Characterization of proteins from human synovium and mononuclear leucocytes that induce resorption of cartilage proteoglycan in vitro.
Both human synovial tissue in culture and lectin-stimulated mononuclear leucocytes produced a protein that induced proteoglycan resorption in explants of bovine nasal cartilage and human articular cartilage. On gel filtration the protein had Mr 16000-20000 and on isoelectric focusing its pI was 5.2-5.3. The protein corresponded to catabolin, which has previously been identified as a product of cultured porcine synovial tissue and mononuclear leucocytes. The action of partially purified human catabolin was not inhibited by cortisol, although the activity of the leucocyte supernatants from which it had been isolated was inhibited. For this reason it is not possible to be sure that the active factor detected in the bioassay of the crude leucocyte culture supernatants is in fact catabolin.
D000818:Animals; D002356:Cartilage / Q000187:drug effects / Q000378:metabolism*; D002417:Cattle; D002850:Chromatography, Gel; D046508:Culture Techniques; D006025:Glycosaminoglycans / Q000378:metabolism; D006801:Humans; D007375:Interleukin-1; D053583:Interleukin-1beta; D007525:Isoelectric Focusing; D007962:Leukocytes / Q000032:analysis*; D008213:Lymphocyte Activation; D011506:Proteins / Q000494:pharmacology; D011509:Proteoglycans / Q000378:metabolism*; D013583:Synovial Membrane / Q000032:analysis*
D006025:Glycosaminoglycans; D007375:Interleukin-1; D053583:Interleukin-1beta; D011506:Proteins; D011509:Proteoglycans