Abstract
BackgroundEzrin-radixin-moesin-binding phosphoprotein 50 (EBP50) is an adapter protein which has been shown to play an active role in a wide variety of cellular processes, including interactions with proteins related to both tumor suppression and oncogenesis. Here we use immunohistochemistry to evaluate EBP50's expression in normal donor prostate (NDP), benign prostatic hyperplasia (BPH), high grade prostatic intraepithelial neoplasia (HGPIN), normal tissue adjacent to prostatic adenocarcinoma (NAC), primary prostatic adenocarcinoma (PCa), and metastatic prostatic adenocarcinoma (Mets).MethodsTissue microarrays were immunohistochemically stained for EBP50, with the staining intensities quantified using automated image analysis software. The data were statistically analyzed using one-way ANOVA with subsequent Tukey tests for multiple comparisons. Eleven cases of NDP, 37 cases of NAC, 15 cases of BPH, 35 cases of HGPIN, 103 cases of PCa, and 36 cases of Mets were analyzed in the microarrays.ResultsSpecimens of PCa and Mets had the lowest absolute staining for EBP50. Mets staining was significantly lower than NDP (p = 0.027), BPH (p = 0.012), NAC (p < 0.001), HGPIN (p < 0.001), and PCa (p = 0.006). Additionally, HGPIN staining was significantly higher than NAC (p < 0.009) and PCa (p < 0.001).ConclusionsTo our knowledge, this represents the first study comparing the immunohistochemical profiles of EBP50 in PCa and Mets to specimens of HGPIN, BPH, NDP, and NAC and suggests that EBP50 expression is decreased in Mets. Given that PCa also had significantly higher expression than Mets, future studies are warranted to assess EBP50's potential as a prognostic biomarker for prostate cancer.
Highlights
Ezrin-radixin-moesin-binding phosphoprotein 50 (EBP50) is an adapter protein which has been shown to play an active role in a wide variety of cellular processes, including interactions with proteins related to both tumor suppression and oncogenesis
Differences were seen between high grade prostatic intraepithelial neoplasia (HGPIN) and prostatic adenocarcinoma (PCa) (p < 0.001) and normal tissue adjacent to prostatic adenocarcinoma (NAC) (p < 0.009)
This finding may indicate that the higher expression of both proteins in HGPIN may reflect a unique feature of the pre-cancerous tissue physiology, and that both may be down regulated in specimens of prostatic adenocarcinoma
Summary
Ezrin-radixin-moesin-binding phosphoprotein 50 (EBP50) is an adapter protein which has been shown to play an active role in a wide variety of cellular processes, including interactions with proteins related to both tumor suppression and oncogenesis. There is currently a limited amount of information in the literature on biomarkers with the potential to discern which cases of prostate cancer have the greatest. One such biomarker is ezrin-radixin-moesin-binding phosphoprotein 50 (EBP50), which is known as Na +/H+ exchanger regulatory factor 1, or NHERF1. It has been described as a participant in at least 30 unique cellular interactions, including those involving ion transport, secondarily coupled signaling receptors, and tyrosine kinase receptors[5]. Among the oncologically relevant functions for the protein that have been demonstrated are its ability to recruit the tumor suppressor PTEN for inactivation of the phosphatidylinositol-3-OH kinase (PI3K)/Akt signaling pathway in glioblastoma multiforme[5,7], as well as an ability to provide cortical stabilization of b-catenin at cellular junctions in murine embryonic fibroblast models[8], both indicative of a tumor suppressor function
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