TIMP‐1 protein expression is stimulated by IL‐1β and IL‐6 in primary rat hepatocytes

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Abstract
Degradation of extracellular matrix proteins is performed by metalloproteinases which are inhibited by tissue inhibitors of metalloproteinases (TIMP). We expressed the murine TIMP-1 protein in E. coli and prepared a polyclonal antiserum against the recombinant protein. Using this antiserum we studied the biosynthesis and glycosylation of murine TIMP-1 protein in COS-7 cells transfected with a TIMP-1 expression plasmid by metabolic labeling and indirect immunofluorescence studies. In primary rat hepatocytes we show for the first time that TIMP-1 protein expression is up-regulated upon stimulation with IL-1β and IL-6. Since TIMP-1 is induced during the acute phase reaction it could possibly be involved in the pathogenesis of liver fibrosis.