Summary
The properties of synovial cells are altered in vitro by monocyte-macrophage polypeptides (monokines), and these changes could explain some of the properties of the inflamed synovium in rheumatoid disease. Purified monokines have become available only recently for testing on the target synovial cells. We report here that purified human interleukin (IL)-1β and recombinant human Il-1α stimulate the extracellular activity of the lysosomal hydrolase, N-acetyl-β-glucosaminidase (NAG), of human synovial fibroblast-like cells. In contrast, another monokine, synovial activator, does not increase the NAG activity. Thus NAG is another cellular activity which can be modulated by interleukin-1.
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References
Hamilton JA, Slywka J (1981) Stimulation of human synovial fibroblast plasminogen activator production by mononuclear cell supernatants. J Immunol 126:851–855
Dayer J-M, Russell RGG, Krane SM (1977) Collagenase production by rheumatoid synovial cells. Stimulation by a human lymphocyte factor. Science 195:181–183
Dayer J-M, Robinson DR, Krane SM (1977) Prostaglandin production by rheumatoid synovial cells. Stimulation by a factor from human mononuclear cells. J Exp Med 145:1399–1404
Hamilton JA, Clarris BJ, Fraser JRE, Niall MC (1985) Peripheral blood mononuclear cells stimulate prostacyclin levels of human synovial fibroblast-like cells. Rheumatol Int 5:121–125
Auron PE, Webb AC, Rosenwasser LJ, Mucci SF, Rich A, Wolff SM, Dinarello CA (1984) Nucleotide sequence of human monocyte interleukin-1 precursor cDNA. Proc Natl Acad Sci USA 81:7909–7911
March CJ, Mosley D, Larsen A, Cerretti DP, Braedt G, Price V, Gillis S, Henney CS, Kronheim SR, Grabstein K, Conlon PJ, Hopp TP, Cosman D (1985) Cloning sequence and expression of two distinct human interleukin-1 complementary DNAs. Nature 315:641–647
Fontana A, Hengartner H, Weber E, Fehr K, Grob PJ, Cohen G (1982) Interleukin-1 activity in the synovial fluid of patients with rheumatoid arthritis. Rheumatol Int 2:49–53
Saklatvala J, Sarsfield SJ, Townsend Y (1985) Pig interleukin-1. Purification of two immunologically different leukocyte proteins that cause cartilage resorption, lymphocyte activation and fever. J Exp Med 162:1208–1222
Muirden KD (1972) Lysosomal enzymes in synovial membrane in rheumatoid arthritis. Ann Rheum Dis 31:265–271
Wegelius O, Klockars M, Vainio U (1968) Acid phosphatase activity in rheumatoid synovium. Acta Med Scand 183:549–551
Vaes G (1980) Collagenase, lysosomes and osteoclastic bone resorption. In: Wooley DE, Evanson JM (eds) Collagenase in normal and pathological connective tissues. Wiley, Chichester, pp 185–207
Eeckhout Y, Vaes G (1977) Further studies on the activation of procollagenease, the latent precursor of bone collagenase. Effects of lysosomal cathepsin B, plasmin and kallikrein, and spontaneous activation. Biochem J 166:21–31
Fraser JRE, Catt KJ (1961) Human synovial cell culture. Use of a new method in a study of rheumatoid arthritis. Lancet II:1437–1439
Clarris BJ, Hamilton JA (1985) Peripheral blood mononuclear cells stimulate N-acetyl-β-glucosaminidase levels of human synovial fibroblast-like cells. Rheumatol Int 5:55–60
Clarris BJ, Fraser JRE (1968) Relationship between chromosomal changes and alterations in the behaviour of a strain of human synovial cells during its life history in vitro. Ann Rheum Dis 27:597–603
Hamilton JA, Leizer T, Lingelbach SR (1986) The stimulation of human synovial fibroblast plasminogen activator activity: involvement of cyclic AMP and cyclooxygenase products. Biochim Biophys Acta 886:195–202
Hamilton JA, Zabriskie JB, Lachman LB, Chen Y-S (1982) Streptococcal cell walls and synovial cell activation. J Exp Med 155:1702–1718
Leizer T, Hart PH, Hamilton JA (submitted) Properties of the human monokine, synovial activator. I. Biochemical and immunological comparison to interleukin-1. J Immunol
Lachman LB, Page SO, Metzgar RS (1980) Purification of human interleukin-1. J Supramol Struct 13:457–462
LeMarshall J, Fraser JRE, Muirden KD (1977) Lysosomal activation by neutral saccharides in cell cultures of synovium. Ann Rheum Dis 36:130–138
Deutsch DG, Mertz J (1970) Plasminogen: purification from human plasma by affinity chromatography. Science 170:1095–1096
Morrison DC, Jacobs DM (1976) Binding of polymyxin B to the lipid A portion of bacterial lipopolysaccharides. Immunochemistry 13:813–818
Dayer J-M, de Rochemonteix B, Burrus B, Demczuk S, Dinarello C (1986) Human recombinant interleukin-1 stimulates collagenase and prostaglandin E2 production by human synovial cells. J Clin Invest 77:645–648
Leizer T, Clarris BJ, Ash PE, Van Damme J, Saklatvala J, Hamilton JA (1987) Interleukin-1β and interleukin-1α stimulate the plasminogen activator activity and prostaglandin E2 levels of human synovial cells. Arthritis Rheum 30:562–566
Clarris BJ, Malcolm LP (1983) Effects of prostaglandin E1, E2 and F2α on N-acetyl-β-glucosaminidase activities of human synovial cells in culture. Ann Rheum Dis 42:187–191
Oppenheim JJ, Kovacs EJ, Matsushima K, Durum SK (1986) There is more than one interleukin-1. Immunol Today 7:45–56
Chin J, Cameron PM, Rupp E, Schmidt JA (1987) Identification of a high-affinity receptor for native human interleukin-1β and interleukin-1α on normal lung fibroblasts. J Exp Med 165:70–86
Butler DM, Vitti GF, Leizer T, Hamilton JA (submitted) Interleukin-1β and interleukin-1α stimulate the hyaluronic acid (hyaluronan) levels of human synovial cells. J Immunol
Ziff M (1974) Relation of cellular infiltration of rheumatoid synovial membrane to its immune response. Arthritis Rheum 17:313–319
Dingle JT (1975) The secretion of enzymes into the pericellular environment. Philos Trans R Soc Lond [Biol] 271:315–324
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Clarris, B.J., Fraser, J.R.E., Ash, P. et al. Interleukin-1β and interleukin-1α stimulate the N-acetyl-β-glucosaminidase activity of human synovial cells. Rheumatol Int 7, 271–275 (1987). https://doi.org/10.1007/BF00270528
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DOI: https://doi.org/10.1007/BF00270528