Abstract
Heat shock proteins (HSP) play multiple roles in cellular physiology and pathology depending on a wide variety of factors including its relative location within the cell (intracellular, plasma membrane or extracellular milieu), the age of the cell or whether it has undergone neoplastic transformation. In normal non-transformed cells, HSP play a cytoprotective role and protect cells from adverse stressful stimuli via chaperoning naïve, misfolded and/or denatured proteins by a process known as the stress response. However, cancer cells have commandeered this function and the result is increased resistance to a number of anti-cancer therapies including hyperthermia, radiation and a wide range of chemotherapeutic agents. Recent advances in our understanding of this dual role of HSP have led to the development of pharmacological and molecular tool to target HSP for therapeutic gain. In this chapter, we highlight evidence for the involvement of HSP in the pathology of various cancers and discuss their proposed mechanism of action and therapeutic potential
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- AP-1:
-
activator protein-1
- AR:
-
androgen receptor
- CRC:
-
colorectal cancer
- CTL:
-
cytotoxic T lymphocytes
- ERK:
-
extracellular-signal regulated kinase
- GRP:
-
glucose regulated proteins
- HBV:
-
hepatitis B virus
- HCC:
-
hepatocellular carcinoma cells
- HCV:
-
hepatitis C virus
- HER:
-
human endothelial growth factor receptor
- HSF:
-
heat shock factor
- Hsp:
-
heat shock proteins
- hsp :
-
heat shock protein gene
- HSP:
-
heat shock protein family
- HSP :
-
heat shock protein family gene
- JAK/STAT:
-
janus-activated-kinase/signal transducer and activator of transcription
- MAPK:
-
mitogen activated protein kinase
- NK cells:
-
natural killer cells
- NSCLC:
-
non-small cell lung cancer
- PSA:
-
prostate specific antigen
- SAPK/JNK:
-
stress-activated protein kinase/c-Jun N-terminal kinase
- SCC:
-
squamous cell carcinoma
- SCLC:
-
small cell lung cancer
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Acknowledgements
This work was supported in part by a grant from the Scott & White Memorial Hospital and Clinic (to G. M. N.), the National Institutes of Health grant RO1CA91889, institutional support from Scott & White Memorial Hospital and Clinic, Texas A&M University System Health Science Center College of Medicine, the Central Texas Veterans Health Administration and an Endowment from the Cain Foundation (to A. A.).
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Nagaraja, G.M., Asea, A. (2010). Heat Shock Proteins and Cancer. In: Asea, A., Pedersen, B. (eds) Heat Shock Proteins and Whole Body Physiology. Heat Shock Proteins, vol 5. Springer, Dordrecht. https://doi.org/10.1007/978-90-481-3381-9_7
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