Biologic effects of an interleukin-1 receptor antagonist protein on interleukin-1-stimulated cartilage erosion and chondrocyte responsiveness

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.

MeSH terms

  • Animals
  • Cartilage / cytology*
  • Dinoprostone / biosynthesis
  • Interleukin-1 / metabolism
  • Interleukin-1 / pharmacology*
  • Rabbits
  • Receptors, Immunologic / antagonists & inhibitors*
  • Receptors, Interleukin-1


  • Interleukin-1
  • Receptors, Immunologic
  • Receptors, Interleukin-1
  • Dinoprostone