Isolation and purification of ILS, an interleukin 1 inhibitor produced by human gingival epithelial cells.
Recent studies have described the presence of an interleukin 1 (IL-1) inhibitor (ILS) in supernatants from human gingival organ cultures. This report describes the isolation and purification of ILS. ILS was produced in serum-free medium and purified to apparent homogeneity by ion exchange chromatography and high pressure liquid chromatography. IL-1 and ILS eluted as discrete proteins using this system, with ILS appearing as a single protein band of 97,400 molecular weight on SDS-PAGE. ILS inhibited the effects of both murine IL-1 and IL-2 on thymocyte proliferation, and was heat resistant, moderately resistant to freeze-thawing and stable for 2 years at 0-4 degrees C or -20 degrees C. Production of ILS by gingival epithelial cell cultures was not affected by depletion of Langerhans cells, implying that ILS is primarily a keratinocyte product.
D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D004848:Epithelium / Q000276:immunology; D005881:Gingiva / Q000276:immunology*; D006801:Humans; D007700:Kinetics; D008213:Lymphocyte Activation; D008222:Lymphokines / Q000096:biosynthesis / Q000302:isolation & purification*; D009924:Organ Culture Techniques; D013601:T-Lymphocytes / Q000276:immunology
D008222:Lymphokines