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Distribution of the cadherin‐catenin complex in normal human thyroid epithelium and a thyroid carcinoma cell line

E‐cadherin is the major cell‐cell adhesion molecule expressed by epithelial cells. Cadherins form a complex with three cytoplasmic proteins, α‐, β‐, and γ‐catenin, and the interaction between them is crucial for anchoring the actin cytoskeleton to the intercellular adherens junctions. The invasive behavior of cancer cells has been attributed to a dysfunction of these molecules. In this study, we examined the distribution of the cadherin‐catenin complex in a Chinese human thyroid cancer cell line, CGTH W‐2, compared with that in normal human thyroid epithelial cells. In the normal cells, using immunofluorescence staining, E‐cadherin and α‐, β‐, and γ‐catenin were found to be localized at the intercellular junction and appeared as 135, 102, 90, and 80 kD proteins on Western blots. In CGTH W‐2 cells, no E‐cadherin and γ‐catenin immunoreactivity was detected by immunofluorescence or Western blotting; α‐ and β‐catenin were detected as 102 and 90 kD proteins on blots but gave a diffuse cytoplasmic immunofluorescence staining pattern in most cells, while β‐catenin was also distributed throughout the cytoplasm in most cells but was found at the cell junction in some, where it colocalized with α‐actinin. The present data indicate that the loss of cell adhesiveness in these cancer cells may be due to incomplete assembly of the cadherin‐catenin complex at the cell junction. However, this defect did not affect the linkage of actin bundles to vinculin‐enriched intercellular junctions. J. Cell. Biochem. 70:330–337, 1998. © 1998 Wiley‐Liss, Inc.