Altered patterns of protein phosphorylation in articular chondrocytes treated with interleukin-1 or synovial cytokines

K. I. Hulkower, H. I. Georgescu, C. H. Evans

Research output: Contribution to journalArticle

5 Scopus citations

Abstract

Cultures of lapine articular chondrocytes were exposed to purified, human, recombinant interleukin-1 α or partially purified preparations of lapine, synovial, cytokines in the presence of [32P]orthophosphate. After 30 min incubation, phosphoproteins were extracted from the cells, separated by two-dimensional gel electrophoresis and visualized autoradiographically. Analysis of the autoradiograms revealed that interleukin-1 and the synovial factors produced marked changes in the pattern of protein phosphorylation. The synovial cytokines induced many of the same changes as interleukin-1, as well as a number of unique changes. This finding is consistent with the notion that, in addition to interleukin-1, synoviocytes secrete other cytokines which modulate the metabolism of chondrocytes. These data support the idea that signal transduction in chondrocytes responding to interleukin-1 involves the activation of one or more protein kinases.

Original languageEnglish (US)
Pages (from-to)228-232
Number of pages5
JournalFEBS Letters
Volume257
Issue number2
DOIs
StatePublished - Nov 6 1989

Keywords

  • Chondrocyte-activating factor
  • Interleukin-1
  • Protein kinase
  • Protein phosphorylation
  • Signal transduction
  • Synovial cytokine

ASJC Scopus subject areas

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

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