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 language | English (US) |
---|---|
Pages (from-to) | 228-232 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 257 |
Issue number | 2 |
DOIs | |
State | Published - 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