Release of interleukin-1 from human synovial tissue in vitro.
During the enzymatic disaggregation of human synovium, used in the process of isolating synoviocytes, a factor was liberated into the culture medium that exhibited the thymocyte mitogenic properties of interleukin-1. Like interleukin-1, this synovial-derived mitogen could be isolated using an affinity column of antihuman leukocytic pyrogen. By gel filtration and isoelectric focusing, the mitogen cofractionated with human monocyte-derived interleukin-1. Finally, the isolated mitogen was shown to exhibit other properties of interleukin-1: stimulation of the secretion of interleukin-2, enhancement of the titer of acute-phase proteins in vivo, and stimulation of the release of prostaglandin E2 from human synoviocyte cultures. These observations suggest that interleukin-1 can be derived from the human synovium.
D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D006801:Humans; D066298:In Vitro Techniques; D007375:Interleukin-1 / Q000032:analysis*; D007376:Interleukin-2 / Q000096:biosynthesis; D007525:Isoelectric Focusing; D008934:Mitogens / Q000378:metabolism; D000685:Serum Amyloid A Protein / Q000096:biosynthesis; D013583:Synovial Membrane / Q000032:analysis* / Q000166:cytology / Q000378:metabolism; D013950:Thymus Gland / Q000166:cytology / Q000378:metabolism; D014020:Tissue Extracts / Q000502:physiology
D007375:Interleukin-1; D007376:Interleukin-2; D008934:Mitogens; D000685:Serum Amyloid A Protein; D014020:Tissue Extracts