Publication | Open Access
Translocation of phospholipid/Ca2+-dependent protein kinase in B-lymphocytes activated by phorbol ester or cross-linking of membrane immunoglobulin
85
Citations
29
References
1986
Year
Proteinlipid InteractionImmunologyBlood CellPeripheral-blood B-lymphocytesReceptor OccupationCellular PhysiologyMembrane ImmunoglobulinReceptor Tyrosine KinaseHematologyEndocytic PathwayCell SignalingBiochemistryProtein TransportPharmacologyCell BiologyProtein PhosphorylationPhorbol EsterSignal TransductionPhospholipid/ca2+-dependent Protein KinaseNatural SciencesMalignant Blood DisorderIntracellular TraffickingCellular BiochemistryMedicine
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.
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