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

Márquez, C.; Martínez, C.; Boscá, L.

Journal of Immunology 147(2): 627-632

1991

ISSN/ISBN: 0022-1767
PMID: 2071898
Document Number: 378622
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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