EGF rapidly translocates tight junction proteins from the cytoplasm to the cell-cell contact via protein kinase C activation in TMK-1 gastric cancer cells

Exp Cell Res. 2005 Oct 1;309(2):397-409. doi: 10.1016/j.yexcr.2005.06.019.

Abstract

Tight junctions are commonly disrupted in cancer cells, including gastric cancer. Various growth factors have been reported to affect the localization of tight junction-associated proteins such as ZO-1 and occludin. We investigated the effect of epidermal growth factor (EGF), a growth factor that is often overexpressed in gastric cancer, and fetal bovine serum (FBS) on the localization of ZO-1 and occludin in a gastric cancer cell line. In the poorly differentiated gastric cancer cell line TMK-1, immunohistochemistry demonstrated that ZO-1 and occludin were predominantly localized to the cytoplasm, although there was some weak expression at the cell-cell contact. When the medium was replaced with fresh medium containing 10% FBS, ZO-1 and occludin were rapidly translocated from the cytosol to the cell-cell contact. A similar effect was seen in EGF exposure. These effects induced by FBS or EGF were attenuated in the presence of protein kinase C (PKC) inhibitors calphostin C and bisindolylmaleimide I, but not another PKC inhibitor Gö6976, PD98059 (MAPK inhibitor), LY294002 (PI3 kinase inhibitor) or KT5720 (protein kinase A inhibitor). These results suggest that serum-derived factors, including EGF, can rapidly alter the localization of ZO-1 and occludin via a protein kinase C signaling pathway in TMK-1 gastric cancer cells.

MeSH terms

  • Animals
  • Cattle
  • Cell Communication / physiology
  • Cell Line, Tumor
  • Culture Media
  • Cytoplasm / enzymology
  • Cytoplasm / metabolism
  • Epidermal Growth Factor / physiology*
  • Humans
  • Immunohistochemistry
  • Membrane Proteins / metabolism*
  • Occludin
  • Phosphoproteins / metabolism
  • Protein Kinase C / antagonists & inhibitors
  • Protein Kinase C / metabolism*
  • Stomach Neoplasms / enzymology*
  • Tight Junctions / metabolism*
  • Zonula Occludens-1 Protein

Substances

  • Culture Media
  • Membrane Proteins
  • OCLN protein, human
  • Occludin
  • Phosphoproteins
  • TJP1 protein, human
  • Zonula Occludens-1 Protein
  • Epidermal Growth Factor
  • Protein Kinase C