In vitro uptake of IgA complexes by Kupffer cells

Liver. 1983 Apr;3(2):71-8. doi: 10.1111/j.1600-0676.1983.tb00853.x.

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

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alkaline Phosphatase / metabolism
  • Animals
  • Antigen-Antibody Complex / metabolism*
  • Binding Sites, Antibody
  • Dose-Response Relationship, Immunologic
  • Female
  • Horseradish Peroxidase / immunology
  • Horseradish Peroxidase / metabolism
  • Immunoglobulin A / immunology
  • Immunoglobulin A / metabolism*
  • Kupffer Cells / metabolism*
  • Mice
  • Mice, Inbred BALB C
  • Myeloma Proteins / metabolism
  • Rosette Formation
  • Trinitrobenzenes / immunology
  • Trinitrobenzenes / metabolism

Substances

  • Antigen-Antibody Complex
  • Immunoglobulin A
  • Myeloma Proteins
  • Trinitrobenzenes
  • Horseradish Peroxidase
  • Alkaline Phosphatase