Translocation of protein kinase C to membranes induced by TNF does not cause the inhibition of EGF binding to human wish cells

Biochem Biophys Res Commun. 1990 Apr 30;168(2):690-5. doi: 10.1016/0006-291x(90)92376-b.

Abstract

Tumor necrosis factor (TNF) caused an inhibition of 125I-labeled epidermal growth factor [( 125I]EGF) binding to its receptors of human amniotic (WISH) cells at 5 min after addition of TNF, which reached a maximal level (60-70% reduction) after 15-30 min and declined thereafter. TNF also induced a translocation of protein kinase C activity from the cytosol to the membrane, which peaked at 45-60 min after addition of TNF and almost returned to basal level at 120 min. Furthermore, prolonged incubation of WISH cells with 12-O-tetradecanoylphorbol 13 acetate (TPA) diminished the TPA effect on the inhibition of EGF binding to the cells due to the desensitization of protein kinase C; however, TNF still reduced the EGF binding to the cells pretreated with TPA for a long time. These results indicate that although TNF causes the translocation of protein kinase C to the membrane, activation of protein kinase C is not required for TNF to induce a decrease in EGF binding to the cells.

MeSH terms

  • Amnion / metabolism
  • Cell Membrane / drug effects
  • Cell Membrane / enzymology
  • Cells, Cultured
  • Cytosol / drug effects
  • Cytosol / enzymology
  • Epidermal Growth Factor / genetics
  • Epidermal Growth Factor / metabolism*
  • Humans
  • Protein Kinase C / genetics*
  • Translocation, Genetic
  • Tumor Necrosis Factor-alpha / pharmacology*

Substances

  • Tumor Necrosis Factor-alpha
  • Epidermal Growth Factor
  • Protein Kinase C