Targeting heat shock proteins in cancer

被引：344

作者：

Jego, Gaetan ^{[1
,2
]}

Hazoume, Adonis ^{[1
]}

Seigneuric, Renaud ^{[1
,2
,3
]}

Garrido, Carmen ^{[1
]}

机构：

[1] INSERM, U866, F-21033 Dijon, France

[2] Univ Burgundy, F-21078 Dijon, France

[3] CNRS, UMR 5209, ICB, Dept Nanosci, F-21078 Dijon, France

来源：

CANCER LETTERS | 2013年 / 332卷 / 02期

关键词：

Heat shock proteins; Apoptosis; Immunogenicity; Cancer cell growth; Cancer cell resistance; BREAST-CANCER; CHAPERONE FUNCTION; HSP90; INHIBITOR; IN-VITRO; BCR-ABL; CONFERS RESISTANCE; ANTITUMOR-ACTIVITY; ANDROGEN ABLATION; CRYSTAL-STRUCTURE; ATPASE ACTIVITY;

D O I：

10.1016/j.canlet.2010.10.014

中图分类号：

R73 [肿瘤学];

学科分类号：

100214 ;

摘要：

Heat shock proteins (HSPs) HSP27, HSP70 and HSP90 are powerful chaperones. Their expression is induced in response to a wide variety of physiological and environmental insults including anti-cancer chemotherapy, thus allowing the cell to survive to lethal conditions. Different functions of HSPs have been described to account for their cytoprotective function, including their role as molecular chaperones as they play a central role in the correct folding of misfolded proteins, but also their anti-apoptotic properties. HSPs are often overexpressed in cancer cells and this constitutive expression is necessary for cancer cells' survival. HSPs may have oncogene-like functions and likewise mediate "non-oncogene addiction" of stressed tumor cells that must adapt to a hostile microenvironment, thereby becoming dependent for their survival on HSPs. HSP-targeting drugs have therefore emerged as potential anti-cancer agents. This review describes the different molecules and approaches being used or proposed in cancer therapy based on the in inhibition of HSP90, HSP70 and HSP27. (C) 2010 Elsevier Ireland Ltd. All rights reserved.

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页码：275 / 285

页数：11

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