Aims: Ezrin-radixin-moesin-binding phosphoprotein 50 (EBP50) is a post synaptic density-95/Disk-large/ZO-1 homologous domain-containing protein that is involved in the linkage of integral membrane proteins to the cytoskeleton and plays an important role in cell signalling. To gain insights into its biological relevance, this study examined expression of EBP50 in two cohorts of breast carcinoma. Methods and results: Forty-nine breast carcinoma tissue specimens were first examined by both immunohistochemistry and RNA in situ hybridization. EBP50 expression was correlated with various clinicopathological variables. The relative abundance of EBP50 mRNA in breast carcinomas and their corresponding normal tissue was compared using reverse transcriptase-polymerase chain reaction (RT-PCR). EBP50 immunoreactivity was then further independently validated in 120 breast carcinomas on tissue microarrays. EBP50 immunoreactivity was observed in morphologically normal and cancerous epithelial cells contrasting with the adjacent immunonegative stromal cells. An elevated cytoplasmic accumulation of EBP50 protein was readily detected in 73.5-80% of breast carcinomas. EBP50 immunoreactivity was significantly associated with tumour stage, lymph node and oestrogen receptor status. These immunohistochemical observations were further validated using RNA in situ hybridization and RT-PCR. EBP50 immunoreactivity was significantly correlated with the mRNA expression level. Conclusion: Oestrogen-responsive EBP50 may play an important role in tumour progression and might be a potential marker of invasiveness for breast cancer.
- Breast cancer
- RNA in situ hybridization
ASJC Scopus subject areas
- Pathology and Forensic Medicine