Matrix metalloproteinase (MMP)-12 regulates MMP-9 expression in interleukin-1beta-treated articular chondrocytes.
Limited information is available on the expression and role of matrix metalloproteinase (MMP)-12 in chondrocytes. We characterized the expression mechanism of MMP-12 and possible function in chondrocytes. Interleukin (IL)-1beta induced the expression and activation of MMP-12 in primary culture chondrocytes and cartilage explants via mitogen-activated protein (MAP) kinase signaling pathways. Among MAP kinases, extracellular signal-regulated kinase and p38 kinase are necessary for MMP-12 expression, whereas c-jun N-terminal kinase is required for the activation of MMP-12. The possibility that MMP-12 acts as a modulator of other MMP was examined. MMP-12 alone did not affect other MMP expressions. However, MMP-12 enhanced expression and activation of MMP-9 in the presence of IL-1beta. Our results indicate that IL-1beta in chondrocytes induces the expression and activation of MMP-12, which, in turn, augments MMP-9 expression and activation.
Oh
Hwanhee
H
Department of Life Science, Cell Dynamics Research Center, Gwangju Institute of Science and Technology, Gwangju 500-712, South Korea.
Yang
Siyoung
S
Park
Meeyoung
M
Chun
Jang-Soo
JS
D000818:Animals; D019902:Chondrocytes / Q000187:drug effects / Q000201:enzymology*; D006801:Humans; D053583:Interleukin-1beta / Q000494:pharmacology*; D020935:MAP Kinase Signaling System; D053508:Matrix Metalloproteinase 12 / Q000235:genetics / Q000378:metabolism*; D020780:Matrix Metalloproteinase 9 / Q000235:genetics / Q000378:metabolism*; D051379:Mice; D011817:Rabbits
D053583:Interleukin-1beta; D020780:Matrix Metalloproteinase 9; D053508:Matrix Metalloproteinase 12