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Hsp60 in Modifications of Nervous System Homeostasis and Neurodegeneration

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Heat Shock Protein 60 in Human Diseases and Disorders

Abstract

Hsp60 is a critical chaperonin for its role in preserving cell survival and protecting mitochondria against stress conditions. Indeed, mutations or malfunctions of Hsp60 are involved in several human diseases, either genetic or acquired, some of them affecting also the brain. In this chapter, we present several experimental observations supporting the role of Hsp60 in some neurodegenerative diseases. Further, Hsp60, as multifunctional protein, contributes to the protein folding system, to protect mitochondria and is involved in several other cellular pathways that are known to be affected in these diseases. Furthermore, due to its role outside of the mitochondria and in the extracellular fluids, it has also been suggested that Hsp60 has a role in triggering neuroinflammation. Taken together, these considerations strongly suggest the important role for Hsp60 in neurodegenerative diseases and might propose Hp60 as an attractive target for developing future therapies.

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Abbreviations

ACADS:

Acyl-CoA dehydrogenase gene

AD:

Alzheimer’s disease

APP:

Amyloid precursor protein

ATPase:

Adenosine triphosphatase

Aβ:

Amyloid-β peptide

BBB:

Blood brain barrier

CNS:

Central nervous system

CS:

Chaperone system

HD:

Huntington’s disease

Hsp60:

Heat shock protein 60 kDa

HSPD1 :

Heat shock protein family D

HTT:

Huntingtin gene

NDDs:

Neurodegenerative disorders

NFTs:

Neurofibrillary tangles

PD:

Parkinson’s disease

sHsp:

Small heat shock proteins

TLR:

Toll-like receptor

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Acknowledgements

A.P., C.C.B. and F.S. were partially supported by UniPA.

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Correspondence to Celeste Caruso Bavisotto .

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Caruso Bavisotto, C., Scalia, F., Pitruzzella, A., Górska-Ponikowska, M., Marino, C., Taglialatela, G. (2019). Hsp60 in Modifications of Nervous System Homeostasis and Neurodegeneration. In: Asea, A., Kaur, P. (eds) Heat Shock Protein 60 in Human Diseases and Disorders. Heat Shock Proteins, vol 18. Springer, Cham. https://doi.org/10.1007/978-3-030-23154-5_16

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