title: C-kinase activity in normal B cells treated with Staphylococcus aureus, Cowan strain I, and phorbol ester: response differences in a patient with prolymphocytic leukaemia.
abstract: Ca+2/phospholipid-dependent kinase (C-kinase) activity is intimately involved with the B-cell response after ligation of its mIg receptor. Here, we extend previous findings with anti-mIg by showing that polyclonal stimulation with Staphylococcus aureus, Cowan strain I (SAC), could also translocate C-kinase from the cytosol of intact, normal human B lymphocytes. This stimulus could not, however, induce redistribution of enzyme in a prolymphocytic leukaemia (PLL) B-cell population. Despite a normal density of mIg receptors on the latter cell type, PPL cells could not be stimulated to proliferate, express interleukin-2 (IL-2) receptors, and differentiate under the influence of SAC, even in the presence of exogenous IL-2. Normal B cells could respond appropriately to the same stimuli. PLL cells had a normal content of C-kinase activity and the enzyme could be translocated under the influence of the specific agonist, 12-0-tetradecanoyl phorbol-13-acetate (TPA). The same agent could induce cellular proliferation and differentiation in PLL cells, showing that its terminal C-kinase dependent pathways were intact. We conclude that the mIg receptor mechanism of this PLL population could not activate C-kinase appropriately.
mesh_terms: D000328:Adult; D000942:Antigens, Bacterial / Q000276:immunology; D001402:B-Lymphocytes / Q000201:enzymology* / Q000276:immunology; D006801:Humans; D007376:Interleukin-2 / Q000276:immunology; D007945:Leukemia, Lymphoid / Q000201:enzymology / Q000276:immunology*; D008213:Lymphocyte Activation; D011493:Protein Kinase C / Q000097:blood*; D013211:Staphylococcus aureus / Q000276:immunology; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology
chemical_list: D000942:Antigens, Bacterial; D007376:Interleukin-2; D011493:Protein Kinase C; D013755:Tetradecanoylphorbol Acetate