Heat Shock Proteins 27 and 70: Anti-Apoptotic Proteins with Tumorigenic Properties

Carmen Garrido, Mathilde Brunet, Celine Didelot, Yael Zermati, Elise Schmitt and Guido Kroemer

volume 5 | issue 22

15 november 2006
Pages: 2592 - 2601

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Heat shock proteins (HSP) HSP27 and HSP70 are expressed in response to a wide variety of physiological and environmental insults including anticancer chemotherapy, thus allowing the cell to survive to lethal conditions. Several mechanisms account for the cytoprotective effect of HSP27 and HSP70. 1) Both proteins are powerful chaperones. 2) They both inhibit key effectors of the apoptotic machinery at the pre- and post-mitochondrial level. 3) They participate in the proteasome-mediated degradation of proteins under stress conditions, thereby contributing to the so called “protein triage”. In cancer cells, the expression of HSP27 and/or HSP70 is abnormally high, and both HSP27 and HSP70 may participate in oncogenesis and in resistance to chemotherapy. In rodent models, HSP27 or HSP70 over-expression increases tumor growth and metastatic potential. The depletion or inhibition of HSP27 and HS70 frequently reduces the size of the tumors and even can cause their complete involution (for HSP70). Therefore, the inhibition of HSP70 and HSP27 has become a novel strategy of cancer therapy.

Authors

Carmen Garrido

INSERM UMR 866, Dijon, Burgundy, France

Mathilde Brunet

INSERM U-517, Faculty of Medicine and Pharmacy; Dijon, Franc

Celine Didelot

INSERM UMR 866, Dijon, Burgundy, France

Yael Zermati

INSERM F-94805; Villejuif, France;

Elise Schmitt

INSERM U-517, Faculty of Medicine and Pharmacy; Dijon, Franc

Guido Kroemer

INSERM; Villejuif, France

We now provide open access to journal articles published online for one year or more. This article may be downloaded at the following link: