Inhibition of human natural killer cell activity by polyclonal IgM

Manciulea, Mioara; Pricop, Luminita; Sulica, Andrei; Rb, Herberman

doi:10.1016/0161-5890(89)90052-7

Cited by 8 publications

(7 citation statements)

References 28 publications

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“…Our previously reported findings revealed that the majority of fresh NK cells and almost all A-NK cells interacted with 1gM, as detected by flow cytometry (30). The results have indicated substantial variability among different myeloma 1gM proteins, as was also the case with IgG myelomas, with regard to their capacity to bind to NK cells (28). The Fcl.LR on NK cells appears to function as a signaltransducing molecule, causing a rapid increase in [Ca2+]i and down-modulation of interferon y (IFN-y) gene expression, but IFN-y release as well as a dose-dependent inhibition of the cytolytic function of these effector cells (30).…”

Section: Proteinmentioning

confidence: 78%

“…Mouse splenic lymphocytes or macrophages coated with cytophilic IgG antibody were found to bind to erythrocytes coated with protein A (termed ES), indicating that a relevant binding site of the Fe region was available for protein A after interaction with FcyR (15). In functional studies, it was also concluded that protein A on the surface of staphylococci promotes an opsonin-independent mechanism of phagocytosis and transduces intracellular signals in human macrophages coated with cytophilic IgC (26 Among the various classes of human immunoglobulins, clear-cut evidence has been obtained for Fe region-mediated interaction with NK cells by polyclonal IgG and 1gM (27,28). In these studies, highly purified molecules from human plasma were used either as monomeric (cytophilic) molecules with direct binding to cell-surface receptors measured by various indirect or direct assays, including the arming process, or as multimeric (opsonic) adherence antibodies previously or simultaneously fixed to the target cell surface by combination with antigen.…”

Section: Proteinmentioning

confidence: 99%

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Cytophilic immunoglobulins revisited via natural killer cells

Sulica¹,

Herberman

1996

FASEB j.

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Cytophilia is one of the biologic properties of the Fc region of immunoglobulins operationally defined as the ability of an antibody molecule to attach to certain cell types before combination with antigen. By attachment of cytophilic antibody to membrane Fc receptors, cells become "armed" with antibodies and able to interact specifically with soluble or particulate antigens. In contrast to this cytophilia, the so-called opsonic antibody binds to FcR of various cell types only after it has complexed with antigen. In spite of knowledge of cytophilic properties of immunoglobulins for more than 30 years and an impressive accumulation of facts regarding the structure and function of cell-surface FcR binding IgG, IgE, or IgA molecules, less progress has been made in understanding the molecular basis of cytophilia. Our extensive studies of the structural and functional aspects of the interaction of IgG in monomeric form with human natural killer cells, via the type IIIA IgG Fc receptor (Fc gamma RIIIA), provide a focal point for revisiting this major pathway of direct and continuous communication between the humoral and cellular compartments of the immune system.

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Section: Proteinmentioning

confidence: 78%

Section: Proteinmentioning

confidence: 99%

Cytophilic immunoglobulins revisited via natural killer cells

Sulica¹,

Herberman

1996

FASEB j.

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“…A still more pronounced dose-dependent decrease in the NK activity of lymphocytes associated with the blockade of their Fc~tR was recorded under the influence of polyclonal IgM [15]. Monoclonal IgM proved to elicit a lower effect, while Fc~t fragments were more active than Fab fragments [15], which, on the contrary, can nonspecifically stimulate the immune response [12]. In a dose of 0.5 mg/ml, which is only one order of magnitude different from the plasma IgG content and is comparable to the IgM content, native IgG and IgM have no effect on NK activity [11].…”

Section: Methodsmentioning

confidence: 93%

Blast transformation of lymphocytes and the activity of natural killer cells in the presence of γ-globulinin vitro

et al. 1994

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1317components increase the sensitivity of platelets to ADP by actively interacting with the cell membrane. This assumption does not contradict the findings of other researchers who demonstrated a stimulatory effect of peptoglycans of nontoxigenic DCB on cultured immune cells in vitro.Thus, this study has shown that diphtheria toxin, diphtheria anatoxin, and codivac are agents that directly affect the functional activity of human platelets. In addition, it was found that diphtheria toxin and anatoxin reduce ADP-induced and total platelet aggregation, the decrease being dependent on preparation dose and incubation time. However, codivac, a glycopeptide from the cell wall of nontoxigenic DCB, stimulates platelet a~gregation in all experimental series.The cytotoxic activity of natural killer cells against 3H-uridine-labeled target cells (human erythromyeloleukosis cells K-562) and the intensity of spontaneous blast transformation are studied in vitro in the presence of human serum T-globulin. It is shown that spontaneous blast transformation is 49-51% due to the presence of aggregated ?-globulin, while the aggregate-free y-globulin fraction does not induce this reaction. The cytotoxic activity of natural killer cells in vitro declines in the presence of native ~,-globulin, which is related to the influence of aggregated y-globulin, the intensity of whose formation may increase upon a manyfold decrease in the y-globulin content of the preparation.

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“…NK cells expressed Fc + RIIIa, Fc + RIIc and Fc ? R, and these cell surface structures exert an important regulatory role on the NK cell activity [11,[33][34][35].…”

Section: Discussionmentioning

confidence: 99%

“…After incubation, the cells were washed extensively. The 51 Cr-release assay was performed with K562 cells as described [33]. Briefly, 51 Crlabeled target cells (3×10 3 ) were incubated for 4 h at 37°C with effector cells in 96-well round-bottom microtiter plates (Limbro, Flow Laboratories, McLean, VA).…”

Section: Cell Killingmentioning

confidence: 99%