Literature DB >> 28739728

Ezrin-Radixin-Moesin Binding Phosphoprotein 50 (EBP50) Suppresses the Metastasis of Breast Cancer and HeLa Cells by Inhibiting Matrix Metalloproteinase-2 Activity.

Lei Wang1, Yijun Qi2, Ying Xiong2, Zhiqiang Peng2, Qiang Ma2, Yue Zhang2, Jian Song1, Junfang Zheng3,4.   

Abstract

BACKGROUND: Expression of ezrin-radixin-moesin-binding phosphoprotein-50 (EBP50) is correlated with human breast and cervical cancer development, but its effects on the metastasis of breast and cervical cancer and the underlying mechanism are not fully understood.
MATERIALS AND METHODS: In this study, EBP50 was overexpressed in MDA-MB-231 breast cancer and HeLa cervical cancer cells; moreover, EBP50 was knocked-down in MCF-7 breast cancer cells and HeLa cells. Metastasis-related ability and matrix metalloproteinase-2 (MMP-2) activity of these cells were investigated.
RESULTS: Cell adhesion, wound-healing and invasion were significantly suppressed in EBP50-overexpressing cells. Contrarily, EBP50-knockdown promoted cell adhesion, wound healing and invasion. EBP50 overexpression inhibited MMP-2 activity, and the knockdown of EBP50 promoted the activity of MMP-2, suggesting that EBP50 inhibited cell metastasis via suppression of MMP-2 activity.
CONCLUSION: Our work reveals the anti-metastatic effect and a new mechanism of EBP50 action in breast and cervical cancer cells. Copyright
© 2017, International Institute of Anticancer Research (Dr. George J. Delinasios), All rights reserved.

Entities:  

Keywords:  EBP50; adhesion; matrix metalloproteinase-2; migration

Mesh:

Substances:

Year:  2017        PMID: 28739728     DOI: 10.21873/anticanres.11829

Source DB:  PubMed          Journal:  Anticancer Res        ISSN: 0250-7005            Impact factor:   2.480


  5 in total

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