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Regular Articles |






From the Department of Physiology and Cellular
Biophysics,*
Columbia University College of Physicians and
Surgeons, New York, New York; the Department of
Pathology,
Albert Einstein College of
Medicine, Bronx, New York; the Bryan Alzheimer Disease Research
Center,
Udall Parkinson Center of Excellence,
Duke University Medical Center, Durham, North Carolina; and the
Department of Medicine, Infectious Disease
Division, and the Center for Immunology and Inflammatory
Diseases,
Massachusetts General Hospital,
Harvard Medical School, Boston, Massachusetts
A pathological hallmark of Alzheimers disease is the senile
plaque, composed of ß-amyloid fibrils,
microglia, astrocytes, and dystrophic neurites. We
reported previously that class A scavenger receptors mediate adhesion
of microglia and macrophages to ß-amyloid fibrils and oxidized
low-density lipoprotein (oxLDL)-coated surfaces. We also showed that
CD36, a class B scavenger receptor and an oxLDL
receptor, promotes H2O2 secretion by
macrophages adherent to oxLDL-coated surfaces. Whether CD36 is
expressed on microglia, and whether it plays a role in
secretion of H2O2 by microglia interacting with
fibrillar ß-amyloid is not known. Using fluorescence-activated cell
sorting analysis and immunohistochemistry, we found that CD36
is expressed on human fetal microglia, and N9-immortalized
mouse microglia. We also found that CD36 is expressed on microglia and
on vascular endothelial cells in the brains of Alzheimers disease
patients. Bowes human melanoma cells, which normally do not
express CD36, gained the ability to specifically bind to
surfaces coated with fibrillar ß-amyloid when transfected with a cDNA
encoding human CD36, suggesting that CD36 is a receptor for
fibrillar ß-amyloid. Furthermore, two different monoclonal
antibodies to CD36 inhibited H2O2 production by
N9 microglia and human macrophages adherent to fibrillar ß-amyloid by
50%. Our data identify a role for CD36 in fibrillar
ß-amyloid-induced H2O2 production by
microglia, and imply that CD36 can mediate binding to fibrillar
ß-amyloid. We propose that similar to their role in the interaction
of macrophages with oxLDL, class A scavenger receptors and CD36
play complimentary roles in the interactions of microglia with
fibrillar ß-amyloid.
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