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Heat Shock Protein70 in Neurological Disease

  • Pinar Ortan
  • Ozden Yildirim Akan
  • Ferda Hosgorler
Chapter
First Online:
Part of the Heat Shock Proteins book series (HESP, volume 14)

Abstract

The HSP70 is a chaperon protein that is expressed during stress conditions that participates in many biological processes, including protein trafficking, nascent polypeptide folding and the refolding of the wrong proteins and cleaning of the misfolded ones. The expression is increased during various pathological conditions such as cerebral ischemia, neurodegenerative diseases, epilepsy, and trauma. They are found in both intracellular and extracellular compartments. HSP70 exhibits different functions in accordance with its location. Intracellular HSP70 exerts cytoprotective functions as a chaperone protein, whereas extracellular HSP70 exerts immunomodulatory functions that trigger immunological responses. They play an auxiliary role in antigen presentation in the appearance of immunological response in multiple sclerosis. Epilepsy is thought to have emerged as a stressor. HSP overexpression is proposed as a potential therapy for neurodegenerative diseases characterized by the accumulation or aggregation of abnormal proteins. In this chapter, we wanted to summarize the recent studies on the role of HSP70 in neurological disorders.

Keywords

Alzheimer disease Heat shock protein 70 Hsp70 Neurological disorders Neuroprotection 

Abbreviations

Aβ

Amiloid beta

ALS

Amyotrophic Lateral Sclerosis

CJD

Creutzfeldt-Jakob disease

DA

Dopamine

EAE

Experimental allegic encephalomyelitis

FFI

Fatal familial insomnia

GSS

Gerstmann-Sträussler-Scheinker syndrome

HD

Huntington disease

HSP

Heat shock protein

LRRK2

Leucine-rich repeat kinase-2

MG

Myasthenia gravis

MS

Multiple sclerosis

MTS

Mesial temporal sclerosis

PD

Parkinson’s disease

PINK1

PTEN-induced putative kinase 1

polyQ

Poly-glutamine

PrPC

Cellular prion associated proteins

PrPSc

Disease associated prion proteins

SNCA

Alpha-synuclein

TDP-43

Tar DNA binding protein 43

UPS

Ubiquitin-proteasome system

vCJD

Variant Creutzfeldt-Jakob disease

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Notes

Acknowledgements

We would like to thank the editorial staff for the opportunity of being able to be among the authors of the book.

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Copyright information

© Springer International Publishing AG, part of Springer Nature 2018

Authors and Affiliations

  • Pinar Ortan
    • 1
  • Ozden Yildirim Akan
    • 2
  • Ferda Hosgorler
    • 3
  1. 1.Division of NeurologySB University, Izmir Bozyaka Training and Research HospitalAlsancak IzmirTurkey
  2. 2.Division of İnternal MedicineSB University, Izmir Bozyaka Training and Research HospitalBornova IzmirTurkey
  3. 3.Division of PhysiologyDokuz Eylul University Medical FacultyInciralti/IzmirTurkey

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