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.
Hulkower
K I
KI
Department of Orthopaedic Surgery, University of Pittsburgh School of Medicine, PA 15261.
Georgscu
H I
HI
Evans
C H
CH
D000818:Animals; D001685:Biological Factors / Q000494:pharmacology*; D002358:Cartilage, Articular / Q000378:metabolism*; D002478:Cells, Cultured; D016207:Cytokines; D015180:Electrophoresis, Gel, Two-Dimensional; D066298:In Vitro Techniques; D007375:Interleukin-1 / Q000494:pharmacology*; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism; D011817:Rabbits; D013583:Synovial Membrane / Q000166:cytology / Q000502:physiology*
D001685:Biological Factors; D016207:Cytokines; D007375:Interleukin-1; D010750:Phosphoproteins; D011494:Protein Kinases