Activation of macrophage promatrix metalloproteinase-9 by lipopolysaccharide-associated proteinases.

@article{Min2002ActivationOM,
  title={Activation of macrophage promatrix metalloproteinase-9 by lipopolysaccharide-associated proteinases.},
  author={Danqing Min and Anthony G. Moore and Michael A. Bain and Samuel N Breit and J Guy Lyons},
  journal={Journal of immunology},
  year={2002},
  volume={168 5},
  pages={
          2449-55
        }
}
LPS induces an up-regulation of promatrix metalloproteinase-9 (proMMP9) gene expression in cells of the monocyte/macrophage lineage. We demonstrate here that LPS preparations are also able to activate proMMP9 made by human macrophages or THP-1 cells via LPS-associated proteinases, which cleave the N-terminal propeptide at a site or sites close to the one cleaved upon activation with organomercurial compounds. LPS-associated proteinases are serine proteinases that are able to cleave denatured… CONTINUE READING
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