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The Journal of Immunology, 2004, 173: 6973-6980.
Copyright © 2004 by The American Association of Immunologists

Lipopolysaccharide Induces Matrix Metalloproteinase-9 Expression via a Mitochondrial Reactive Oxygen Species-p38 Kinase-Activator Protein-1 Pathway in Raw 264.7 Cells1

Chang-Hoon Woo, Jae-Hyang Lim2 and Jae-Hong Kim3

School of Life Sciences and Biotechnology, Korea University, Seoul, Korea

We have identified a novel signaling pathway that leads to expression of matrix metalloproteinase-9 (MMP-9) in murine macrophages in response to the bacterial endotoxin, LPS. We showed that p38 kinase was essential for this induction and observed that LPS-induced MMP-9 expression was sensitive to rottlerin, a putative protein kinase C{delta} (PKC{delta}) inhibitor. However neither infection with a retrovirus expressing a dominant negative mutant of PKC{delta} nor down-regulation of PKC{delta} by prolonged PMA treatment affected MMP-9 expression, thus excluding involvement of PKC{delta}. Interestingly, LPS-induced MMP-9 expression and p38 kinase phosphorylation were shown to be suppressed by the antioxidant N-acetylcysteine and the flavoenzyme inhibitor diphenyleneiodonium chloride, but not by pyrrolidine dithiocarbamate, an NF-{kappa}B inhibitor. In addition, LPS was found to induce the production of mitochondrial reactive oxygen species (ROS) and this effect was rottlerin-sensitive, suggesting an inhibitory effect of rottlerin on mitochondrial ROS. LPS-induced MMP-9 expression and p38 kinase phosphorylation were also inhibited by rotenone, a specific inhibitor of mitochondrial complex I, supporting the role of mitochondrial ROS in LPS signaling to MMP-9. Finally, we showed that the ROS-p38 kinase cascade targets the transcription factor AP-1. Taken together, our findings identify a ROS-p38 kinase-AP-1 cascade as a novel pathway mediating LPS signaling to MMP-9 expression in macrophages.




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