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- W1857723745 abstract "Abstract The proteolytic cleavage of a variety of membrane proteins, including pro-tumor necrosis factor α (pro-TNF-α), is induced by various reagents such as phorbol 12-myristate 13-acetate (PMA). In this study we generated a human macrophage cell line that constitutively produces TNF-α, and examined how the processing and release of TNF-α are regulated. The processing and release of TNF-α were enhanced by PMA through a protein kinase C-dependent pathway. Although only hy-droxamate matrix metalloproteinase (MMP) inhibitors inhibited the basal processing and release of TNF-α, the PMA-induced processing and release of TNF-α were inhibited not only by MMP inhibitors but also by 1,10-phenanthroline, 3,4-dichloroiso-coumarin (3,4-DCI), iodoacetamide, and Nα-p-tosyl-l-phenylalanine chloromethyl ketone (TPCK). Hydroxamate MMP inhibitors and 1,10-phenanthroline inhibited the processing of TNF-α on the cell surface, whereas 3,4-DCI, iodoacetamide, and TPCK inhibited the transport of TNF-α to the cell surface. These results suggest that serine and/or cysteine protease(s) may be involved in PMA-induced processing and/or transport to the cell surface. J. Leukoc. Biol. 66: 968–973; 1999." @default.
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- W1857723745 date "1999-12-01" @default.
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- W1857723745 title "Regulation of the processing and release of tumor necrosis factor α in a human macrophage cell line" @default.
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- W1857723745 doi "https://doi.org/10.1002/jlb.66.6.968" @default.
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