© 1999 American Heart Association, Inc.
Rapid Communication |
Expression of Human Scavenger Receptor Class B Type I in Cultured Human Monocyte-Derived Macrophages and Atherosclerotic Lesions
Presented in part at the 71st Scientific Sessions of the American Heart Association, Dallas, Tex, November 8–11, 1998.
From the Department of Internal Medicine and Molecular Science, Graduate School of Medicine, Osaka University, Osaka, Japan.
Correspondence to Ken-ichi Hirano, MD, PhD, Department of Internal Medicine and Molecular Science, Graduate School of Medicine, B5, Osaka University, 2-2, Yamadaoka, Suita, Osaka 565-0871, Japan. E-mail khirano{at}kb3.so-net.ne.jp
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Abstract |
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Abstract—The scavenger receptor class B type I (SR-BI) and its human homologue CLA-1 (CD36 and LIMPII Analogous-1) have recently been identified to bind HDL and mediate the selective uptake of HDL lipids. Tissue distribution of both murine and human receptors is quite similar, in that they are expressed abundantly in liver and steroidogenic tissues. However, expression and function of the human SR-BI (hSR-BI), in the periphery of reverse cholesterol transport such as macrophages, are still unclear. In the present study, we have raised two different kinds of anti–hSR-BI polypeptide antibodies (Abs): one against the extracellular domain and the other against the intracellular domain. We have investigated the expression of hSR-BI mRNA and immunoreactive mass in freshly isolated cultured human monocyte-derived macrophages (hM
)
and in atherosclerotic lesions. Contrary to the earlier report, hSR-BI
mRNA was expressed in cultured hM and markedly upregulated with
differentiation, determined by Northern blot and reverse
transcriptase–based polymerase chain reaction analyses. The
mRNA expression pattern during differentiation of hM was very
similar to those of SR class A and another member of SR class B, CD36.
Protein expression was confirmed by Western blot analyses with
the above Abs to show a major 83-kDa band. Modified lipoproteins such
as oxidized LDL and acetylated LDL induced a 5-fold increase in
mRNA and protein expression of hSR-BI. Confocal
immunofluorescence microscopy demonstrated that
hSR-BI immunoreactive mass was detectable as a
heterogeneous, punctate staining pattern. Furthermore,
immunohistochemical analysis showed that immunoreactive mass of
hSR-BI was detected in foam cells in human aortic atherosclerotic
lesions and that there was no significant difference of staining
patterns between the two Abs. This study clearly demonstrates that
hSR-BI is expressed in the lipid-laden macrophages in human
atherosclerotic lesions, suggesting that it is very important to know
its function and regulation in hM to understand the biological
utility of this molecule.
Key Words: atherosclerosis • human scavenger receptor class B type I • high-density lipoprotein • reverse cholesterol transport • scavenger receptor
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Introduction |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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High-density lipoprotein (HDL) is postulated to have antiatherogenic functions.1 2 One of the major protective systems against atherosclerosis is called reverse cholesterol transport (RCT),3 in which HDL plays a crucial role as a shuttle carrying cholesterol derived from peripheral tissue to the liver. In the first step of RCT, HDL removes cholesterol from atherosclerotic lesions. The cholesterol incorporated into HDL particles is esterified by the action of lecithin:cholesterol acyltransferase (LCAT).4 The cholesteryl ester in HDL is transferred from HDL to the apolipoprotein (apo) B–containing lipoproteins by plasma cholesteryl ester transfer protein (CETP).5 6 In addition to LCAT and CETP, hepatic triglyceride lipase (HTGL) and lipoprotein lipase (LPL) are thought to take some part in the RCT system by modulating the particle size and composition of HDL.7 Apo B–containing lipoproteins and HDL particles are finally taken up by the liver and steroidogenic tissues, the terminal of RCT.8 9
Recently, scavenger receptor class B type I (SR-BI) and its human
homologue CLA-1 (CD36 and LIMPII
Analogous-I) have been cloned10 11
and identified to bind HDL and mediate selective uptake of HDL
lipids.12 13 Studies with genetic-engineered mice have
demonstrated that SR-BI has an essential role in taking up
cholesterol in liver and steroidogenic
tissues14 and have suggested that levels of SR-BI
expression may determine the plasma HDL cholesterol levels
in rodents.15 16 17 However, expression and function of
SR-BI and its human homologue, especially in the initial step of RCT,
such as macrophages in blood vessels, are still not clear and
rather controversial. Some studies with in situ hybridization technique
showed that murine SR-BI mRNA is expressed in the atherosclerotic
lesions in atherogenic-engineered mice.18 One earlier
report as to human SR-BI (hSR-BI) showed that hSR-BI expression was
much lower in human monocyte-derived macrophages (hM) than
in a human promonocytic leukemia cell line, THP-1 and that the
expression was decreased after stimulation by phorbol
12-myristate 13-acetate (PMA).13
On the other hand, SR-BI belongs to the family of SR class B that includes CD3619 and lysosomal integral membrane protein-II (LIMPII).20 We have reported that CD36 is an important receptor for oxidized LDL by the study of subjects with genetic CD36 deficiency21 22 23 and that CD 36 is expressed in lipid-laden macrophages in human aortic24 and coronary atherosclerosis by morphological studies (Nakagawa Y et al, unpublished data, 1999).
In the present study, we have raised two different kinds of
anti–hSR-BI polypeptide antibodies: one against the extracellular
domain and the other against the intracellular domain. We have
examined the expression of hSR-BI in freshly isolated hM. We clearly
demonstrate that hSR-BI is expressed in both cultured hM and in the
human atherosclerotic lesion.
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Materials and Methods |
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Human Monocyte-Derived Macrophages and Tissue Specimens
Mononuclear cells were isolated from healthy volunteers by density gradient centrifugation by using lymphocyte separation solution (Nacalai Tesque, Kyoto, Japan) and were suspended in RPMI-1640 medium supplemented with 10% human type AB serum and antibiotics. In the indicated experiments, we used 10% FCS in place of 10% human AB serum. Mononuclear cells were plated in 10-cm cell culture dishes (Falcon Labware; Becton-Dickinson) and incubated for 1 hour at 37°C. Nonadherent cells were then removed by washing the dishes twice with PBS (150 mmol/L NaCl and 10 mmol/L phosphate buffer, pH 7.2), and the remaining adherent cells were grown in culture medium. The medium was replaced every 3 days. Cell viability determined by trypan blue exclusion was 95% in all experiments.
Human aortic tissues (mainly descending thoracic aorta) were obtained from 20 autopsy cases with informed consents from the families. Tissues were embedded in Tissue-Tek O.C.T. compound (Sakura Finetechnical Co, Ltd, Tokyo, Japan), frozen in liquid nitrogen, and stored at -80°C until use. Cryostat sections were 6 µm thick and air-dried for 30 minutes.
Isolation and Modification of LDL
LDL (1.019 < density < 1.063 g/mL) was
isolated from the sera of normolipidemic healthy volunteers by
preparative ultracentrifugation. Acetylated LDL
(AcLDL) was made by repeated additions of acetic anhydride. Oxidized
LDL (OxLDL) was prepared by incubating LDL with 5 µmol/L
CuSO4 for 24 hours at 37°C. Modified LDLs used
were extensively dialyzed against PBS and sterilized before use. The
extent of oxidative modification of LDL was evaluated by agarose gel
electrophoresis. We have measured the endotoxin concentration in the
OxLDL preparation by using an ELISA kit and the concentration was <60
pg/mL, which is below the level that has any effect on biological
activity.
Cloning of hSR-BI cDNA From hM and Transient Transfection of
hSR-BI cDNA in Chinese Hamster Ovary (CHO) Cells
Total RNA from hM on the seventh day after plating was used
for reverse transcriptase–based polymerase chain reaction (RT-PCR).
Two micrograms of total RNA was reverse-transcribed by Superscript
Reverse Transcriptase (GibcoBRL), according to the manufacturer's
recommendation. One tenth of the volume of RT reactions was applied for
the PCR with primers P1 and P2 by Advantage cDNA synthesis kit
(Clontech). PCR products with expected length were subcloned into
pGEM 3zf(+). The entire insert was sequenced by an autosequence
analyzer (Perkin-Elmer), according to the manufacturer's
recommendation. The sequence obtained was completely identical to the
sequence of the long form of hSR-BI (GenBank accession No. Z22555). The
full-length cDNA was cloned into a mammalian expression vector, pcDNA
3.1(-) (Invitrogen) and transfected into CHO cells by Lipofectamine
reagent (GibcoBRL).
Antibodies Against hSR-BI
Two different kinds of rabbit polyclonal antipolypeptide
antibodies were raised against amino acid residues 75 to 93 and 490 to
509 of the long form of hSR-BI sequence (GenBank accession No. Z22555)
(Sawady Technology, Tokyo, Japan). Their specificities and titers were
determined by analysis of reactivities to the synthetic
peptides used for immunization. ELISA analysis showed
high-titer immunoreactivity of the antisera to the peptide for
immunization.
Western Blot Analysis
Human monocyte-derived macrophages were lysed and passed
10 times through 25-gauge needles. Human liver and kidney
homogenates were purchased (Clontech). Samples were reduced
with 2-mercaptoethanol in gel loading buffer, fractionated on 5% to
10% Tris-glycine gel (BioRad), and transferred to a 0.45-µmol/L
polyvinylidene difluoride (PVDF) membrane (Millipore). The
membrane was blocked with a solution of 0.1% Tween 20/PBS (PBS-T)
containing 1% BSA overnight and then incubated with rabbit
anti–hSR-BI polyclonal antibodies at 2 µg/mL in PBS-T/BSA for 1 hour
at room temperature followed by washing 3 times for 5 minutes with
PBS-T buffer. The blot was reblocked with PBS-T/BSA for an additional
hour before adding HRP conjugated with goat anti-rabbit immunoglobulin
(Ig)G (1:500 dilution) for another hour at room temperature. After
washing 3 times for 10 minutes with PBS-T, detection was performed by
the protocol of the enhanced chemiluminescence (ECL) plus kit
(Amersham).
RNA Isolation and Northern Blot Analysis
Total cellular RNA from hM was isolated using Trizol reagent
(Gibco BRL). For Northern analysis, 10 µg RNA was separated
on 1.2% agarose formaldehyde gels and was transferred onto positively
charged nylon membranes by the Northern Max kit (Ambion). Biotinylated
hSR-BI and GAPDH cRNA probes were made by in vitro transcription by the
StripEZ kit (Ambion) and labeled by the Psoralen-Biotin kit (Ambion).
Hybridization and visualization were performed, using the BioDetect kit
(Ambion). Data were analyzed by the National Institutes of
Health (NIH, Bethesda, Md) image programs.
Reverse Transcription–Coupled Polymerase Chain Reaction
(RT-PCR)
Conditions for RT-PCR used 2 µg of total RNA and used
downstream priming with primers P3, P4, P5, and P6 in the presence of
50 U Superscript reverse transcriptase (GibcoBRL) at 42°C for 60
minutes. Fragments of 696 bp, 443 bp, and 330 bp from hSR-BI, CD36, and
SR-A, respectively, were amplified from cDNA samples in the same tube.
A 244-bp fragment from human GAPDH was amplified in a separate tube.
Sample sizes and the number of amplification cycles were optimized to
produce measurements within a linear range. After heating the reaction
at 75°C for 5 minutes, one tenth of the volume was used for PCR with
Advantage cDNA Polymerase Mix (Clontech). After denaturation at
95°C for 5 minutes, PCR was conducted: 95°C for 30 seconds,
annealing at 55°C for 30 seconds, and extension at 68°C for 60
seconds. The cycle numbers were 28 for hSR-BI, CD36, and SR-A and 20
for GAPDH. The density was quantitated using NIH image programs.
Immunofluorescent Microscopy of Macrophages
Human monocyte-derived macrophages were washed with PBS,
fixed for 10 minutes with paraformaldehyde on ice, and
permeabilized for 5 minutes with 0.2% Triton X-100.
Cells were blocked with PBS containing 10% FBS and 10% human
immunoglobulins to inhibit the interaction of antibodies with
fragment-crystallizable receptors and to decrease the
nonspecific bindings. Primary antibodies (1:100 dilution) were applied
for 1 hour. After washing twice, rhodamine phalloidin (Molecular
Probes) and FITC-conjugated anti-rabbit IgG were added to visualize
F-actin and hSR-BI, respectively. Images were acquired successively for
each fluorescent probe by confocal laser microscopy as a single
1-µm-thick optical section using a Zeiss LSM 410 confocal microscope
and x60 objective.
Immunohistochemical Analysis
Frozen sections were fixed for 10 minutes with cold acetone and
washed in 0.05 mol/L Tris-HCl buffer (pH 7.6) for 10 minutes.
Endogenous peroxidase activity was quenched by incubating
the section for 10 minutes with 3% hydrogen peroxide. For detection of
hSR-BI, after incubation of the section with 10% normal goat serum for
5 minutes at room temperature, the labeled
streptavidin-biotin-peroxidase method was used, with rabbit
anti–hSR-BI antibodies hSR-BI-75 and hSR-BI-490 diluted into 1:500 and
1:200, respectively, in PBS containing 1% BSA (for 60 minutes at room
temperature). Sections were incubated with biotinylated goat
anti-rabbit immunoglobulins and peroxidase-labeled streptavidin for 10
minutes in turn. A positive reaction on the tissue was visualized with
3, 3'-diaminobenzidine (DAB). These sections were counterstained with
hematoxylin. As a negative control, preimmune rabbit serum diluted into
1:500 and 1:200, respectively, in PBS containing 1% BSA was used.
For identification of macrophages, frozen sections were incubated for 20 minutes at room temperature with 1.5% normal goat serum diluted in PBS containing 1% BSA, followed by an incubation with mouse monoclonal antibodies against human macrophages (HAM56, Biomeda) diluted 1:50 in PBS containing 1% BSA. After washing the section in PBS, the ABC (avidin-biotin complex) method was applied to detect macrophages using biotinylated goat anti-mouse IgM diluted 1:2000 and Vecstatin ABC reagent (Vector Laboratories). A positive reaction was visualized by incubation for 5 to 20 minutes at room temperature in peroxidase substrate solution containing DAB (Zymed Laboratories, Inc). As a negative control, normal mouse IgM (DAKO) was used.
Primers Used in the Present Study
- P1: 5'-ATA AGC TTC TAC AGT TTT
GCT TCC TGC AG-3', hSR-BI cDNA nucleotides 1599 to 1579
(GenBank accession No. Z22555)
P2: 5'-ATG GTA CCA TGG GCT GCT CCG CCA AAG CG-3', hSR-BI cDNA nucleotides 70 to 90 (GenBank accession No. Z22555)
P3: 5'-TGA CCG GGT GGA TGT CCA GGA AC-3', hSR-BI cDNA nucleotides 1201 to 1179 (GenBank accession No. Z22555)
P4: 5'-ATT CCC ATG TCC CTG GAC TGA G-3', SR-A cDNA nucleotides 559 to 538 (GenBank accession No. E05210)
P5: 5'-GGC TGC ATC TGT ACC ATT AAT CAT GT-3', CD36 cDNA nucleotides 880 to 854 (GenBank accession No. L06850)
P6: 5'-GGC AGT GAT GGC ATG GAC TGT G-3', GAPDH cDNA nucleotides 609 to 588 (GenBank accession No. M33197)
P7: 5'-TGA TGA TGG AGA ATA AGC CCA T-3', hSR-BI cDNA nucleotides 506 to 527 (GenBank accession No. Z22555)
P8: 5'-GCA GTT CTC ATC CCT CTC ATT GGA-3', SR-A cDNA nucleotides 230 to 253 (GenBank accession No. E05210)
P9: 5'-TGT AAC CCA GGA CGC TGA GGA C-3', CD36 cDNA nucleotides 438 to 459 (GenBank accession No. L06850)
P10: 5'-CAC CAC CAT GGA GAA GGC TGG-3', GAPDH cDNA nucleotides 366 to 386 (GenBank accession No. M33197)
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Results |
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Characterization of Two Kinds of Anti–hSR-BI Polypeptide Antibodies
To identify the hSR-BI protein expression in hM
, we have raised
two different kinds of anti–hSR-BI polypeptide antibodies: one against
the extracellular domain (AA 75 to 93, GenBank accession No. Z22555) of
hSR-BI polypeptide, designated hSR-BI-75, and the other against the
intracellular domain (AA 490 to 509), designated hSR-BI-490. Figure 1
shows the data of Western blot
analysis with the two antibodies raised, demonstrating that
whole cell lysates from hSR-BI-transfected CHO cells as well as human
liver homogenates showed a major 83-kDa band. Patterns of
immunoreactive mass detected by the Abs were quite similar.
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Expression of hSR-BI mRNA and Protein in Cultured hM
We have investigated the expression of SR-BI of hM in 10%
human AB serum. As shown in Figure 2A and 2B, Northern blot analysis using a 550-nt
(nucleotides 1050 to 1599, hSR-BI cDNA, GenBank accession
No. Z22555) biotinylated hSR-BI cRNA probe showed a major 2.9-kbp mRNA
species. The size of the transcript was consistent with that of
previous reports. However, contrary to the earlier
report,13 expression levels were markedly upregulated to
80-fold during differentiation of monocytes to macrophages.
Figure 2C shows the data of Western blot analysis using
hSR-BI-490 antibody for in vitro differentiated hM. During the
differentiation, immunoreactive mass of hSR-BI was increased after
plating in parallel with the increased expression of hSR-BI mRNA. To
investigate the discrepancy between our findings and the earlier report
by Murao et al,13 we have examined the effect of FCS on
the expression of hSR-BI, because they used 10% FCS in place of 10%
AB serum. RT-PCR showed a differentiation-dependent increase of SR-BI
expression in macrophages cultured, even in medium containing
10% FCS, as shown in Figure 2D.
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In Vitro Differentiation Induces Expression of SRs in Cultured
hM
To compare the expression pattern of hSR-BI with those of other
SRs, such as SR class A and another member of SR class B, CD36, we have
performed RT-PCR analyses. As shown in Figure 3, other SRs, CD36 and SR-A, were also
markedly upregulated during the in vitro differentiation in medium
containing 10% human AB serum. On day 0, a trace amount of hSR-BI
immunoreactive mass was detectable, as shown in Figure 2C
, whereas mRNA expression was hardly seen by Northern blot and RT-PCR
analyses (Figures 2A and 3A). We have done the second
round of RT-PCR with nested primers and successfully amplified the
expected length of cDNA and confirmed the entire sequence (data not
shown).
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Modified Lipoproteins Induce the Expression of hSR-BI In
Vitro
We have investigated whether modified lipoproteins such as OxLDL
and AcLDL induce the expression of hSR-BI. The addition of 50 µg/mL
of protein of each modified LDL for 24 hours made 
5-fold increase in
both mRNA and protein of hSR-BI, as shown in Figure 4A and 4B.
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Immunofluorescence Microscopy of hSR-BI in
Cultured hM
Both of the anti–hSR-BI polypeptide antibodies hSR-BI-75 and
hSR-BI-490 showed the heterogeneous and punctate pattern,
as shown in Figure 5. As shown in Figure 6, the addition of OxLDL (50 µg/mL)
into medium clearly enhanced the signals for hSR-BI along with the
accumulation of lipids stained by Oil Red O.
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Immunohistochemical Analysis of hSR-BI in Human
Atherosclerotic Lesion of Aorta
It has not been clarified whether hSR-BI is expressed in human
aortic tissues. Figure 7 shows the
immunohistochemical staining of aortic specimens, demonstrating the
presence of hSR-BI immunoreactive mass in lipid-laden cells in the
atherosclerotic lesions. No reaction product was detectable with
preimmune serum. A comparison of the staining pattern for
macrophage-specific marker confirmed that hSR-BI was
expressed in lipid-laden macrophages (data not shown).
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Discussion |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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The present study demonstrates for the first time that hSR-BI is expressed and markedly upregulated in differentiated hM
and in
human atherosclerotic lesions of aorta. Our results showing the
expression of hSR-BI in differentiated hM are in sharp contrast to
an earlier study by Murao et al,13 who reported the
differentiation-dependent decrease in hSR-BI expression in hM. We
have tested more than 15 lines of hM from healthy volunteers, all of
which showed a differentiation-dependent increase in hSR-BI mRNA.
Because we have noticed the difference of culture conditions between
our study and the previous one in which 10% FCS was used for
culture,13 the expression of hSR-BI in medium containing
10% FCS was also examined. We have observed the
differentiation-dependent increase of hSR-BI expression even in their
condition, which indicated that the difference of sera in culture could
not explain the discrepancy. We were able to demonstrate that the
immunoreactive mass of hSR-BI was detected in differentiated hM and
in human atherosclerotic lesions by two different antibodies raised. Ji
et al18 reported that SR-BI mRNA was expressed abundantly
in murine atherosclerotic lesions. These observations strongly suggest
that SR-BIs are expressed in atherosclerotic lesions.
Recently, data have been accumulated to show that SR-BI may play an
important role in both cholesterol efflux and influx. This
seems to depend on the concentration gradient of
cholesterol across the cell membrane. The function of SR-BI
in the liver and steroidogenic tissues has been extensively
analyzed by studies with genetic-engineered mice technology and
cellular biology. These studies showed that SR-BI is essential for the
selective uptake of HDL lipids and that the levels of expression in the
liver may determine the plasma HDL cholesterol levels in
rodents. However, the function of SR-BI in the blood vessels was still
obscure. Some studies suggested that expression levels of SR-BI are
correlated to the degree of cholesterol
efflux.18 In contrast, another study showed that stable
cell lines of hSR-BI had the accumulation of intracellular
cholesterol.13 Our preliminary results show
that the immunostaining pattern of the M in the
atherosclerotic lesions and Kupffer cells in human liver is different
from that of hepatic parenchymal cells (Nakagawa Y, Hirano K,
unpublished observation, 1998), suggesting that subcellular
localization of hSR-BI is different between these cell types. Recently,
Fluiter et al25 have reported that the regulation of SR-BI
expression in hepatic parenchymal cells, by estradiol administration
and cholesterol feeding, was opposite to that in Kupffer
cells. The possibility has become focused that overexpression of SR-BI
may be a new strategy for antidyslipidemic and
antiatherosclerotic treatment, and it has recently been reported that
the introduction of SR-BI into the liver reduced
atherosclerosis in heterozygous LDL receptor knockout
mice.26 The present study indicates that it is
essential to clarify the function and regulation of hSR-BI expressed in
phagocytotic cells as well as hepatic parenchymal cells and
steroidogenic cells to understand the biological utility of this
molecule.
We have reported the molecular and biochemical bases of patients with
marked hyperalphalipoproteinemia (HALP), such as a genetic cholesteryl
ester transfer protein (CETP) deficiency,27 28 suggesting
that marked HALP is not always a beneficial state but rather an
impairment of the RCT system.29 30 Recently, we have found
that marked HALP caused by CETP deficiency is not a longevity syndrome,
on the basis of a large population-based study.31 Human
genetic CETP deficiency is characterized by the accumulation of large
HDL particles in plasma,32 which is also observed in
SR-BI knockout mice.14 Considering that genetic defects in
large percentages of patients with HALP are still unknown, it is of
great importance to further analyze the function of this type
of SR in hM and to know how relevant this molecule is in humans.
Received March 3, 1999; accepted May 17, 1999.
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