cytochalasin-b has been researched along with Multiple-Myeloma* in 2 studies
2 other study(ies) available for cytochalasin-b and Multiple-Myeloma
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IgA immune aggregates stimulate platelet-activating factor and superoxide anion production by human neutrophils. A comparison with IgG aggregates.
We have examined the possibility that human polymorphonuclear cells exposed to IgA immune complexes can mediate the production of platelet-activating factor (PAF) and oxygen radicals. We found that human IgA and IgG immune aggregates stimulated, to a similar extent, PAF and O2- production by human polymorphonuclear cells (PMN) in a concentration and time dependent manner. The PAF, that was largely associated with cells, was shown to be identical to synthetic PAF, as determined by physicochemical, chromatographic and enzymatic assay. Furthermore, de novo synthesis of PAF by PMN was shown to occur by incorporation of radioactive precursors, such as [3H]acetate. The addition of normal human serum to PMN incubated with IgG aggregates resulted in a significant amount of PAF formation which was not observed with IgA aggregates. By contrast, no change was seen in PMN O2- with either aggregates. The preincubation of PMN with cytochalasin B, an inhibitor of phagocytosis, did not affect PAF and O2- production by both aggregates. The results suggest that the interaction of PMN with the IgA complexes in blood vessel walls of different tissues can result in the release of lipid mediators, such as PAF and oxygen radicals that could contribute to the inflammatory response. Topics: Cytochalasin B; Humans; Immunoglobulin A; Immunoglobulin Fab Fragments; Immunoglobulin G; In Vitro Techniques; Macromolecular Substances; Multiple Myeloma; Neutrophils; Platelet Activating Factor; Reference Values; Superoxides; Tetradecanoylphorbol Acetate | 1991 |
Adhesion of lymphoid cell lines to fibronectin-coated substratum: biochemical and physiological characterization and the identification of a 140-kDa fibronectin receptor.
Little information is available on the interaction between lymphocytes and fibronectin (fn). To gain a better understanding on this issue we examined the adhesion of 12 lymphoid cell lines, each exhibiting different phenotypic characteristics, to fn-coated substratum. Of the cell lines tested, five that adhered to fn possessed B-cell characteristics, while neither the T-cell lines nor the pre-B-cell line adhered. The physiology and biochemistry of adhesion of a B-cell line, MOPC 315, were examined in detail. Our results indicated that (1) the adhesion was a specific and time-dependent process, (2) the adhesion was temperature-dependent and inhibited by metabolic inhibitors, such as KCN and 2-deoxyglucose, (3) the presence of cycloheximide and pretreatment of cells with trypsin inhibited adhesion, (4) a 140-kDa surface protein was immunoprecipitated by anti-fn receptor antibodies, (5) the presence of divalent cations was essential for adhesion, (6) the presence of colchicine had no effect on adhesion, while cytochalasin B partially inhibited adhesion, and (7) the treatment of cells by both phorbol 12-myristate 13-acetate and calcium ionophore A23187 enhanced adhesion. In this study, we have established the interaction between lymphoid cell lines and fn. Such an interaction might play an important role in the behavior of lymphocytes in tissues. Topics: Animals; Calcimycin; Cations, Divalent; Cell Adhesion; Cell Differentiation; Cell Line; Cycloheximide; Cytochalasin B; Fibronectins; Humans; Lymphocytes; Lymphoma; Multiple Myeloma; Receptors, Fibronectin; Receptors, Immunologic; Tetradecanoylphorbol Acetate; Trypsin | 1987 |