cloned. They encode homotrimeric membrane proteins with collagen domains, differing only at the C terminus.7 8 9 These receptors are expressed on macrophages and exhibit broad ligand-binding specificity, recognizing modified forms of LDL, four-stranded nucleic acids (polyinosinic acid), polysaccharides (dextran sulfate, fucoidan), and endotoxin.10
Modification of LDL by acetylation, acetoacetylation, or malondialdehyde treatment abolishes the positive charge on lysine residues of LDL, which prevents recognition by the LDL receptor but facilitates recognition by the scavenger receptor. Because these modifications do not occur under physiological conditions, the natural ligand for this receptor was unclear until it was demonstrated by Steinberg and his colleagues (Parthasarathy et al11 ) that Ox-LDL competes for the binding of Ac-LDL to macrophages. However, this competitive inhibition was only partial. Binding studies with both Ox-LDL and Ac-LDL demonstrated the existence of a scavenger receptor or receptors that recognized both Ac-LDL and Ox-LDL and another receptor that recognized Ox-LDL but not Ac-LDL.12 A similar conclusion was reached by Arai et al.13 Using cross-competition experiments in mouse peritoneal macrophages, they concluded that macrophage receptors for modified LDL consist of at least three different receptors: a receptor that recognizes Ac-LDL, one that recognizes Ox-LDL, and a third that recognizes both. Nonreciprocal cross competition between Ac-LDL and Ox-LDL was also demonstrated in Chinese hamster ovary cells transfected with type I and type II bovine scavenger receptors.14 The type I and II receptors exhibited a similar binding specificity; thus, it does not appear that differences at the C terminus account for differences in ligand recognition. At least two potential mechanisms could explain these data: The scavenger receptor could have different binding sites for Ac-LDL and Ox-LDL, or there may be as yet uncharacterized scavenger receptors with distinctive binding properties.
Recently an expression cloning strategy was used to identify mouse
macrophage receptors that recognize Ox-LDL but not Ac-LDL. Two clones
were identified. The first encoded an Fc receptor for IgG,
Fc
RII-B2.15 Transfection of the receptor into a cell
line without intrinsic scavenger receptor activity resulted in the
ability of these cells to internalize and degrade Ox-LDL. However, the
physiological relevance of this receptor is questionable because
antibodies directed against FcRII-B2 did not block the binding of
Ox-LDL to macrophages.15 The second clone isolated encoded
the mouse homologue of CD36,16 an 88-kD membrane
glycoprotein expressed on monocytes/macrophages,17
platelets,18 microvascular endothelial cells, breast
epithelium, and some tumor cell lines.19 CD36 has been
shown to function as an adhesion receptor for collagen,20
thrombospondin,21 and Plasmodium
falciparum–infected erythrocytes.22 In this study,
we present evidence implicating CD36 as a specific Ox-LDL receptor
on human monocyte–derived macrophages. We demonstrate for the first
time that, unlike the case with the scavenger receptor, which
recognizes the modified apoprotein portion of the lipoprotein, the
lipid moiety of Ox-LDL mediates binding to CD36.
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Methods |
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Materials
Disposable tissue culture materials were purchased from Corning Glass Works. Amphotericin B (Fungizone) was purchased from Flow Laboratories, Inc. RPMI, L-glutamine, penicillin/streptomycin, and human serum were purchased from GIBCO Laboratories. Iodine-125 was purchased from ICN Biochemicals. Sodium oleate and sodium linoleate were obtained from Sigma Chemical Co.
Cells and Cell Lines
Human monocytes were isolated from the blood of volunteer
donors. They were propagated in RPMI medium containing 5% human serum,
penicillin/streptomycin, and amphotericin ß. The monocytes were
allowed to adhere overnight, and the nonadherent cells were removed by
washing two times with phosphate-buffered saline (PBS). Binding studies
were performed after 1 week in culture. CHO-K1 cells and NIH-3T3 cells
were transfected with a eukaryotic expression vector, pMV7, containing
the full coding sequence of CD36 driven by a viral LTR promoter as
described.21 Transfected cells were selected with GM418.
CD36 expression on transfected 3T3 cells was demonstrated by flow
cytometry. Mock-transfected (vector alone) or CD36-sense
cDNA–transfected cells were incubated in suspension with murine
monoclonal anti-CD36 IgG 8A6 (2 µg/mL) in Hanks' balanced
salts/bovine serum albumin for 30 minutes at 4°C. Cells were then
pelleted, resuspended in Phycoerythrin (PE)-conjugated goat anti-mouse
IgG for 20 minutes at 22°C, and analyzed by flow cytometry. CD36
expression was evident on the transfected cells but not on the
mock-transfected cells.
Isolation, Labeling, and Oxidation of LDL
LDL (density, 1.019 to 1.063 g/mL) was prepared from human
plasma and isolated by ultracentrifugation.23 The LDL was
dialyzed against HEPES-buffered saline with EDTA, sterilized by
filtration through a 0.22-µm filter, and stored under nitrogen gas at
4°C. LDL was iodinated by the method of Bilheimer et
al24 as described by Goldstein et al25 using
carrier-free 125I-NaCl (Amersham Corp). LDL and
125I-LDL were fully oxidized by dialyzing against PBS with
5 µmol/L CuSO4 at 37°C for 16 hours. The specific
activity of the 125I-Ox-LDL was approximately 100
cpm/ng.
Delipidation of 125I-Ox-LDL
125I-Ox-LDL was delipidated by the method of Bligh
and Dyer as described by Parthasarathy et al.26 The
apoprotein was solubilized in an aqueous solution of octyl glucoside (6
mg/mL) and dialyzed against PBS.
Ox-LDL Binding, Internalization, and Degradation
The binding, internalization, and degradation of Ox-LDL was
performed according to the methods of Goldstein et al25
using 125I-Ox-LDL. For binding studies,
125I-Ox-LDL was added to cells in the presence or absence
of a 25- to 50-fold excess of unlabeled Ox-LDL at 4°C on a rotary
shaker. After 2 hours the cells were washed three times with ice-cold
PBS containing 2 mg/mL bovine serum albumin and then twice with
ice-cold PBS. The cells were then solubilized in NaOH (0.2 mol/L).
Radioactivity was quantified by gamma spectroscopy, and aliquots were
taken for protein determination. For internalization and degradation
studies, cells were exposed to 125I-Ox-LDL (20 µg/mL) at
37°C for 5 hours. Supernatants were assayed for trichloroacetic acid
(TCA)–nonprecipitable radioactivity as well as TCA-soluble noniodide
radioactivity. Specific binding, internalization, and degradation were
determined as total binding minus nonspecific (in the presence of
excess cold) binding. Internalization represents
cell-associated 125I-Ox-LDL after multiple washes with PBS
and an acid-glycine wash (50 mmol/L glycine, 100 mmol/L NaCl, pH 3).
That there was some residual cell surface–bound
125I-Ox-LDL cannot be completely ruled out, but it is
unlikely.
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Results |
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Macrophages express CD36 and are the primary cells that become foam cells during atherosclerosis. To determine the role of CD36 relative to other binding sites for Ox-LDL, we performed binding studies with 125I-Ox-LDL on human peripheral blood monocyte–derived macrophages with and without 8A6, an anti-CD36 monoclonal antibody. We observed that 50% of the specific binding of Ox-LDL to human monocyte–derived macrophages was inhibited by an anti-CD36 IgG (Fig 1
). No inhibition was seen with a
control monoclonal antibody against CD11/18. In studies performed at
37°C, 8A6 inhibited 26% of the specific degradation of
125I-Ox-LDL by human monocyte–derived macrophages (Fig 2).
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Because human monocyte–derived macrophages express the cloned types I
and II scavenger receptors for Ox-LDL, CD36 cDNA–transfected cell
lines were used in subsequent studies to characterize the role of CD36
in a more defined system. CHO-K1 cells and NIH-3T3 cells, neither of
which expresses CD36, were transfected with a eukaryotic expression
vector, pMV7, that contained the full coding sequence of CD36 and the
gene for neomycin resistance.21 Stable transfectants were
selected in GM418 antibiotic-containing media. CD36 surface expression
in the transfected cells was demonstrated by flow cytometry. CD36 was
expressed on transfected cells but not on the mock-transfected (vector
alone) 3T3 cells (data not shown). The binding of
125I-Ox-LDL was increased twofold by CD36-transfected
CHO-K1 cells and fourfold by CD36-transfected 3T3 cells compared with
their respective control cells transfected with the vector alone (Fig 3). This is consistent with the degree of CD36
expression in transfected 3T3 cells compared with CHO-K1 cells. Only
the CD36-transfected 3T3 cells were used in subsequent studies. Ox-LDL
bound to CD36-transfected 3T3 cells in a saturable manner (Fig 4). Binding of Ox-LDL to CD36-transfected 3T3 cells was
inhibited by 8A6, a monoclonal anti-CD36 IgG antibody. Four additional
monoclonal anti-CD36 antibodies as well as a polyclonal rabbit
anti-CD36 antibody had similar inhibitory effects (data not shown). In
addition, coincubation of 125I-Ox-LDL with purified
platelet CD36 (50 µg/mL) markedly inhibited binding by approximately
90%. However, coincubation with thrombospondin did not affect the
binding of 125I-Ox-LDL to CD36-transfected 3T3 cells (Fig 5). To evaluate whether the bound ligand was
internalized and degraded, the specific binding, internalization, and
degradation of Ox-LDL were measured in the transfected cell line at
37°C. Internalization and degradation were increased fourfold in
CD36-transfected cell lines compared with 3T3 cells transfected with
vector alone (Fig 6). To demonstrate the specificity of
the interaction of Ox-LDL and CD36, we evaluated the binding of
125I-LDL (LDL receptor ligand) and Ac-LDL labeled with
iodine-125 (125I-Ac-LDL) (scavenger receptor ligand) to
control cells and CD36-transfected 3T3 cells (Fig 7).
The binding of 125I-LDL and 125I-Ac-LDL was
equivalent in CD36-transfected 3T3 cells and mock-transfected 3T3
cells. Furthermore, neither cold Ac-LDL nor LDL inhibited the binding
of 125I-Ox-LDL to CD36-transfected cells (data not
shown).
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The epitope or epitopes on Ox-LDL that are recognized by CD36 are
undefined. Two observations suggest that CD36 recognizes a lipid moiety
or that the lipid portion of the lipoprotein is essential for
apoprotein recognition. The first is that the increased binding of
Ox-LDL to CD36-transfected 3T3 cells is abrogated by delipidation of
the lipoprotein (Fig 8). The second is that coincubated
fatty acids (oleic and linoleic) compete for the binding of Ox-LDL to
CD36-transfected 3T3 cells. (Fig 9). Oleic acid (sodium
oleate, 100 µmol/L) significantly inhibited binding of
125I-Ox-LDL to CD36-transfected 3T3 cells. Specific binding
was inhibited by 70%. Linoleic acid (sodium linoleate, 100 µmol/L)
had a modest inhibitory effect. Phosphatidylcholine and
phosphatidylserine liposomes (100 µmol/L), lysophosphatidylcholine
(up to 100 µmol/L), and 4-hydroxynonenal (up to 100 µmol/L) had no
effect (data not shown).
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Discussion |
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Our data demonstrate that CD36 functions as an Ox-LDL receptor in human monocyte–derived macrophages. An anti-CD36 monoclonal antibody inhibited approximately 50% of the specific binding and 26% of the specific degradation of Ox-LDL in human monocyte–derived macrophages, implicating CD36 as a major receptor for oxidatively modified forms of LDL. These data suggest that CD36 may play a functional role in lipid accumulation by human macrophages and subsequent foam cell development during atherosclerosis.
Interactions between CD36 and Ox-LDL were evaluated in murine NIH-3T3
cells stably transfected with human CD36 cDNA. Ox-LDL bound to
CD36-transfected 3T3 cells in a saturable and specific manner. LDL
binding was equivalent in transfected and sham-transfected cells, as
was Ac-LDL binding. Binding, internalization, and degradation of Ox-LDL
were increased fourfold in CD36-transfected cell lines compared with
3T3 cells transfected with vector alone. However, the absolute amount
of degraded 125I-Ox-LDL in CD36-transfected 3T3 cells is at
least an order of magnitude less than the amount in macrophages.
Interestingly, the amount of cell-associated Ox-LDL was three to four
times greater than degraded Ox-LDL (Fig 6
). This ratio of
cell-associated to degraded lipoprotein is normally reversed in
macrophages and smooth muscle cells over similar time periods at
37°C. The reason for reversal of the usual ratio is unclear, but it
may reflect an uncoupling of binding and internalization from lysosomal
degradation in the transfected cells.
It is likely that the cloned type I and type II scavenger receptors are two members of what may be a large family of scavenger receptors with broad ligand specificity.27 28 29 Recently Krieger and his colleagues (Acton et al30 ) identified a Class B scavenger receptor, SR-BI, that binds both Ox-LDL and Ac-LDL and has 30% homology to CD36. With regard to receptors that recognize modified lipoproteins, it appears that there may be at least three independent receptors: one that recognizes Ac-LDL, another that recognizes Ox-LDL, and a third that recognizes both.12 13 Scavenger receptor activity has been observed in hepatic tissue on endothelial cells and Kupffer cells and, to a lesser degree, on parenchymal cells of the liver.31 32 Results of both in vivo and in vitro studies suggest that scavenger receptor activity on endothelial cells and Kupffer cells is probably not mediated by the cloned type I and type II scavenger receptors. Rabbit venous endothelial cells and bovine aortic endothelial cells bind and degrade Ac-LDL, but they do not express mRNA for the macrophage or smooth muscle cell scavenger receptor. This suggests that the endothelial cell scavenger receptor is a distinct entity.33 Injected 125I-Ac-LDL in rats is taken up primarily by the liver and predominantly by endothelial cells.31 However, 125I-Ox-LDL is cleared predominantly by Kupffer cells.34 De Rijke and Van Berkel35 found that when Kupffer cell membranes were isolated, two sites of 125I-Ox-LDL binding were identified by ligand blotting: a major binding site with a mass of 95 kD and a minor site, the cloned Ac-LDL receptor, with a mass of 220 kD. The authors suggest that the 95-kD protein is the most likely candidate to function as a specific Ox-LDL receptor in the liver. They further speculate, on the basis of the molecular weight of this receptor, that CD36 (MW 88 kD) is a potential candidate for the hepatic Ox-LDL receptor.
The physiochemical changes that occur in the LDL particle and that impart scavenger receptor recognition are complex and incompletely understood. Initially, during the oxidative process, there is a rapid depletion of LDL-associated antioxidants, such as vitamin E and carotenoids. This is followed by oxidation of polyunsaturated fatty acids, decomposition and fragmentation of fatty acids, and generation of reactive aldehydes. The loss of linoleic acid and arachidonic acid is concomitant with the generation of their specific hydroxyl and hydroperoxy derivatives. Phosphatidylcholine undergoes hydrolysis to lysophosphatidylcholine. Cholesterol is oxidized, leading to the formation of oxy-sterols. These changes precede the fragmentation of apoprotein B.36 37 38 Aldehydes generated during lipid peroxidation form Schiff bases with lysine residues of apoprotein B, resulting in a negative charge of the molecule.39 40 It is believed that the resulting negative charge of the LDL particle is responsible for interaction of the Ox-LDL with the scavenger receptor.
Our data demonstrate that recognition of Ox-LDL by CD36 differs from
scavenger receptor recognition. The binding of Ox-LDL to the scavenger
receptor is mediated by the apoprotein moiety of the lipoprotein.
Delipidated and resolubilized 125I-Ox-LDL is degraded by
macrophages, and intact Ox-LDL competes for this
degradation.26 Studies of a mutant scavenger receptor with
the use of C-terminus deletion demonstrate that the
positively charged collagen domain of the receptor mediates the
recognition of negatively charged macromolecules such as Ac-LDL and
Ox-LDL.8 41 The mechanism of interaction between CD36 and
Ox-LDL remains to be determined. However, the binding of delipidated
and resolubilized 125I-Ox-LDL was not increased in
CD36-transfected 3T3 cells (Fig 8), which suggests that CD36 does not
recognize the apoprotein without the lipid moiety. Furthermore, binding
could be partially inhibited by coincubation of 125I-Ox-LDL
with oleic and, to a lesser extent, linoleic acid (Fig 9).
Phosphatidylcholine and phosphatidylserine liposomes,
lysophosphatidylcholine, and 4-hydroxynonenal had no effect. This
suggests that oleic acid is recognized by and binds to CD36 or that the
fatty acid may inhibit binding of Ox-LDL by acting in a steric manner
(perhaps after incorporation into the surface phospholipid layer). The
recent cloning of a rat adipocyte membrane protein, fatty acid
transport protein (FAT), supports this hypothesis. The cDNA of FAT is
85% homologous to CD36, suggesting that this protein is the rat
homologue of human CD36.42 FAT has been implicated in the
binding or transport of long-chain fatty acids, particularly oleate. It
is conceivable that CD36 recognizes fatty acid(s) or oxidized fatty
acid(s) within the phospholipid layer of the lipoprotein and is the
binding site of the molecule.
Interestingly, CD36 has also been shown to function in macrophage scavenging of apoptotic cells43 and in retinal epithelial scavenging of shed photoreceptor outer rod segments.44 Both apoptotic cells and shed outer rod segments express modified phospholipids on their outer surfaces,45 suggesting that CD36 recognition of oxidized lipid may play an important role in several biological systems. The ligand-binding site on CD36 for Ox-LDL is as yet undetermined. Thrombospondin, which has previously been shown to be a CD36 ligand, did not compete with Ox-LDL for binding to CD36.
Our data implicate CD36 as an Ox-LDL receptor in human monocyte–derived macrophages, the principal foam cells of the atherosclerotic lesion. Our data support the concept of CD36 as a unique scavenger receptor that binds and internalizes Ox-LDL but does not bind LDL or Ac-LDL. CD36 is thus a member of the expanding family of scavenger receptors. We demonstrate that, in vitro, an anti-CD36 monoclonal antibody inhibited 50% of the specific binding and 26% of the specific degradation of Ox-LDL to human monocyte–derived macrophages. Furthermore, we implicate the lipid moiety of Ox-LDL as the binding site recognized by CD36. The relative extent to which CD36 and other scavenger receptors participate in the binding and uptake of modified lipid in vivo and the role of the receptors in the atherosclerotic process remain to be determined.
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Acknowledgments |
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This work was supported by National Institutes of Health grants RR-00085 (A.C. Nicholson), HL-42540 (Roy L. Silverstein), and HL-46403 (A.C. Nicholson, Roy L. Silverstein) We thank John Shuman, Rene Crombie, Qinghu Zheng, and Lewis Yesner for technical expertise.
Received August 2, 1994; accepted November 8, 1994.
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