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Receptors and Opsonizes Particles for Phagocytosis1
*
Veterans Affairs Medical Center; and Departments of
Medicine and
Molecular Genetics and Microbiology, University of New Mexico School of Medicine, Albuquerque, NM 87108
Serum amyloid P component (SAP) is a member of the pentraxin family
of proteins. These proteins are characterized by cyclic pentameric
structure, calcium-dependent ligand binding, and frequent regulation as
acute-phase serum proteins. SAP is the serum precursor of the P
component of amyloid. It binds to a broad group of molecules, including
autoantigens, through a pattern recognition binding site. The related
pentraxin, C-reactive protein (CRP), is a strong acute-phase reactant
in man and an opsonin. We previously determined that the binding of CRP
to leukocytes occurs through Fc receptors for IgG (Fc
R). We now
report that SAP also binds to FcR and opsonizes particles for
phagocytosis by human polymorphonuclear leukocytes (PMN). Specific,
saturable binding of SAP to FcRI, FcRIIa, and FcRIIIb
expressed on transfected COS cells was detected using SAP-biotin and
PE-streptavidin. Zymosan was used to test the functional consequences
of SAP and CRP binding to FcR. Both SAP and CRP bound to zymosan and
enhanced its uptake by PMN. This enhanced phagocytosis was abrogated by
treatment of PMN with wortmannin, a phosphatidylinositol-3 kinase
inhibitor, or with piceatannol, a Syk inhibitor, consistent with uptake
through FcR. Treatment of PMN with phosphatidylinositol-specific
phospholipase C to remove FcRIIIb also decreased phagocytosis of
SAP-opsonized zymosan, but not CRP-opsonized zymosan. These results
suggest that SAP may function in host defense. In addition, as SAP
binds to chromatin, a major immunogen in systemic lupus erythematosus,
it may provide a clearance mechanism for this Ag through FcR bearing
cells.
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