Citation: ZHAI Rui, GONG Xiao-Yun, XIONG Xing-Chuang, JIANG You, HUANG Ze-Jian, FANG Xiang. Progress in Molecular Chaperone Regulation of Heat Shock Protein 90 and Cancer[J]. Chinese Journal of Analytical Chemistry, ;2018, 46(3): 301-310. doi: 10.11895/j.issn.0253-3820.171024 shu

Progress in Molecular Chaperone Regulation of Heat Shock Protein 90 and Cancer

National Institute of Metrology, Beijing 100013, China

Received Date: 20 June 2017
Revised Date: 3 January 2018

Fund Project: This work was supported by the National Key Research and Development Program of China (Nos. 2016YFF0200502,016YFF0200504,2016YFF0102603).

Heat shock protein 90 (HSP90) is a member of genetically conserved heat shock protein family. As an important molecular chaperone in eukaryotic cells, HSP90 plays a key regulatory role in maintaining cellular protein homeostasis. HSP90 clients encompass a wide range of proteins, thus HSP90 is involved in diverse biological process. With the deeper study, it is found that HSP90 takes an important part in the development and metastasis of cancer, and has become a promising target for the study of anticancer biology. We review the progress of HSP90 as molecular chaperone and its relationship with cancer.
- Heat shock protein 90,
- Molecular chaperone,
- Cancer,
- Review
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