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The engineered expression of secreted HSPB5-Fc in CHO cells exhibits cytoprotection in vitro

Authors
  • Li, Jing1, 2
  • Yu, Jingjing1
  • Xue, Wenxian1
  • Huang, Huili1
  • Yan, Longjun1
  • Sang, Fan1
  • An, Shuangshuang1
  • Zhang, Jing1
  • Wang, Mingli1
  • Zhang, Jun1
  • Li, Hui1
  • Cui, Xiukun1
  • He, Jiang3
  • Hu, Yanzhong1, 2, 4
  • 1 Henan University, Jin-Ming Road, Kaifeng, 475004, China , Kaifeng (China)
  • 2 Kaifeng Central Hospital, Kaifeng, China , Kaifeng (China)
  • 3 Central South University, Changsha, China , Changsha (China)
  • 4 First Affiliated Hospital of Zhengzhou University, Zhengzhou, China , Zhengzhou (China)
Type
Published Article
Journal
BMC Biotechnology
Publisher
Springer (Biomed Central Ltd.)
Publication Date
Jun 14, 2021
Volume
21
Issue
1
Identifiers
DOI: 10.1186/s12896-021-00700-y
Source
Springer Nature
Keywords
Disciplines
  • Research
License
Green

Abstract

BackgroundHSPB5 is an ATP-independent molecular chaperone that is induced by heat shock or other proteotoxic stresses. HSPB5 is cytoprotective against stress both intracellularly and extracellularly. It acts as a potential therapeutic candidate in ischemia-reperfusion and neurodegenerative diseases.ResultsIn this paper, we constructed a recombinant plasmid that expresses and extracellularly secrets a HSPB5-Fc fusion protein (sHSPB5-Fc) at 0.42 μg/ml in CHO-K1 cells. This sHSPB5-Fc protein contains a Fc-tag at the C-terminal extension of HSPB5, facilitating protein-affinity purification. Our study shows that sHSPB5-Fc inhibits heat-induced aggregation of citrate synthase in a time and dose dependent manner in vitro. Administration of sHSPB5-Fc protects lens epithelial cells against cisplatin- or UVB-induced cell apoptosis. It also decreases GFP-Httex1-Q74 insolubility, and reduces the size and cytotoxicity of GFP-Httex1-Q74 aggregates in PC-12 cells.ConclusionThis recombinant sHSPB5-Fc exhibits chaperone activity to protect cells against proteotoxicity.

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