Heat Shock Proteins: A Potential Anticancer Target

Author(s): Kamalesh K. Sankhala, Monica M. Mita, Alain C. Mita, Chris H. Takimoto

Journal Name: Current Drug Targets

Volume 12 , Issue 14 , 2011

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Heat shock proteins (Hsp) are highly conserved proteins and their expression is dependent on the level of various cellular stresses. Hsp work as a molecular chaperon for several cellular proteins and have cytoprotective roles. Their function is essential for normal cell viability and growth. Hsp90 interacts with proteins mediating cell signaling involved in essential processes such as proliferation, cell cycle control, angiogenesis and apoptosis. The naturally occurring Hsp90 inhibitor geldanamycin (GA) was the first to demonstrate anticancer activity but its significant toxicity profile in pre-clinical models precluded its clinical development. Subsequent, several Hsp90 inhibitors have been developed and underwent clinical development with favorable safety profiles. Several initial clinical studies have shown promising anticancer activity of Hsp90 inhibitors mainly in breast cancer, non small cell lung carcinoma (NSCLC), gastrointestinal stromal tumors (GIST) and various hematological malignancies. The universal involvement of Hsp90 in multiple oncogenic processes makes Hsp90 inhibitors ideal compounds to be explored as a single agent or in combination with other anticancer therapies.

Keywords: Hsp inhibitors, Hsp90, Geldanamycin, cancer hallmarks, apoptosis, 17-AAG, Tanespamycin, CNF-1010, CNF-2024, Retaspamycin, Avespimycin, SNX-5422

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Article Details

Year: 2011
Published on: 01 March, 2012
Page: [2001 - 2008]
Pages: 8
DOI: 10.2174/138945011798829339
Price: $65

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