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• W1671601265 endingPage "2455" @default.
• W1671601265 startingPage "2449" @default.
• W1671601265 abstract "Abstract 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 collagens (gelatin) and the mammalian serine proteinase inhibitor, α1-proteinase inhibitor, thereby pushing the balance of extracellular matrix turnover even further toward degradation. A low molecular mass, low affinity inhibitor of MMP9, possibly derived from the propeptide, is generated during proMMP9 activation. However, inhibition of the LPS-associated proteinases had no effect on proMMP9 synthesis, indicating that their proteolytic activity was not required for signaling the up-regulation of the proMMP9 gene." @default.
• W1671601265 created "2016-06-24" @default.
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• W1671601265 date "2002-03-01" @default.
• W1671601265 modified "2023-10-18" @default.
• W1671601265 title "Activation of Macrophage Promatrix Metalloproteinase-9 by Lipopolysaccharide-Associated Proteinases" @default.
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• W1671601265 doi "https://doi.org/10.4049/jimmunol.168.5.2449" @default.
• W1671601265 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11859137" @default.
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