Proteolytic activation of protein kinase C in the extracts of cells treated for a short time with phorbol ester

László Buday, János Seprödi, Gyöngyi Farkas, György Mészáros, Tibor Romhányi, Gábor Bánhegyi, József Mandl, Ferenc Antoni, Anna Faragó

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21 Citations (Scopus)


A 10 min treatment of human neutrophils with phorbol 12-myristate 13-acetate (PMA) has been reported to induce accumulation of the proteolytically activated Ca2 +/phospholipid-independent catalytic fragment of protein kinase C in the cytosol of intact cells [(1986) J. Biol. Chem. 261, 4101-4105]. We investigated the proteolytic conversion of protein kinase C to the Ca2 +/phospholipid-independent form in the cytosol and membrane fractions of pig neutrophils. The activity of protein kinase C was measured with its specific oligopeptide substrate Ala-Ala-Ala-Ser-Phe-Lys-Ala-Lys-Lys-amide designed previously. In our experiments the short-term treatment of neutrophils with PMA did not induce the accumulation of the proteolytically activated form of protein kinase C in the cytosol of intact cells. However, treatment of cells with PMA enhanced the limited proteolysis of protein kinase C during the preparation of cell extracts.

Original languageEnglish
Pages (from-to)15-19
Number of pages5
JournalFEBS letters
Issue number1
Publication statusPublished - Oct 19 1987



  • (Neutrophil, Lymphocyte, Hepatocyte)
  • Phorbol ester
  • Protein kinase C
  • Proteolytic activation
  • Synthetic peptide substrate

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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