Down-Regulation and Release of CD14 On Human Monocytes by IL-4 Depends on the Presence of Serum Or GM-CSF

Ruppert, Jörg; Ostermeier, Dorothea; Peters, J. H.; Schütt, Christine

doi:10.1007/978-1-4615-2930-9_47

Cited by 41 publications

(22 citation statements)

References 9 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In the present work, DC were also obtained from peripheral blood using lower concentrations of IL-4 and GM-CSF than previously reported (50 and 100 U/ml, respectively). These cells expressed high levels of MHC class I and 11, CD80, CD86, CD4, CD40, CD33 and CD54 molecules, and had a great stimulatory activity for T cell proliferation, confirming that low concentrations of IL-4 and GM-CSF can generate cells with a high accessory capacity [28]. Under our experimental conditions, 9-60 YO of the large cells, corresponding to 4-45 % of the total number of cultured cells, were found to express the CDla antigen.…”

Section: Discussionmentioning

confidence: 56%

Expression of a mannose/fucose membrane lectin on human dendritic cells

et al. 1996

View full text Add to dashboard Cite

Expression of a mannoselfucose membrane lectin on human dendritic cellsDendritic cells (DC) are the most efficient antigen presenting cells for T lymphocytes. CDla' CD14-DC with high antigen-presenting capacities can now be obtained easily from adherent peripheral blood monocytes by culture in the presence of granulocyte/macrophage colony-stimulating factor and interleukin-4 (Sallusto et al., J . Exp. Med. 1994. 179: 1109). Human macrophages express a membrane lectin, or sugar-specific receptor, which specifically mediates the binding and endocytosis of mannose-and fucose-terminated glycoproteins and is involved in the phagocytosis of pathogens. Asimilar lectin activity was sought on cultured human DC using flow cytometry and confocal microscopy to detect binding and internalization of fluoresceinated neoglycoproteins [bovine serum albumin (BSA) substituted with sugar residues]. Several neoglycoproteins, especially a-L-fucosyl-, a-D-mannosyl-, N,N'-di-acetyl-P-chitobiosyl-and 0-Dglucosyl-BSA, were endocytosed by cultured human CDla' DC as well as by CDla-CD14-cells which were also obtained in the culture. Fuc-BSA and Man-BSA had the same number of binding sites (1.7 x 10h/cell) on CDla' DC, and bound with an affinity constant close to lo7 Vmol. Inhibition experiments indicated that these two neoglycoproteins bound to the same membrane lectin. CDla' and CDla-cells were both labeled by an antiserum specific for the human macrophage mannose receptor. The membrane lectin specific for mannose and fucose that is evidenced in these experiments on cultured DC may be similar to the macrophage membrane lectin or may share functional and structural properties with it. IntroductionDendritic cells (DC) are particularly efficient in presenting antigens to naive as well as to mature T lymphocytes [ 1-31. They initiate primary T cell responses in vivo and in vitro. They can stimulate an allogeneic mixed lymphocyte reaction with a much lower presenting celYeffector cell ratio than unseparated mononuclear cells, and they can present much lower concentrations of antigens than macrophages or nonspecific B lymphocytes [l]. DC are derived from human myeloid-lineage cells and express high levels of MHC class I and MHC class I1 molecules, CD40, CD80 (B7.1) and CD86 (B7.2) co-stimulatory molecules, several

show abstract

Section: Discussionmentioning

confidence: 56%

Expression of a mannose/fucose membrane lectin on human dendritic cells

et al. 1996

View full text Add to dashboard Cite

show abstract

“…Further studies will be needed to determine the molecular basis of this cellular and substrate selectivity and whether this selectivity is apparent with primary populations of macrophages (35,36) and DC (37). BPI-dependent delivery of purified endotoxin, OM blebs, and intact Gram-negative bacteria is CD14-independent (17,18), compatible with the very low levels of membrane-bound CD14 in immature DC (38) (Fig. 1).…”

Section: Discussionmentioning

confidence: 87%

A Novel Role for the Bactericidal/Permeability Increasing Protein in Interactions of Gram-Negative Bacterial Outer Membrane Blebs with Dendritic Cells

Schultz

Hume

Zhang

et al. 2007

The Journal of Immunology

View full text Add to dashboard Cite

The bactericidal/permeability-increasing protein (BPI) is thought to play an important role in killing and clearance of Gram-negative bacteria and the neutralization of endotoxin. A possible role for BPI in clearance of cell-free endotoxin has also been suggested based on studies with purified endotoxin aggregates and blood monocytes. Because the interaction of BPI with cell-free endotoxin, during infection, occurs mainly in tissue and most likely in the form of shed bacterial outer membrane vesicles (“blebs”), we examined the effect of BPI on interactions of metabolically labeled ([14C]-acetate) blebs purified from Neisseria meningitidis serogroup B with either human monocyte-derived macrophages or monocyte-derived dendritic cells (MDDC). BPI produced a dose-dependent increase (up to 3-fold) in delivery of 14C-labeled blebs to MDDC, but not to monocyte-derived macrophages in the presence or absence of serum. Both, fluorescently labeled blebs and BPI were internalized by MDDC under these conditions. The closely related LPS-binding protein, in contrast to BPI, did not increase association of the blebs with MDDC. BPI-enhanced delivery of the blebs to MDDC did not increase cell activation but permitted CD14-dependent signaling by the blebs as measured by changes in MDDC morphology, surface expression of CD80, CD83, CD86, and MHC class II and secretion of IL-8, RANTES, and IP-10. These findings suggest a novel role of BPI in the interaction of bacterial outer membrane vesicles with dendritic cells that may help link innate immune recognition of endotoxin to Ag delivery and presentation.

show abstract

“…[41][42][43] Monocytes cultured in vitro in serum-containing medium (eg, fetal calf serum or human serum) develop characteristics of immature DCs after 6 or 7 days. 4,43,44 In contrast to such lengthy culture activation, monocytes can also acquire characteristics of DCs more rapidly. 45 Randolph et al 46 have shown, using an endothelial reverse-transmigration model, that monocytes crossing an endothelial monolayer and contacting particulate collagen matrix can acquire characteristics of DCs in as few as 2 days.…”

Section: Discussionmentioning

confidence: 99%

Calcium signaling inhibits interleukin-12 production and activates CD83+ dendritic cells that induce Th2 cell development

Faries

Bedrosian

et al. 2001

Blood

View full text Add to dashboard Cite

Mature dendritic cells (DCs), in addition to providing costimulation, can define the Th1, in contrast to the Th2, nature of a T-cell response through the production of cytokines and chemokines. Because calcium signaling alone causes rapid DC maturation of both normal and transformed myeloid cells, it was evaluated whether calcium-mobilized DCs polarize T cells toward a Th1 or a Th2 phenotype. After human monocytes were cultured for 24 hours in serum-free medium and granulocyte-macrophage colony-stimulating factor to produce immature DCs, additional overnight culture with either calcium ionophore (CI) or interferon ␥ (IFN-␥), tumor necrosis factor-␣ (TNF-␣), and soluble CD40L resulted in phenotypically mature DCs that produced interleukin-8 (IL-8) and displayed marked expression of CD80, CD86, CD40, CD54, CD83, DC-LAMP, and RelB. DCs matured by IFN-␥,

show abstract

Down-Regulation and Release of CD14 On Human Monocytes by IL-4 Depends on the Presence of Serum Or GM-CSF

Cited by 41 publications

References 9 publications

Expression of a mannose/fucose membrane lectin on human dendritic cells

Expression of a mannose/fucose membrane lectin on human dendritic cells

A Novel Role for the Bactericidal/Permeability Increasing Protein in Interactions of Gram-Negative Bacterial Outer Membrane Blebs with Dendritic Cells

Calcium signaling inhibits interleukin-12 production and activates CD83+ dendritic cells that induce Th2 cell development

Contact Info

Product

Resources

About