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Human dendritic cells handling of binding, uptake and degradation of free and IgG‐immune complexed dinitrophenylated human serum albumin in vitro
Author(s) -
LARSSON M.,
BERGE J.,
JOHANSSON A. G.,
FORSUM U.
Publication year - 1997
Publication title -
immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.297
H-Index - 133
eISSN - 1365-2567
pISSN - 0019-2805
DOI - 10.1046/j.1365-2567.1997.00140.x
Subject(s) - endocytosis , pinocytosis , human serum albumin , immune system , antigen , in vitro , immunoglobulin g , antibody , antigen presentation , receptor , chemistry , immune complex , microbiology and biotechnology , immunology , serum albumin , biology , biochemistry , t cell
The handling of free and IgG‐complexed dinitrophenylated human serum albumin (DNP‐HSA) by human dendritic cells (DC) cultured with granulocyte–macrophage colony‐stimulating factor (GM‐CSF) and interleukin‐4 (IL‐4) was studied. It has been shown that the amount of uncomplexed or IgG‐complexed antigen required by DC to start an immune response is low compared with other antigen‐presenting cells. We therefore examined whether such efficient presentation of immune complexes is due to an enhanced Fc γ RII‐mediated endocytosis or to a specialized and efficient antigen handling, i.e. macropinocytosis. The Fc γ RII expression was found to be heterogeneous on the GM‐CSF‐ and IL‐4‐cultured DC, i.e. it ranges from low to high expression. The handling of antigen and immune complexes revealed, that the level of binding and uptake of IgG–DNP‐HSA complexes by in vitro expanded DC is low compared with free antigen. Uncomplexed DNP‐HSA is probably handled either by endocytosis via receptors being more abundant and/or efficient than the Fc γ RII or via non‐receptor‐mediated endocytosis. The binding and uptake of IgG‐complexed DNP‐HSA was blocked by anti‐Fc γ RII antibody, indicating the specificity of the interaction.