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Rs1
,
Department of
*
Molecular Genetics and Microbiology,
Veterans Affairs Medical Center, and
Department of Medicine, University of New Mexico, Albuquerque, NM 87131
The pentraxins, serum amyloid P component (SAP) and C-reactive
protein (CRP) are acute-phase serum proteins in mice and humans,
respectively. Although SAP binds to DNA and chromatin and affects
clearance of these autoantigens, no specific receptor for SAP has been
identified. CRP is an opsonin, and we have shown that it binds to
Fc
R. Mice deficient in FcR were used to assess the role of these
receptors in phagocytosis by pentraxins using zymosan as a ligand.
Phagocytosis of zymosan by bone marrow macrophages (BMM) was enhanced
by opsonization with SAP or CRP. BMM from mice deficient in all three
FcR or in -chain ingested unopsonized zymosan, but phagocytosis
of SAP- or CRP-opsonized zymosan was not enhanced. SAP binding to BMM
from -chain-deficient mice was also greatly reduced, indicating
little or no binding of SAP to FcRII. SAP and CRP opsonized zymosan
for phagocytosis by BMM from mice deficient in FcRII or FcRIII.
SAP, but not CRP, opsonized zymosan for uptake by neutrophils that
express only low levels of FcRI. Together these results indicate
that FcRI and FcRIII are receptors for SAP in the mouse.
Opsonization of zymosan by CRP is mediated through FcRI. Pentraxins
are major proteins of the innate immune system and arose earlier in
evolution than Igs. The use of FcR by the pentraxins links innate
and adaptive immunity and may have important consequences for
processing, presentation, and clearance of the self-Ags to which these
proteins bind.
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