Interleukin-1 mediated signal transduction associated with synovial cell activation.
The early biochemical events that link interleukin-1 (IL-1) receptor occupancy to neutral proteinase production in synovial cells were studied. Addition of human r-IL-1 to human synovial cells in culture stimulated phospholipase A2 (PLA2) activity, inositol triphosphate production and plasminogen activator (PA) activity in a dose dependent manner with similar EC50 values (0.1-0.5 nM). These results, coupled with time courses and other studies, suggest that the IL-1 modulation of PA involves both products of PLA2 and phospholipase C (PLC) activation. On the other hand, the IL-1 induction of collagenase may primarily involve PLC and protein kinase C activation.
Mochan
E
E
Department of Family Medicine, University of Medicine and Dentistry, School of Osteopathic Medicine, Camden, NJ 08103.
Ross
B
B
Sporer
R
R
Uhl
J
J
D001172:Arthritis, Rheumatoid / Q000503:physiopathology; D002478:Cells, Cultured; D010450:Endopeptidases / Q000096:biosynthesis; D004790:Enzyme Induction; D006801:Humans; D007375:Interleukin-1 / Q000502:physiology*; D015398:Signal Transduction; D013583:Synovial Membrane / Q000473:pathology / Q000502:physiology*
D007375:Interleukin-1; D010450:Endopeptidases