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. 1997 Jan;90(1):138–146. doi: 10.1046/j.1365-2567.1997.00140.x

Human dendritic cells handling of binding, uptake and degradation of free and IgG-immune complexed dinitrophenylated human serum albumin in vitro.

M Larsson 1, J Berge 1, A G Johansson 1, U Forsum 1
PMCID: PMC1456721  PMID: 9038724

Abstract

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 gamma RII-mediated endocytosis or to a specialized and efficient antigen handling, i.e., macropinocytosis. The Fc gamma 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 gamma RII or via non-receptor-mediated endocytosis. The binding and uptake of IgG-complexed DNP-HSA was blocked by anti-Fc gamma RII antibody, indicating the specificity of the interaction.

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