Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Alkaline Phosphatase / metabolism
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Animals
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Antigen-Antibody Complex / metabolism*
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Binding Sites, Antibody
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Dose-Response Relationship, Immunologic
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Female
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Horseradish Peroxidase / immunology
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Horseradish Peroxidase / metabolism
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Immunoglobulin A / immunology
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Immunoglobulin A / metabolism*
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Kupffer Cells / metabolism*
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Mice
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Mice, Inbred BALB C
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Myeloma Proteins / metabolism
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Rosette Formation
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Trinitrobenzenes / immunology
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Trinitrobenzenes / metabolism
Substances
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Antigen-Antibody Complex
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Immunoglobulin A
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Myeloma Proteins
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Trinitrobenzenes
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Horseradish Peroxidase
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Alkaline Phosphatase