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-1 beta and IL-6. Since TIMP-1 is induced during the acute phase reaction it could possibly be involved in the pathogenesis of liver fibrosis.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Roeb E,Graeve L,Müllberg J,Matern S,Rose-John Sdoi
10.1016/0014-5793(94)00636-9subject
Has Abstractpub_date
1994-07-25 00:00:00pages
45-9issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(94)00636-9journal_volume
349pub_type
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