1. Heat shock proteins and cancer: How can nanomedicine be harnessed?
- Author
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Sauvage F, Messaoudi S, Fattal E, Barratt G, and Vergnaud-Gauduchon J
- Subjects
- Animals, Antineoplastic Agents therapeutic use, Drug Carriers chemistry, HSP90 Heat-Shock Proteins metabolism, Heat-Shock Proteins antagonists & inhibitors, Heat-Shock Proteins metabolism, Humans, Molecular Targeted Therapy methods, Nanomedicine methods, Nanoparticles chemistry, Neoplasms metabolism, Antineoplastic Agents administration & dosage, Drug Delivery Systems methods, HSP90 Heat-Shock Proteins antagonists & inhibitors, Neoplasms drug therapy
- Abstract
Heat shock protein (hsp90) is an interesting target for cancer therapy because it is involved in the folding and stabilization of numerous proteins, including many that contribute to the development of cancer. It is part of the chaperone machinery that includes other heat shock proteins (hsp70, hsp27, hsp40) and is mainly localized in the cytosol, although many analogues or isoforms can be found in mitochondrion, endoplasmic reticulum and the cell membrane. Many potential inhibitors of hsp90 have been tested for cancer therapy but their usefulness is limited by their poor solubility in water and their ability to reach the target cells and the correct intracellular compartment. Nanomedicine, the incorporation of active molecules into an appropriate delivery system, could provide a solution to these drawbacks. In this review, we explain the rationale for using nanomedicine for this sort of cancer therapy, considering the properties of the chaperone machinery and of the different hsp90 analogues. We present some results that have already been obtained and put forward some strategies for delivery of hsp90 analogues to specific organelles., (Copyright © 2017 Elsevier B.V. All rights reserved.)
- Published
- 2017
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