Inhibition of Heat Shock Protein 90 as a Novel Platform for the Treatment of Cancer

Chang Gao; Ya-Nan Peng; Hai-Zhou Wang; Shi-Lin Fang; Meng Zhang; Qiu Zhao; Jing Liu

doi:10.2174/1381612825666190503145944

Inhibition of Heat Shock Protein 90 as a Novel Platform for the Treatment of Cancer

Curr Pharm Des. 2019;25(8):849-855. doi: 10.2174/1381612825666190503145944.

Authors

Chang Gao^{1

2}, Ya-Nan Peng^{1

2}, Hai-Zhou Wang^{1

2}, Shi-Lin Fang^{1

2}, Meng Zhang^{1

2}, Qiu Zhao^{1

2}, Jing Liu^{1

2}

Affiliations

¹ Department of Gastroenterology, Zhongnan Hospital of Wuhan University, Wuhan, China.
² Hubei Clinical Center and Key Lab of Intestinal and Colorectal Diseases, Wuhan, China.

PMID: 31244417
DOI: 10.2174/1381612825666190503145944

Abstract

Heat shock protein 90 (Hsp90) plays an essential role in various physiological and pathological processes. It activates client proteins to participate in tumor progression. Blocking Hsp90 could enable effective antitumor effects in many tumor types, such as multiple myeloma and colon cancer. Recently, it has motivated an interest in Hsp90 inhibitors that bind to the N-terminal or C-terminal ATP pocket as antitumor drugs. We reviewed the data from experimental and clinical trials on Hsp90 inhibitors in the treatment of different malignancies to explore and summarize their antitumor mechanisms.

Keywords: ATPase; Heat shock protein 90; cancer treatment; client protein; inhibitor; signaling pathway..

Publication types

Research Support, Non-U.S. Gov't
Review

MeSH terms

Antineoplastic Agents / pharmacology*
HSP90 Heat-Shock Proteins / antagonists & inhibitors*
Humans
Neoplasms / drug therapy*

Substances

Antineoplastic Agents
HSP90 Heat-Shock Proteins