The Journal of Immunology, Vol 147, Issue 2 627-632, Copyright © 1991 by American Association of Immunologists

ARTICLES

Protein kinase C mobilization in B lymphocytes. Differential isoenzyme translocation upon activation

C Marquez, C Martinez and L Bosca
Centro de Biologia Molecular, Universidad Autonoma, Madrid, Spain.

The subcellular distribution of protein kinase C has been analyzed in murine B lymphocytes exposed to LPS, anti-IgM antibodies and phorbol dibutyrate. An accurate determination of the enzyme mobilized from the soluble to the particulate fractions by these activators, has been made possible by the use of B cells in which the major part of the activity was present in the cytosol. Upon stimulation, we have analyzed the isoenzymatic forms translocated to the B cell membrane, showing a differential pattern of isoenzyme mobilization between LPS and anti-IgM antibodies. These data, together with the different Ca2+ requirements for the activation of the translocated protein kinase C isoenzymes, might help to unravel the mechanism responsible for the clonal expansion and differentiation of B lymphocytes, induced by the two ligands.

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