Expression of ezrin and moesin in primary breast carcinoma and matched lymph node metastases

Abstract

Ezrin, radixin, moesin (ERM) are important membrane-cytoskeletal crosslinkers and are suggested to play important role in cancer progression and metastasis. Even though ERM proteins were generally considered to be functionally redundant and the most studied was ezrin, recent studies highlight their distinct roles in metastatic process. Little information is available regarding the role of individual ERM proteins and their phosphorylated forms in human breast cancer. Our study is the first to examine expression of ezrin, moesin and their phosphorylated forms in primary breast tumors and matched lymph node metastases (LNMs) and their correlation with clinicopathological variables. A total of 88 primary breast cancer, 91 LNMs, 54 intraductal carcinoma and 26 normal adjacent breast tissue samples from tissue microarrays were studied. Expression was determined by immunohistochemistry, the intensity and number of positive cells was scored. Statistical analysis of protein expression and patients' age, tumor grade and hormonal status was performed. No statistical significant difference was found in ezrin, moesin, p-ezrinTyr353 and pan-p-ezrinThr567/radixinThr564/moesinThr558 expression between primary tumors and LNMs. Even though it was not significant, moesin expression varied between primary tumors, intraductal carcinoma, normal breast adjacent tissue and LNMs. A significant positive correlation between moesin and tumor grade has been proven. Even though primary tumors and matched LNMs did not show different expression patterns, moesin correlated significantly with higher tumor grade. Its positivity in intraductal carcinoma and normal breast tissue adjacent to cancer might indicate its role in tumor intiation/progression.

Microgravity Affects Thyroid Cancer Cells during the TEXUS-53 Mission Stronger than Hypergravity

“…Moesin forms a complex with ezrin and is able to bind to actin [36,37]. These proteins are strikingly involved in the surface structure adhesion, migration and have been associated with some human cancers [38,39]. Ezrin and moesin have also been found to be modulated in previous µ g -experiments with thyroid cells [12,28].…”

Ezrin and E-cadherin expression profile in cervical cytology: a prognostic marker for tumor progression in cervical cancer

“…Proteins of the Ezrin/Radixin/Moesin (ERM) family, participate in the regulation of cell networks associated with tumor progression, through their interaction with membrane proteins, the actin cytoskeleton and signaling molecules, such as CD43, CD44, ICAM-1, ICAM-2 or EGFR [ 9 , 10 ]. Ezrin is the most studied member of the family, it is expressed in epithelial cells and its overexpression has been reported in breast cancer [ 11 ], prostate cancer [ 12 ], hepatocellular carcinoma [ 13 ], ovarian cancer [ 14 ], and endometrial cancer [ 15 ]. Ezrin overexpression is associated with poor prognosis and tumor invasiveness.…”

Kallikrein-related peptidases 4, 5, 6 and 7 regulate tumour-associated factors in serous ovarian cancer

“…Upregulation and phosphorylation of MSN, and other ERM proteins, are prerequisites for a malignant phenotype in other tumour types, for example in glioblastoma, 40 melanoma, 41 cervical cancer, 42 oral squamous cell carcinoma, 43 diffuse large B-cell lymphoma 44 and breast cancer. 45 MSN was positively correlated with tumour grade of breast cancers, depicting a cytoplasmic and membranous staining pattern mostly in normal adjacent tissues. 45 Interaction of the tumour suppressor BRCA1 with ERM proteins reduced spreading and motility of breast cancer cells.…”