tretinoin and interleukin-1beta-(163-171)

Monocyte/macrophage polypeptides (monokines) alter the properties of synovial cells. This interaction could explain some of the properties of the inflamed synovium in rheumatic disease. Only recently has it been possible to test the action of purified monokines on the target synovial cells. We report here that recombinant human tumor necrosis factor alpha, tumor necrosis factor beta (lymphotoxin), interleukin-1 alpha, and interleukin-1 beta stimulate the hyaluronic acid (HA) levels of human synovial fibroblast-like cells. The effect of monokines was generally inhibited by indomethacin, suggesting the involvement of an endogenous cyclooxygenase product in the stimulation, and by the glucocorticoid, dexamethasone. In contrast, all-trans-retinoic acid stimulated synovial cell plasminogen activator activity but did not increase the HA levels. These findings could help to explain the raised HA levels found in the joint fluids and in the circulation of patients with rheumatic disease.

Topics: Dexamethasone; Fibroblasts; Humans; Hyaluronic Acid; Interleukin-1; Interleukin-1beta; Peptide Fragments; Plasminogen Activators; Prostaglandin-Endoperoxide Synthases; Recombinant Proteins; Stimulation, Chemical; Synovial Membrane; Tretinoin; Tumor Necrosis Factor-alpha