FEBS Letters | |
Nitric oxide and proteoglycan biosynthesis by human articular chondrocytes in alginate culture | |
Stefanovic-Racic, M.1  Häuselmann, H.J.2  Evans, C.H.1  Michel, B.A.2  Oppliger, L.3  | |
[1] Ferguson Laboratory, Musculoskeletal Research Center, Department of Orthopaedic Surgery, University of Pittsburgh School of Medicine, 986 Scaife Hall, Pittsburgh, PA 15261, USA;Department of Rheumatology, University Hospital, Gloriastrasse 25, 8091 Zürich, Switzerland;M.E. Müller Institute for Biomechanics, University of Bern, Murtenstrasse 35, PO Box 30, 3010 Bern, Switzerland | |
关键词: Nitric oxide; Interleukin-1; Chondrocyte; Proteoglycan synthesis; Arthritis; Human articular cartilage; hrIL-1; human; recombinant interleukin-1; hrIL-1ra; human; recombinant interleukin-1 receptor antagonist; NMA; N G-monomethyl-l-arginine; NO; nitric oxide; NOS; nitric oxide synthase; PG; proteoglycan; SNAP; S-nitrosyl-acetyl-d; l-penicillamine; | |
DOI : 10.1016/0014-5793(94)00994-5 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Interleukin-1α and β induced the production of large amounts of nitric oxide by normal, human articular chondrocytes in alginate culture; at the same time the biosynthesis of proteoglycan was strongly suppressed. In a dose-dependent manner, N G-monomethyl-l-arginine both inhibited nitric oxide formation and relieved the suppression of proteoglycan synthesis. However concentrations of N G-monomethyl-l-arginine which completely prevented nitric oxide production only partially restored proteoglycan biosynthesis, even at low doses of interleukin-1 where suppression of proteoglycan synthesis was modest. The organic donor of nitric oxide, S-nitrosyl-acetyl-d,l- penicillamine also inhibited proteoglycan biosynthesis, but not as extensively as interleukin-1. These data suggest that interleukin-1 suppresses synthesis of the cartilaginous matrix through more than one mechanism, at least one of which is dependent upon the production of nitric oxide.
【 授权许可】
Unknown
【 预 览 】
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