Premium
TIMP‐1 protein expression is stimulated by IL‐1β and IL‐6 in primary rat hepatocytes
Author(s) -
Roeb Elke,
Graeve Lutz,
Müllberg Jürgen,
Matern Siegfried,
Rose-John Stefan
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00636-9
Subject(s) - antiserum , polyclonal antibodies , microbiology and biotechnology , transfection , matrix metalloproteinase , immunofluorescence , extracellular matrix , recombinant dna , expression vector , chemistry , glycosylation , biology , biochemistry , antibody , gene , immunology
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.