HspB1, HspB5 and HspB4 in Human Cancers: Potent Oncogenic Role of Some of Their Client Proteins

被引：83

作者：

Arrigo, Andre-Patrick ^{[1
]}

Gibert, Benjamin ^{[1
]}

机构：

[1] Claude Bernard Univ Lyon 1, INSERM U1052 CNRS UMR5286, Lyon Canc Res Ctr, Canc & Dev Lab, F-69008 Lyon, France

来源：

CANCERS | 2014年 / 6卷 / 01期

关键词：

human small Hsps; HspB1; HspB5; HspB4; Hsp27; alphaA-crystallin; alphaB-crystallin; clients; cancer; ALPHA-B-CRYSTALLIN; HEAT-SHOCK-PROTEIN; SMALL STRESS-PROTEINS; EPITHELIAL-MESENCHYMAL TRANSITION; CISPLATIN-INDUCED APOPTOSIS; SQUAMOUS-CELL CARCINOMA; C-DEPENDENT ACTIVATION; PROTECTIVE ACTIVITY; ACTIN CYTOSKELETON; OXIDATIVE STRESS;

D O I：

10.3390/cancers6010333

中图分类号：

R73 [肿瘤学];

学科分类号：

100214 [肿瘤学];

摘要：

Human small heat shock proteins are molecular chaperones that regulate fundamental cellular processes in normal unstressed cells as well as in many cancer cells where they are over-expressed. These proteins are characterized by cell physiology dependent changes in their oligomerization and phosphorylation status. These structural changes allow them to interact with many different client proteins that subsequently display modified activity and/or half-life. Nowdays, the protein interactomes of small Hsps are under intense investigations and will represent, when completed, key parameters to elaborate therapeutic strategies aimed at modulating the functions of these chaperones. Here, we have analyzed the potential pro-cancerous roles of several client proteins that have been described so far to interact with HspB1 (Hsp27) and its close members HspB5 (alpha B-crystallin) and HspB4 (alpha A-crystallin).

引用

页码：333 / 365

页数：33

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