phorbol has been researched along with Lymphoma* in 1 studies
1 other study(ies) available for phorbol and Lymphoma
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Protein kinase C-linked inactivation of the interleukin-1 receptor in a human transformed B-cell line.
The effect of tumor-promoting phorbol ester treatment on the binding of interleukin-1 beta (IL-1 beta) to specific cell surface receptors was investigated. A 1 h exposure of Raji human B lymphoma cells with the protein kinase C-activating phorbol ester, phorbol dibutyrate (PDBu), reduced IL-1 beta binding by up to 90% of control cells. This effect was dose-dependent and was not observed with 4-alpha-phorbol, an inactive tumor promoter. Analysis of 125I-labeled IL-1 beta binding to intact cells revealed that PDBu caused a 91% decrease in high-affinity cell-surface receptor number without an effect on receptor affinity. The phorbol ester response was rapid (30 min), observed both at 4 and 37 degrees C, and was preceded by the rapid translocation (t much less than 6 min) of protein kinase C (PKC) from the cytosol to the cell membrane. The PDBu-induced decrease in IL-1 beta receptor number was inhibited by prior incubation of cells for 30 min with the PKC inhibitor 1-(5-Isoquinoline sulfonyl)-2-methylpiperazine (H7). The decrease in receptor binding was not due to enhanced IL-1 beta receptor internalization or shedding into the extracellular medium, since a similar effect was observed with solubilized IL-1 beta receptor. The most likely explanation for the phorbol ester effect appears to be cell surface inactivation of IL-1 receptors. These data suggest that modulation of PKC activity could play a role in the regulation of the IL-1 beta receptor. Topics: B-Lymphocytes; Caenorhabditis elegans Proteins; Carrier Proteins; Cell Line; Cell Membrane; Enzyme Activation; Humans; Interleukin-1; Kinetics; Lymphoma; Phorbol 12,13-Dibutyrate; Phorbols; Protein Kinase C; Receptors, Drug; Receptors, Immunologic; Receptors, Interleukin-1; Recombinant Proteins; Tetradecanoylphorbol Acetate; Tumor Cells, Cultured | 1990 |