Interleukin-6-type cytokine-induced changes in acute phase protein glycosylation

Ann N Y Acad Sci. 1995 Jul 21;762:319-30. doi: 10.1111/j.1749-6632.1995.tb32336.x.

Abstract

The plasma levels and the glycosylation of acute-phase proteins (APP) are subject to marked changes during acute and chronic inflammation. The pathophysiological variations in different glycoforms of APP in serum most likely result from changes in the glycosylation process during their biosynthesis in the parenchymal cells of the liver. This is suggested from in vitro studies with isolated hepatocytes and hepatoma cell lines. Inflammatory cytokines appear to regulate the changes in glycosylation independent from the rate of synthesis of the APP. In addition, other humoral factors like corticosteroids and growth factors are involved. The interplay of these factors is determined by the stage of the disease (as in rheumatoid arthritis) or the physiological situation (as in pregnancy). The changes in glycosylation of specific APP might affect the operation of the immune system.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acute-Phase Proteins / metabolism*
  • Concanavalin A / pharmacology
  • Cytokines / pharmacology*
  • Dexamethasone / pharmacology
  • Glycosylation
  • Humans
  • Interleukin-6 / pharmacology*
  • Orosomucoid / metabolism
  • Protein Processing, Post-Translational
  • Transforming Growth Factor beta / pharmacology
  • Tumor Cells, Cultured

Substances

  • Acute-Phase Proteins
  • Cytokines
  • Interleukin-6
  • Orosomucoid
  • Transforming Growth Factor beta
  • Concanavalin A
  • Dexamethasone