Translocation of phospholipid/Ca2+-dependent protein kinase in B-lymphocytes activated by phorbol ester or cross-linking of membrane immunoglobulin.
Stimulation of peripheral-blood B-lymphocytes with phorbol ester or anti-immunoglobulin demonstrated intracellular translocation of phospholipid/Ca2+-dependent protein kinase (C-kinase) activity from cytosol to membrane fractions. This phenomenon, which was dose- and time-dependent, was found in both normal and chronic-lymphocytic-leukemia B-cells. This suggests that C-kinase-dependent protein phosphorylation may be related to membrane receptor occupation and may therefore be important in B-lymphocyte responses.
D000888:Antibodies, Anti-Idiotypic / Q000378:metabolism; D001402:B-Lymphocytes / Q000201:enzymology*; D001692:Biological Transport; D002118:Calcium / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism; D003600:Cytosol / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008213:Lymphocyte Activation / Q000187:drug effects; D010704:Phorbols / Q000494:pharmacology*; D010743:Phospholipids / Q000378:metabolism; D010766:Phosphorylation; D011493:Protein Kinase C / Q000097:blood*; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology*
D000888:Antibodies, Anti-Idiotypic; D010704:Phorbols; D010743:Phospholipids; D011493:Protein Kinase C; D013755:Tetradecanoylphorbol Acetate; D002118:Calcium