| http://purl.uniprot.org/citations/18250462 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18250462 | http://www.w3.org/2000/01/rdf-schema#comment | "Prompt phagocytosis of apoptotic cells prevents inflammatory and autoimmune responses to dying cells. We have previously shown that the blood anticoagulant factor protein S stimulates phagocytosis of apoptotic human B lymphoma cells by human monocyte-derived macrophages. In this study, we show that protein S must first undergo oxidative activation to stimulate phagocytosis. Binding of human protein S to apoptotic cells or to phosphatidylserine multilamellar vesicles promotes auto-oxidation of Cys residues in protein S, resulting in covalent, disulfide-linked dimers and oligomers that preferentially bind to and activate the human Mer tyrosine kinase (MerTK) receptor on the macrophages. The prophagocytic activity of protein S is eliminated when disulfide-mediated oligomerization is prevented, or when MerTK is blocked with neutralizing Abs. Protein S oligomerization is independent of phospholipid oxidation. The data suggest that membranes containing phosphatidylserine serve as a scaffold for protein S-protein S interactions and that the resulting auto-oxidation and oligomerization is required for the prophagocytic activity of protein S. In this way, apoptotic cells facilitate their own uptake by macrophages. The requirement for oxidative modification of protein S can explain why this abundant blood protein does not constitutively activate MerTK in circulating monocytes and tissue macrophages."xsd:string |
| http://purl.uniprot.org/citations/18250462 | http://purl.org/dc/terms/identifier | "doi:10.4049/jimmunol.180.4.2522"xsd:string |
| http://purl.uniprot.org/citations/18250462 | http://purl.uniprot.org/core/author | "Uehara H."xsd:string |
| http://purl.uniprot.org/citations/18250462 | http://purl.uniprot.org/core/author | "Shacter E."xsd:string |
| http://purl.uniprot.org/citations/18250462 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18250462 | http://purl.uniprot.org/core/name | "J Immunol"xsd:string |
| http://purl.uniprot.org/citations/18250462 | http://purl.uniprot.org/core/pages | "2522-2530"xsd:string |
| http://purl.uniprot.org/citations/18250462 | http://purl.uniprot.org/core/title | "Auto-oxidation and oligomerization of protein S on the apoptotic cell surface is required for Mer tyrosine kinase-mediated phagocytosis of apoptotic cells."xsd:string |
| http://purl.uniprot.org/citations/18250462 | http://purl.uniprot.org/core/volume | "180"xsd:string |
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