Iron‐transferrin‐induced increase in protein kinase C activity in CCRF‐CEM cells

Jerry L. Phillips, David H. Boldt, Jamie Harper

Research output: Contribution to journalArticlepeer-review

7 Scopus citations


Iron transferrin has been found to induce a mean 10‐fold increase in the activity of protein kinase C in CCRF‐CEM cells. This increase was not detectable up to 45 min after treatment of cells with iron transferrin, although after 60 min, a maximal increase in enzyme activity was observed. Similarly, iron transferrin at concentrations of 0.1–0.5 μg/ml did not alter protein kinase C activity, while concentrations of iron transferrin of 1–100 μg/ml induced a maximal increase in enzyme activity. Apotransferrin and iron in the form of ferric citrate, as well as complexes of transferin with copper, nickel, zinc, manganese, and cobalt did not increase protein kinase C activity. Additionally, CCRF‐CEM cells pretreated with either actinomycin D or cycloheximide and then incubated with iron transferrin did not exhibit increased enzyme activity. Treatment with iron transferrin was found to have no effect on protein kinase C activity in normal human peripheral blood lymphocytes and in HL60, Daudi, and U937 cells. However, normal lymphocytes stimulated with phytohemagglutinin for 48 hr exhibited a 2‐fold increase in protein kinase C activity following treatment with iron transferrin. These results indicate a specific effect of iron transferrin on protein kinase C activity in CCRF‐CEM cells and in mitogen‐stimulated human lymphocytes that may occur through increased synthesis of the enzyme.

Original languageEnglish (US)
Pages (from-to)349-353
Number of pages5
JournalJournal of Cellular Physiology
Issue number2
StatePublished - Aug 1987

ASJC Scopus subject areas

  • Physiology
  • Clinical Biochemistry
  • Cell Biology


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