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    Biochem J. 1991 Aug 1;277 ( Pt 3):659-64.

    Structural and functional studies on the human hepatic interleukin-6 receptor. Molecular cloning and overexpression in HepG2 cells.

    Schooltink H, Stoyan T, Lenz D, Schmitz H, Hirano T, Kishimoto T, Heinrich PC, Rose-John S.

    Institut für Biochemie der RWTH Aacehn, Federal Republic of Germany.

    cDNAs coding for the human hepatic interleukin-6 receptor (IL-6-R) have been isolated from a library made from poly(A) RNA of dexamethasone-treated human hepatoma cells (HepG2). We found the hepatic IL-6-R to be identical to the one expressed by leucocytes. A polyclonal antiserum was raised in rabbits against the IL-6-R protein expressed in Escherichia coli. Although the entire IL-6-R protein was used for immunization, only antibodies to the cytoplasmic domain of the IL-6-R were obtained. It is demonstrated by affinity cross-linking and subsequent immunoprecipitation with antibodies against the ligand as well as against the receptor that the cloned cDNA codes for the functional IL-6-R on HepG2 cells. When the hepatic IL-6-R cDNA was overexpressed in HepG2 cells, these cells became more sensitive to low concentrations of IL-6 with respect to the induction of gamma-fibrinogen mRNA.

    PMID: 1872801 [PubMed - indexed for MEDLINE]

    PMCID: PMC1151293

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