Soluble human interleukin-6-receptor modulates interleukin-6-dependent N-glycosylation of α 1-protease inhibitor secreted by HepG2 cells

Interleukin-6 (IL-6) induces changes in gene expression and the N-glycosylation pattern of acute-phase proteins in hepatocytes. IL-6 exerts its action via a cell surface receptor complex consisting of an 80 kDa IL-6 binding protein (gp80) and a 130 kDa glycoprotein (gp130) involved in signal transdu...

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Veröffentlicht in:FEBS letters 1992-07, Vol.306 (2), p.257-261
Hauptverfasser: Mackiewicz, Andrzej, Rose-John, Stefan, Schooltink, Heidi, Laciak, Maria, Górny, Aleksander, Heinrich, Peter C.
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Sprache:eng
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Zusammenfassung:Interleukin-6 (IL-6) induces changes in gene expression and the N-glycosylation pattern of acute-phase proteins in hepatocytes. IL-6 exerts its action via a cell surface receptor complex consisting of an 80 kDa IL-6 binding protein (gp80) and a 130 kDa glycoprotein (gp130) involved in signal transduction. A genetically engineered gp80-derived soluble human IL-6-receptor (shIL-6-R) significantly enhanced the IL-6 effect on N-glycosylation changes (revealed by reactivity with the lectin—concanavalin A) of a 1-protease inhibitor (PI) secreted by human hepatoma cells (HepG2). Stable transfection of IL-6-cDNA into HepG2 cells (HepG2-IL-6) resulting in constitutive secretion of 2 μg of IL-6 per 10 6 cells in 24 h led to a down-regulation of surface-bound gp80 and subsequent homologous desensitization or HepG2-IL-6 cells towards IL-6. Soluble human IL-6-R functionally substituted membrane-bound gp80 resulting in a reconstitution of responsiveness of HepG2-IL-6 cells.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(92)81012-B