Frequent mutation and nuclear localization of β-catenin in anaplastic thyroid carcinoma

Ginesa Garcia-Rostan, Giovanni Tallini, Agustin Herrero, Thomas G. D'Aquila, Maria Luisa Carcangiu, David L. Rimm

Research output: Contribution to journalArticlepeer-review


β-catenin is an ubiquitously expressed cytoplasmic protein that has a crucial role in both E-cadherin-mediated cell-cell adhesion and as a downstream signaling molecule in the wingless pathway. Stabilization of β- catenin followed by nuclear translocation and subsequent T-cell factor/lympboid-enhancing factor-mediated transcriptional activation has been proposed as an important step in oncogenesis. Stabilization may occur through activating mutations in exon-3 at the phosphorylation sites for ubiquitination and degradation of β-catenin. Immunohistochemical subcellular localization of β-catenin and mutational analysis of exon-3 of the β- catenin gene by single-strand conformational polymorphism followed by DNA sequencing was performed on 37 samples from 31 patients with anaplastic thyroid carcinoma. Immunofluorescent staining showed nuclear localization in 15 (42%) of the 36 samples examined. Nucleotide sequencing of mobility shifts detected by single-strand conformational polymorphism revealed somatic alterations in 19 (61%) of the 31 patients analyzed. We conclude that mutations in β-catenin are common in anaplastic thyroid cancer and that they may activate transcription, as illustrated by frequent nuclear localization of the protein. These findings support the idea that β-catenin acts as an oncogene and contributes to the highly aggressive behavior of this tumor.

Original languageEnglish
Pages (from-to)1811-1815
Number of pages5
JournalCancer Research
Issue number8
Publication statusPublished - Apr 15 1999

ASJC Scopus subject areas

  • Cancer Research
  • Oncology

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