Metalioprotemases a,ld their specific mhibltors, believed to play a role in extraeellular matrix metabolism, are regulated by inflammatory cytokmes. Here we have addressed the question of whether liver, the major site of ~yntltests of plasma pl'oteinase mh~b~tors, is al~o capable ,~f synthesxzing the tissue inhibitor of metalloprotentase-I (TIMP.I) We show at mRNA and protein levels that TIMP-I 15 expres~d in differentiated human hepatoma cells (HepG2) and that its syntltesi.~ is up-regulated by interleakin-6 (IL-6), transforming growth factor ,81 and phorbol 12-mynstate 13-acetate. The physiological role of this phenomenon is underhned by the fact that hpopoly~aeehartde admmistmtmn into rat~ in vlvo. a~ well as IL-6-stmmlation of mt hepatocytes in primary culture, also leads to an merea~e ofTIMP-I mRNA in liver cells
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