{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,20]],"date-time":"2026-10-20T21:53:49Z","timestamp":1792533229617,"version":"4.5.0"},"reference-count":39,"publisher":"Oxford University Press (OUP)","issue":"11","license":[{"start":{"date-parts":[[2001,6,1]],"date-time":"2001-06-01T00:00:00Z","timestamp":991353600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/pages\/standard-publication-reuse-rights"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2001,6,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>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\u03b3R). We now report that SAP also binds to Fc\u03b3R and opsonizes particles for phagocytosis by human polymorphonuclear leukocytes (PMN). Specific, saturable binding of SAP to Fc\u03b3RI, Fc\u03b3RIIa, and Fc\u03b3RIIIb 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 Fc\u03b3R. 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 Fc\u03b3R. Treatment of PMN with phosphatidylinositol-specific phospholipase C to remove Fc\u03b3RIIIb 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 Fc\u03b3R bearing cells.<\/jats:p>","DOI":"10.4049\/jimmunol.166.11.6735","type":"journal-article","created":{"date-parts":[[2014,4,20]],"date-time":"2014-04-20T22:55:28Z","timestamp":1398034528000},"page":"6735-6741","source":"Crossref","is-referenced-by-count":143,"title":["Serum Amyloid P Component Binds to Fc\u03b3 Receptors and Opsonizes Particles for Phagocytosis"],"prefix":"10.1093","volume":"166","author":[{"given":"Dwaipayan","family":"Bharadwaj","sequence":"first","affiliation":[{"name":"Veterans Affairs Medical Center, University of New Mexico School of Medicine , Albuquerque, NM 87108"},{"name":"Department of Medicine, University of New Mexico School of Medicine , Albuquerque, NM 87108"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carolyn","family":"Mold","sequence":"additional","affiliation":[{"name":"Department of Molecular Genetics and Microbiology, University of New Mexico School of Medicine , Albuquerque, NM 87108"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eric","family":"Markham","sequence":"additional","affiliation":[{"name":"Department of Molecular Genetics and Microbiology, University of New Mexico School of Medicine , Albuquerque, NM 87108"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Terry W","family":"Du Clos","sequence":"additional","affiliation":[{"name":"Veterans Affairs Medical Center, University of New Mexico School of Medicine , Albuquerque, NM 87108"},{"name":"Department of Medicine, University of New Mexico School of Medicine , Albuquerque, NM 87108"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2001,6,1]]},"reference":[{"key":"2026020209180863000_R1","first-page":"47","volume-title":"Curr. 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