Smith R J, Chin J E, Sam L M, Justen J M
Department of Hypersensitivity Diseases Research, Upjohn Company, Kalamazoo, Michigan 49001.
Arthritis Rheum. 1991 Jan;34(1):78-83. doi: 10.1002/art.1780340112.
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.
重组人白细胞介素 -1α（IL-1α）和重组人白细胞介素 -1β刺激牛鼻软骨外植体中的基质蛋白聚糖降解并抑制糖胺聚糖合成。一种17-kd的重组人白细胞介素 -1受体拮抗剂蛋白（IRAP）在软骨器官培养物中引起对IL-1α和IL-1β作用的浓度依赖性（0.2 - 200 ng/ml）抑制。IRAP抑制放射性标记的IL-1α与兔关节软骨细胞的结合。IRAP还抑制IL-1激活的兔关节软骨细胞产生基质金属蛋白酶（胶原酶、明胶酶和基质溶解素）和类前列腺素。这些结果对于基于IRAP开发新的抗关节炎疗法可能具有潜在意义。
