title: Biologic effects of an interleukin-1 receptor antagonist protein on interleukin-1-stimulated cartilage erosion and chondrocyte responsiveness.
abstract: Recombinant human interleukin-1 alpha (IL-1 alpha) and recombinant human IL-1 beta stimulate matrix proteoglycan degradation and inhibit glycosaminoglycan synthesis in bovine nasal cartilage explants. A 17-kd human recombinant IL-1 receptor antagonist protein (IRAP) caused a concentration-dependent (0.2-200 ng/ml) suppression of the effects of IL-1 alpha and IL-1 beta in cartilage organ cultures. IRAP inhibited the binding of radiolabeled IL-1 alpha to rabbit articular chondrocytes. Matrix metalloproteinase (collagenase, gelatinase, and stromelysin) and prostanoid production by IL-1-activated rabbit articular chondrocytes was also suppressed by IRAP. These results could have potential significance in the development of a new antiarthritis therapy based on an IRAP.
authors.affiliation: Department of Hypersensitivity Diseases Research, Upjohn Company, Kalamazoo, Michigan 49001.
authors.forename: R J
authors.initials: RJ
authors.lastname: Smith
authors.forename: J E
authors.initials: JE
authors.lastname: Chin
authors.forename: L M
authors.initials: LM
authors.lastname: Sam
authors.forename: J M
authors.initials: JM
authors.lastname: Justen
mesh_terms: D000818:Animals; D002356:Cartilage / Q000166:cytology*; D015232:Dinoprostone / Q000096:biosynthesis; D007375:Interleukin-1 / Q000378:metabolism / Q000494:pharmacology*; D011817:Rabbits; D011971:Receptors, Immunologic / Q000037:antagonists & inhibitors*; D017472:Receptors, Interleukin-1
chemical_list: D007375:Interleukin-1; D011971:Receptors, Immunologic; D017472:Receptors, Interleukin-1; D015232:Dinoprostone