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Hsp60 Friend and Foe of the Nervous System

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Heat Shock Proteins in Neuroscience

Part of the book series: Heat Shock Proteins ((HESP,volume 20))

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Abstract

Hsp60 belongs to the subgroup of molecular chaperones named chaperonins and, typically, resides and functions in the mitochondria but it is also present in extramitochondrial sites. It chaperones client peptides as they fold to achieve the native conformation and also displays anti-stress roles by helping stress-damaged proteins regain a functional shape. Thus, Hsp60 is central to the integrity and functionality of mitochondria and energy production. All cells in the nervous system depend on Hsp60 so when the chaperonin malfunctions the consequences on nervous tissues are usually devastating, causing diverse diseases. These are the Hsp60 chaperonopathies, which can be genetic or acquired with the former caused by gene variants and the latter by various post-transcriptional mechanisms. All forms of chaperonopathies, i.e., by defect, by excess, and by mistake, associated with Hsp60 have been described, and some illustrative examples are discussed here. It is clear that this chaperonin is key to neuromuscular physiology but, when qualitatively and/or quantitatively abnormal causes diseases, often very serious.

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Abbreviations

Aβ:

Amyloid-β

AChR:

Acetylcholine receptor

AD:

Alzheimer’s disease

APP:

Amyloid precursor protein

BBB:

Blood-brain barrier

CCT:

Chaperonin containing TCP-1

CNS:

Central nervous system

CNV:

Copy number variant

CP:

Chaperoning system

CSF:

Cerebrospinal fluid

CypD:

Cyclophilin D

GMB:

Glioblastoma multiforme

HIP1:

Huntingtin-interacting protein 1

Hsp:

Heat shock protein;

HSP:

Hereditary spastic paraplegia

IS:

Immune system

L-DOPA:

3,4-dihydroxy- L-phenylalanine

MECP2:

Methyl CpG binding protein 2

MG:

Myasthenia gravis

MS:

Multiple sclerosis

mtUPR:

The mitochondrial unfolded protein response

PBMNc:

Peripheral blood mononuclear cells

ROS:

Reactive oxygen species

SNP:

Single-nucleotide polymorphism

SPG:

Spastic paraplegia

TLE:

Temporal lobe epilepsy

TRiC:

TCP-1 ring complex

WHO:

World Health Organization

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Acknowledgements

A.J.L.M, and E.C. de M. were partially supported by IMET. This work was done under the agreement between IEMEST (Italy) and IMET (USA) (this is IMET contribution number IMET 19-007).

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Authors and Affiliations

  1. Department of Biomedicine, Neurosciences, and Advanced Diagnostics, University of Palermo, Palermo, Italy

    Antonella Marino Gammazza, Celeste Caruso Bavisotto, Francesca Rappa, Federica Scalia & Francesco Cappello

  2. Euro-Mediterranean Institute of Science and Technology (IEMEST), Palermo, Italy

    Celeste Caruso Bavisotto, Everly Conway de Macario & Alberto J. L. Macario

  3. Institute of Biophysics (IBF-CNR), National Research Council, Palermo, Italy

    Celeste Caruso Bavisotto

  4. Department of Microbiology and Immunology, University of Maryland at Baltimore-Institute of Marine and Environmental Technology (IMET), Baltimore, MD, USA

    Everly Conway de Macario & Alberto J. L. Macario

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  1. Antonella Marino Gammazza
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  2. Celeste Caruso Bavisotto
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  3. Francesca Rappa
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  4. Federica Scalia
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  5. Everly Conway de Macario
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  6. Alberto J. L. Macario
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  7. Francesco Cappello
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Editors and Affiliations

  1. Department of Medicine and Director, Precision Therapeutics Proteogenomics Diagnostic Center, Eleanor N. Dana Cancer Center, University of Toledo, College of Medicine and Life Sciences, Toledo, OH, USA

    Alexzander A. A. Asea

  2. Department of Experimental Radiation Oncology, MD Anderson Cancer Center, Houston, TX, USA

    Punit Kaur

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Marino Gammazza, A. et al. (2019). Hsp60 Friend and Foe of the Nervous System. In: Asea, A., Kaur, P. (eds) Heat Shock Proteins in Neuroscience. Heat Shock Proteins, vol 20. Springer, Cham. https://doi.org/10.1007/978-3-030-24285-5_1

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