Stimulation of rheumatoid synovial cell collagenase and prostaglandin production by partially purified lymphocyte-activating factor (interleukin 1).

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Abstract
Human macrophages produce in culture a factor termed mononuclear cell factor (MCF) that increases the production of collagenase and prostaglandins by isolated adherent rheumatoid synovial cells. A factor with similar biological activity is also produced by the murine macrophage cell line P388D1. A sequential purification scheme involving ammonium sulfate fractionation was used, in addition to chromatography on DEAE-cellulose, Sephacryl S-200 and phenyl-Sepharose and discontinuous polyacrylamide gel electrophoresis; the P388D1 cell-derived, synovial cell-stimulating factor was co-purified with the lymphocyte-activating factor [LAF; interleukin 1 (IL 1)]. The specific activity of the partially purified LAF (IL 1) was approximately 15,000-fold higher than that of the LAF (IL 1) in the original P388D1 cell culture supernatant. Co-purification of the P388D1 cell-derived LAF (IL 1) and synovial cell-stimulating factors; the similarity in cell of origin, MW, and phenylglyoxal sensitivity of human MCF and murine LAF (IL 1); and the presence of LAF (IL 1) activity in preparations of partially purified human MCF indicated that LAF (IL 1) may have effects on cell targets nonlymphoid in nature, and that human MCF may be similar to, or identical with human LAF (IL 1). LAF (IL 1) may play a role in macrophage-mediated activation of synovial cells and lymphocytes involved in the inflammatory responses associated with rheumatoid arthritis.