Interleukin-1 beta and interleukin-1 alpha stimulate the N-acetyl-beta-glucosaminidase activity of human synovial cells.
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)-1 beta and recombinant human IL-1 alpha stimulate the extracellular activity of the lysosomal hydrolase, N-acetyl-beta-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.
D000118:Acetylglucosaminidase / Q000378:metabolism*; D001172:Arthritis, Rheumatoid / Q000378:metabolism; D005347:Fibroblasts / Q000201:enzymology; D006596:Hexosaminidases / Q000378:metabolism*; D006801:Humans; D007375:Interleukin-1 / Q000502:physiology*; D011994:Recombinant Proteins / Q000502:physiology; D013582:Synovial Fluid / Q000201:enzymology*
D007375:Interleukin-1; D011994:Recombinant Proteins; D006596:Hexosaminidases; D000118:Acetylglucosaminidase