Redistribution of protein kinase C during mitogenesis of human B lymphocytes

Graeme R. Guy*, John Gordon, Leonie Walker, Robert H. Michell, Geoffrey Brown

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

53 Citations (Scopus)


G0 human tonsillar B-lymphocytes were stimulated to divide by the polyclonal mitogen Staphylococcus Aureus Cowan strain 1 (SAC) and by the combined use of 12-O-tetradecanoyl phorbol-13-acetate (TPA) and the calcium ionophore ionomycin. The activities of protein kinase C, which requires Ca++ and phospholipid as co-factors, and a proteolytically cleaved form of this enzyme (protein kinase M), which is independent of calcium and phospholipid control, were determined in soluble and particulate fractions obtained from activated B cells. Treatment of G0 B cells with SAC or TPA together with ionomycin caused redistribution of protein kinase C from the soluble to the particulate fraction where the 80,000-Dalton protein kinase C was cleaved to give rise to a 50,000-Dalton form of the kinase which was also found in the cytoplasm. These data suggest that redistribution and proteolytic cleavage of protein kinase C are key signal transduction events in B cell mitogenesis.

Original languageEnglish
Pages (from-to)146-153
Number of pages8
JournalBiochemical and Biophysical Research Communications
Issue number1
Publication statusPublished - 26 Feb 1986

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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