Biochemical Journal · 1983 · 60 citations · 16 references
Life SciencesBiochemistryImmunologyImmunophysiologyImmunoregulationProteomicsAnimal Cell CultureCartilage BreakdownCartilage DegenerationCartilage MetabolismSynovial InflammationArticular Cartilage ProteoglycansChondrocyte CatabolismProteoglycan BiologyProteoglycan DegradationProteoglycan LossProteoglycan Metabolism
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.
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S B Mizel, J M Dayer, S. M. Krane et al. · Proceedings of the National Academy of Sciences · 1981 · 614 citations · Full text
J H Korn, Perry V. Halushka, E. Carwile LeRoy · Journal of Clinical Investigation · 1980 · 282 citations · Full text
Jean‐Michel Dayer, J Bréard, Leonard Chess et al. · Journal of Clinical Investigation · 1979 · 281 citations · Full text
Purification to apparent homogeneity of murine interleukin 1.
S B Mizel, Diane Mizel · The Journal of Immunology · 1981 · 257 citations