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

Cultures of lapine articular chondrocytes were exposed to purified, human, recombinant interleukin-1 alpha 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.