Cancer Res  1998 Jun 15;58(12):2520-3 

Beta-catenin mutations in human prostate cancer.

Voeller HJ, Truica CI, Gelmann EP.

Division of Hematology/Oncology, Lombardi Cancer Center, Georgetown University
School of Medicine, Washington, DC 20007-2197, USA.

Beta-catenin plays essential roles in both intercellular adhesion and signal
transduction. As a signaling molecule, beta-catenin supplies an activating
domain to the T-cell factor/lymphoid enhancer-binding factor family of
DNA-binding proteins and activates gene transcription. Posttranslational
stabilization of beta-catenin, leading to elevated protein levels and
constitutive gene activation, has been proposed as an important step in
oncogenesis. Stabilization of beta-catenin can occur through mutation to highly
conserved amino acids encoded in exon 3 of the beta-catenin gene (CTNNB1). To
determine whether this pathway of malignant transformation is important in
prostate cancer, we analyzed 104 prostate cancer tissue specimens, 4 prostate
cancer cell lines, and 3 prostate tumor xenografts for activating mutations in
exon 3 of CTNNB1. Mutations were detected in 5 of the 104 prostate cancer tissue
samples. Four of the five mutations involved serine or threonine residues
implicated in the degradation of beta-catenin. A fifth tumor had a mutation at
codon 32, changing a highly conserved aspartic acid to a tyrosine. Mutational
analysis of multiple regions from several tumor samples showed that the
beta-catenin mutations were present focally and therefore may occur during tumor
progression.

PMID: 9635571 [PubMed - indexed for MEDLINE]