In vitro uptake of IgA complexes by Kupffer cells.
Cultured murine Kupffer cells were tested for their ability to bind TNP-sensitized erythrocytes coated with IgA myeloma proteins (MOPC 315 & 460) which have high affinity for TNP ligands, and to ingest TNP-enzyme-IgA soluble immune complexes. In these experimental conditions, 6-18% of Kupffer cells were found to express surface binding sites for IgA, a feature they share with lymphocytes and granulocytes. This functional property, also displayed by circulating monocytes, is thus maintained in liver-residing macrophages, and may contribute to the regulation of immune response to gut-derived antigens.
D000469:Alkaline Phosphatase / Q000378:metabolism; D000818:Animals; D000936:Antigen-Antibody Complex / Q000378:metabolism*; D001666:Binding Sites, Antibody; D004306:Dose-Response Relationship, Immunologic; D005260:Female; D006735:Horseradish Peroxidase / Q000276:immunology / Q000378:metabolism; D007070:Immunoglobulin A / Q000276:immunology / Q000378:metabolism*; D007728:Kupffer Cells / Q000378:metabolism*; D051379:Mice; D008807:Mice, Inbred BALB C; D009194:Myeloma Proteins / Q000378:metabolism; D012397:Rosette Formation; D014301:Trinitrobenzenes / Q000276:immunology / Q000378:metabolism
D000936:Antigen-Antibody Complex; D007070:Immunoglobulin A; D009194:Myeloma Proteins; D014301:Trinitrobenzenes; D006735:Horseradish Peroxidase; D000469:Alkaline Phosphatase