In this study, we determined whether the proinflammatory cytokines tumor necrosis factor (TNF)-alpha and interleukin-1 beta contribute to the regulation of matrix metalloproteinase (MMP)-9 in human bronchial epithelial cells and whether the induction of MMP-9 is regulated by the transcription factor nuclear factor (NF)-kappa B. We demonstrated that TNF-alpha induced MMP-9 at both the protein and mRNA levels in human bronchial epithelial cells and that interleukin-1 beta did not. In contrast, induction of the tissue inhibitor of metalloproteinase-1 by TNF-alpha was less than that of interleukin-1 beta. Increased expression of MMP-9 and NF-kappa B activation induced by TNF-alpha were inhibited by pyrrolidine dithiocarbamate and N-acetyl-L-cysteine but were not inhibited by curcumin. These results suggest that TNF-alpha induces the expression of MMP-9 in human bronchial epithelial cells and that this induction is mediated via the NF-kappa B-mediated pathway.
A supramolecular dual-synthon with 2 R 4 (10) ring and columnar motifs is observed in crystal structures of all 2-, 3-and 4-methylstyrylpyridinium chlorides and 3-bromo-, 3-nitro-and 4-trifluoromethylstyrylpyridinium chlorides. The dual-synthon assembled through N-H … Cl 2 and C-H … Cl 2 hydrogen bonds and cation-p interactions forms both ladder-like and head-to-head or head-to-tail columnar motifs. The position of the methyl group at the benzene ring affects the size and shape of the channel structure.Infinite hydrogen bond networks involving chloride anions, water and HCl molecules are found in the channels of 3-and 4-methylstyrylpyridinium chlorides. Variations in electron-withdrawing groups such as Br, NO 2 and CF 3 have little effect on the crystal structures.
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