Dual effect of arachidonic acid on protein kinase C isoenzymes isolated from rabbit thymus cells

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Abstract

Type II and type III isoenzymes of protein kinase C isolated from rabbit thymus cells were activated at relatively low concentrations but were inhibited at higher concentrations of arachidonic acid. Activation by cis-unsaturated fatty acids required Ca2+ the maximal activity was approached at about 10-6 M Ca2+ concentration. The kinetics of activation and inhibition by arachidonic acid depended strongly on the nature of the substrate (synthetic oligopeptide or H1 histone), on the concentration of the protein substrate and on the stage of purification of the isoenzyme preparation investigated. Activation seemed to be favoured at high protein concentrations.

Original languageEnglish
Pages (from-to)223-226
Number of pages4
JournalFEBS letters
Volume276
Issue number1-2
DOIs
Publication statusPublished - Dec 10 1990

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Keywords

  • Activation by cis-unsaturated fatty acid
  • Arachidonic acid
  • Protein kinase C isoenzyme
  • Thymus cell

ASJC Scopus subject areas

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

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