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Query: UNIPROT:P04141 (granulocyte-macrophage colony-stimulating factor)
 6,790 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

This report examines the effects of recombinant murine interleukin-10 (rmIL-10) on antigen-induced beta-hexosaminidase, leukotriene (LT)C4 and cytokine release from mouse bone marrow-derived mast cells (BMMC). BMMC sensitized to hapten-monoclonal IgE directed against dinitrophenol-bovine serum albumin (DNP-BSA) and challenged with 10 ng/ml DNP-BSA generated beta-hexosaminidase and LTC4-like material which was followed by tumor necrosis factor-alpha (TNF-alpha) and granulocyte-macrophage colony-stimulating factor (GM-CSF) mRNA expression and protein release. Incubation of BMMC with 1-100 ng/ml rmIL-10 inhibited cytokine generation, without affecting beta-hexosaminidase and LTC4-like material release. TNF-alpha, but not GM-CSF mRNA expression, was also diminished in rmIL-10-treated BMMC, suggesting that down-regulation of cytokine production by rmIL-10 involves different mechanisms. These results identify a novel biological action of IL-10 as an inhibitor of cytokine production by stimulated mast cells.
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PMID:Interleukin-10 inhibits cytokine generation from mast cells. 856 61

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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PMID:Human dendritic cells handling of binding, uptake and degradation of free and IgG-immune complexed dinitrophenylated human serum albumin in vitro. 903 24

We have evaluated the uptake of a soluble protein antigen, denitrophenylated human serum albumin (DNP-HSA), and two different intracellular bacteria; Chlamydia trachomatis serovar L2 and Mycobacterium tuberculosis strain H37Ra, by immature human dendritic cells. These were generated by culturing progenitor cells from blood in the presence of cytokines (granulocyte-macrophage colony-stimulating factor and interleukin-4). Dendritic cells play a crucial part in antigen presentation for the induction of T-cell-dependent immune responses in various tissues. Recently, macropinocytic and phagocytic activity has been shown for immature dendritic cells of mouse, rat and human origin. In the present study, macropinocytosis characterized the uptake of the soluble protein-antigen DNP-HSA, whereas the C. trachomatis were ingested via receptor-mediated endocytosis in coated pits, and opsonized M. tuberculosis via phagocytosis. To follow the intracellular routes of the antigens, their positions were compared with the localization of annexins, a family of Ca(2+)-and phospholipid-binding proteins, involved in membrane fusion, aggregation and transport of different vesicles. To elucidate further the intracellular pathway of the antigens, two other proteins, lysosome-associated membrane protein-1 (LAMP-1) and cathepsin D, were labelled. They are known to colocalize with major histocompatibility complex class II compartments in the immature dendritic cells. We observed a distinct translocation of annexin V to DNP-HSA containing endosomes, and annexin III to vesicles with C. trachomatis. Furthermore, annexin III, IV and V redistributed to phagosomes with M. tuberculosis. Both LAMP-1 and cathepsin D colocalized with DNP-HSA endosomes, and with phagosomes with M. tuberculosis. Thus, immature human dendritic cells have the capacity to phagocytose. Moreover, the handling of these antigens by dendritic cells may represent three distinct intracellular pathways, albeit some properties and compartments are shared.
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PMID:Role of annexins in endocytosis of antigens in immature human dendritic cells. 949 92