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Role of Heat Shock Protein 90 in the Cause of Various Diseases: A Potential Therapeutic Target

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Heat Shock Protein-Based Therapies

Part of the book series: Heat Shock Proteins ((HESP,volume 9))

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Abstract

Different classes of Heat shock proteins (HSP) play a diverse role in influencing proper assembly, folding, and translocation of cellular proteins. HSP90 is one such kind of molecular chaperone which has been implicated the formation of number of diseases like cancer and various kinds of neurodegenerations. The chaperone, HSP90 assists in folding, maturation and maintains the functional stability of many proteins that includes many oncoproteins like p53 as well as neuronal proteins like tau. It also regulates transcription factors including Heat shock factor-1 (HSF-1). In addition to its well characterized functions in malignancy, recent evidence from several laboratories suggests a role for HSP90 in maintaining the functional stability of neuronal proteins of aberrant capacity, whether mutated or over-activated, allowing and sustaining the accumulation of toxic aggregates. Preclinical studies have demonstrated that disruption of much client proteins chaperoned by HSP90 is a possible strategy to reduce tumorigenesis but could suppress many neurodegeneration both in vivo and in vitro. Thus, inhibition of HSP90 has been found to be a novel strategy to target such diseases and pave the novel way of battling with these lethal diseases.

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Abbreviations

17-AAG:

17-allylamino-17-demethoxygeldanamycin

17-DMAG:

17-(Dimethylaminoethylamino)-17-demethoxygeldanamycin

AD:

Alzheimer’s disease

ALS:

Amyotrophic lateral sclerosis

AR:

Androgen receptor

CTD:

C-terminal domain

EGFR:

Epidermal growth factor receptor

GA:

Geldanamycin

HD:

Huntington’s disease

HIF:

Hypoxia-inducible factor

HSF-1:

Heat shock factor-1

HSP:

Heat shock protein

HSR:

Heat stress response

HTS:

High throughput screening

NTD:

N-terminal domain

PD:

Parkinson’s disease

polyQ:

Polyglutamine diseases

SBMA:

Spinal and bulbar muscular atrophy

SCA:

Spinocerebeller ataxia

UPS:

Ubiquitin–proteasome system

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Acknowledgements

We sincerely acknowledge the support provided by Department of Science and Technology (DST) National Institute of Technology Rourkela, Govt. of India for providing necessary facilities to complete this work.

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Authors and Affiliations

  1. Structural Biology & Nanomedicine Laboratory, Department of Biotechnology and Medical Engineering, National Institute of Technology Rourkela, Rourkela, Odisha, 769 008, India

    Subhankar Paul

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Editors and Affiliations

  1. Professor and VD for Research Innovations, Deanship for Scientific Research,, University of Dammam, Dammam, Saudi Arabia

    Alexzander A.A. Asea

  2. Deanship for Scientific Research and Preventive Dental Sciences Department, College of Dentistry, University of Dammam, Dammam, Saudi Arabia

    Naif N. Almasoud

  3. Gastrointestinal Translational Research, Center for Radiation Oncology Research, University of Texas MD Anderson Cancer Center, Houston, Texas, USA

    Sunil Krishnan

  4. Department of Microbiology, Immunology & Biochemistry, Morehouse School of Medicine, Atlanta, Georgia, USA

    Punit Kaur

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Paul, S. (2015). Role of Heat Shock Protein 90 in the Cause of Various Diseases: A Potential Therapeutic Target. In: Asea, A., Almasoud, N., Krishnan, S., Kaur, P. (eds) Heat Shock Protein-Based Therapies. Heat Shock Proteins, vol 9. Springer, Cham. https://doi.org/10.1007/978-3-319-17211-8_14

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