Oxidation-induced persistent activation of protein kinase C in hippocampal homogenates

Elizabeth J. Palumbo, J. David Sweatt, Shu Jen Chen, Eric Klann

Research output: Contribution to journalArticlepeer-review

Abstract

Incubation of purified protein kinase C with H2O2 results in the generation of a persistently activated form of the enzyme which is no longer dependent on Ca2+ or lipid cofactors. This oxidative activation of purified protein kinase C requires added Fe2+ in the incubation medium. Treatment of the soluble fraction of hippocampal homogenates with H2O2 also leads to persistent activation of protein kinase C; however, oxidative activation of protein kinase C under these conditions does not require the addition of Fe2+. The persistently activated form of protein kinase C appears as a novel peak of activity on DE52 anion exchange columns, suggesting a modification of the charge character of the enzyme. Thus, oxidative modification of protein kinase C can result in its persistent activation, and this mechanism may constitute a pathway for physiological activation of the enzyme in the hippocampus.

Original languageEnglish (US)
Pages (from-to)1439-1445
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume187
Issue number3
DOIs
StatePublished - Sep 30 1992

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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