Esterase D interacts with metallothionein 2A and inhibits the migration of A549 lung cancer cells in vitro

Author:

Yao Wen12,Chen Xinpeng13,Cui Xiaoling1,Zhou Bangzhao1,Zhao Baoxiang4,Lin ZhaoMin5,Miao Junying1ORCID

Affiliation:

1. Shandong Provincial Key Laboratory of Animal Cells and Developmental Biology, School of Life Science Shandong University Qingdao People's Republic of China

2. Jinan Microecological Biomedicine Shandong Laboratory Jinan People's Republic of China

3. Hubei Key laboratory of Edible Wild Plants Conservation & Utilization, School of Life Science, National Demonstration Center for Experimental Biology Education Hubei Normal University Huangshi People's Republic of China

4. School of Chemistry and Chemical Engineering, Institute of Organic Chemistry Shandong University Jinan People's Republic of China

5. Institute of Medical Science The Second Hospital of Shandong University Jinan People's Republic of China

Abstract

AbstractEsterase D (ESD) is a nonspecific esterase widely distributed in various organisms. ESD plays an important role in regulating cholesterol efflux, inhibiting viral replication and lung cancer growth. MT2A (metallothionein 2A) is the most important isoform of metallothionein (MTs) in human and high expression of MT2A in tumors represents poor prognosis and metastatic behavior. However, there are no reports about the molecular mechanism of ESD in the regulation of tumor metastasis. In this study, we found for the first time that activation ESD promoted its interaction with MT2A and decreased the protein level of MT2A, which resulting in the concentration of free zinc ions up‐regulated, and inhibited the migration of A549 lung cancer cells in vitro.

Funder

National Natural Science Foundation of China

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

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