Exp Mol Med.  2004 Jun;36(3):226-232.

Interleukin-1beta stimulates matrix metalloproteinase-2 expression via a prostaglandin E2-dependent mechanism in human chondrocytes

  • 1Department of Biochemistry and Molecular Biology, Yeungnam University, Daegu 705-035, Korea. sbaek@med.yu.ac.kr
  • 2Department of Plastic Surgery, College of Medicine, Yeungnam University, Daegu 705-035, Korea.
  • 3Department of Biology, Teacher's, Kyungpook National University, Daegu 702-70, Korea.
  • 4Department of Biology, College of Natural Sciences, Kyungpook National University, Daegu 702-70, Korea.


IL-1beta is known promote cyclooxygenase-2 (COX- 2) and matrix metalloproteinase-2 (MMP-2) expression. This study focuses on the characterization of the signaling cascade associated with IL-1beta-induced matrix metalloproteinase-2 (MMP- 2) regulation in human chondrocytes. The decrease in collagen levels in the conditioned media was prevented by a broad spectrum MMP inhibitor, suggesting that IL-1beta promotes the proteolytic process leading to MMP-2 activation. IL-1beta-related MMP-2 expression was found to be dependent on prostaglandin E2 (PGE2) production. In addition, the induction of COX-2 and MMP-2 was inhibited by the pretreatment of chondrocytes with a SB203580 or Ro 31-8220, indicating the involvement of protein kinase C (PKC) or p38 mitogen-activated protein kinase (MAPK). However, there is no cross-talk between PKC and p38 MAPK in the IL-1beta-induced MMP-2 activation. Taken together, these results demonstrated that IL-1beta induces MMP-2 expression through the PGE2-dependent mechanism in human chondrocytes.


chondrocytes; gelatinase A; interleukin-1; mitogen-activated; prostaglandin endoperoxide synthase; prostaglandin E; protein kinases
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