EBP50 inhibits EGF-induced breast cancer cell proliferation by blocking EGFR phosphorylation

• DOI: 10.1007/s00726-012-1277-z
• Publication Date: 2012-04-03T02:11:21Z
• Authors: Wenfang Yao; Duiping Feng; Weihua Bian; Longyan Yang; Yang Li; Zhiyu Yang; Ying Xiong; Junfang Zheng; Renyou Zhai; Junqi He
• Keywords: 0301 basic medicine; Sodium-Hydrogen Exchangers; Clinical Biochemistry; Breast Neoplasms; Transfection; Biochemistry; 03 medical and health sciences; Cell Line, Tumor; Humans; Phosphorylation; RNA, Small Interfering; Cell Proliferation; Mitogen-Activated Protein Kinase 1; Mitogen-Activated Protein Kinase 3; Epidermal Growth Factor; Organic Chemistry; Phosphoproteins; 3. Good health; ErbB Receptors; Gene Expression Regulation, Neoplastic; Gene Knockdown Techniques; Original Article; Female; Proto-Oncogene Proteins c-akt; Plasmids; Signal Transduction

Ezrin-radixin-moesin-binding phosphoprotein-50 (EBP50) suppresses breast cancer cell proliferation, potentially through its regulatory effect on epidermal growth factor receptor (EGFR) signaling, although the mechanism by which this occurs remains unknown. Thus in our studies, we aimed to determine of EBP50 expression EGF-induced proliferation and activation EGFR signaling lines, MDA-MB-231 MCF-7. In cells, express low levels EBP50, overexpression inhibited ERK1/2 AKT phosphorylation. MCF-7 high knockdown promoted Knockdown EBP50-overexpressed cells abrogated inhibitory EGF-stimulated phosphorylation restoration EBP50-knockdown rescued inhibition phosphorylation, further confirming that downstream molecules could be specifically expression. Since was triggered EGF ligands via detected status presence or absence Overexpression whereas enhanced Meanwhile, total were unaffected during stimulation. Taken together, data shows can suppress inhibiting blocking cells. These results provide insight into molecular regulates development progression cancer.