The heat shock proteins as targets for radiosensitization and chemosensitization in cancer
- 15 December 2011
- journal article
- review article
- Published by Informa UK Limited in Cancer Biology & Therapy
- Vol. 12 (12), 1023-1031
- https://doi.org/10.4161/cbt.12.12.18374
Abstract
The heat shock proteins (HSPs) represent a class of proteins which are induced under physiologic stress to promote cell survival in the face of endogenous or exogenous injury. HSPs function predominantly as molecular chaperones, maintaining their "client" proteins in the correct conformational state in order to withstand a biologic stressor. Elevated HSP expression is also found in a range of pathologic conditions, notably malignancy. Cancer cells exploit the pro-survival phenotype endowed by HSPs to bolster their proliferative potential. Consequently, developing means of abrogating HSP expression may provide a way to render cancer cells more susceptible to radiation or chemotherapy. Here, we review the members of the HSP class and their roles in malignancy. We focus on attempts to target these proteins, particularly the small HSPs, in developing potent radiation and chemotherapy sensitizers, as well as proposed mechanisms for this sensitization effect.Keywords
This publication has 96 references indexed in Scilit:
- Current state of knowledge regarding the use of antiangiogenic agents with radiation therapyCancer Treatment Reviews, 2011
- Heat shock factors: integrators of cell stress, development and lifespanNature Reviews Molecular Cell Biology, 2010
- Silencing Heat Shock Protein 27 Decreases Metastatic Behavior of Human Head and Neck Squamous Cell Cancer Cells in VitroMolecular Pharmaceutics, 2010
- Heat shock proteins: Cellular and molecular mechanisms in the central nervous systemProgress in Neurobiology, 2010
- Heat Shock Protein 27 as a New Therapeutic Target for Radiation Sensitization of Head and Neck Squamous Cell CarcinomaMolecular Therapy, 2009
- Inhibition of Heat Shock Induction of Heat Shock Protein 70 and Enhancement of Heat Shock Protein 27 Phosphorylation by Quercetin DerivativesJournal of Medicinal Chemistry, 2009
- Targeting Heat Shock Protein 90 Overrides the Resistance of Lung Cancer Cells by Blocking Radiation-Induced Stabilization of Hypoxia-Inducible Factor-1αCancer Research, 2009
- Hsp60D is essential for caspase-mediated induced apoptosis in Drosophila melanogasterCell Stress and Chaperones, 2008
- Hsp27 Inhibits Bax Activation and Apoptosis via a Phosphatidylinositol 3-Kinase-dependent MechanismPublished by Elsevier BV ,2008
- ER chaperones in mammalian development and human diseasesFEBS Letters, 2007