Ochratoxin A alters cell adhesion and gap junction intercellular communication in MDCK cells

Toxicology. 2006 Jun 1;223(1-2):15-25. doi: 10.1016/j.tox.2006.02.024. Epub 2006 Apr 18.

Abstract

Ochratoxin A (OTA) is one of the most potent renal carcinogens studied to date, but the mechanism of tumor formation by ochratoxin A remains largely unknown. Cell adhesion and cell-cell communication participate in the regulation of signaling pathways involved in cell proliferation and growth control and it is therefore not surprising that modulation of cell-cell signaling has been implicated in cancer development. Several nephrotoxicants and renal carcinogens have been shown to alter cell-cell signaling by interference with gap junction intercell communication (GJIC) and/or cell adhesion, and the aim of this study was to determine if disruption of cell-cell interactions occurs in kidney epithelial cells in response to OTA treatment. MDCK cells were treated with OTA (0-50 microM) for up to 24h and gap junction function was analyzed using the scrape-load/dye transfer assay. In addition, expression and intracellular localization of C x 43, E-cadherin and beta-catenin were determined by immunoblot and immunofluorescence analysis. A clear decrease in the distance of dye transfer was evident following treatment with OTA at concentrations/incubation times which did not affect cell viability. Consistent with the functional inhibition of GJIC, treatment with OTA resulted in a dose-dependent decrease in C x 43 expression. In contrast to C x 43, OTA did not alter total amount of the adherens junction proteins E-cadherin and beta-catenin. Moreover, Western blot analysis of Triton X-100 soluble and insoluble protein fractions did not indicate translocation of cell adhesion molecules from the membrane to the cytoplasm. However, a approximately 78 kDa fragment of beta-catenin was detected in the detergent soluble fraction, indicating proteolytic cleavage of beta-catenin. Immunofluorescence analysis also revealed changes in the pattern of both beta-catenin and E-cadherin labeling, suggesting that OTA may alter cell-adhesion. Taken together, these data support the hypothesis that disruption of cell-cell signaling may contribute to OTA toxicity and carcinogenicity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Blotting, Western
  • Cadherins / biosynthesis
  • Carcinogens / toxicity*
  • Cell Adhesion / drug effects
  • Cell Communication / drug effects*
  • Cell Line
  • Cell Survival / drug effects
  • Connexin 43 / biosynthesis
  • Dogs
  • Dose-Response Relationship, Drug
  • Epithelial Cells / cytology
  • Epithelial Cells / drug effects*
  • Epithelial Cells / metabolism
  • Gap Junctions / drug effects*
  • Kidney Tubules, Proximal / cytology
  • Kidney Tubules, Proximal / drug effects
  • Kidney Tubules, Proximal / metabolism
  • Microscopy, Fluorescence
  • Ochratoxins / toxicity*
  • beta Catenin / biosynthesis

Substances

  • Cadherins
  • Carcinogens
  • Connexin 43
  • Ochratoxins
  • beta Catenin
  • ochratoxin A