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Biology of Extracellular HSP60

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Chaperokine Activity of Heat Shock Proteins

Part of the book series: Heat Shock Proteins ((HESP,volume 16))

Abstract

The exposure of cells or organisms to high temperature leads to the release of alert molecules such as Heat Shock Protein: the HSP. This protein family has been initially described in Drosophila. The cellular response to a heat shock involving HSP is conserved across species, from bacteria to humans and including plants. Other stresses, such as ischemia, heavy metal poisoning, nutrient deprivation, irradiations, infections, oxidative stress and inflammation, can also induce the HSP expression. HSP form a large family of proteins which are classified according to their molecular weight: HSP100, HSP90, HSP70, HSP60, HSP40, HSP from 20 to 30 kDa and HSP10. HSP60 has different functions depending on its localization. Intracellular HSP60 can be found in the cytosol, mitochondria and the chloroplast. Therein, it has a chaperone activity by assisting the proteins folding. On the cell surface or in the extracellular medium, HSP60 acts as a danger signaling molecule. Thus, stressed or damaged cells can stimulate the immune system. Indeed, this extracellular HSP60 are involved in several inflammatory pathologies.

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Abbreviations

APC:

Antigen presenting cells

CCT:

“chaperon” containing the T-complex of polypeptide 1

Cpn60:

Chaperonin 60 kDa

DAMP:

Damage associated molecular pattern

DC:

Dendritic cells

HSP:

Heat shock protein

LPS:

Lipopolysaccharide

LTγδ:

Gamma delta T lymphocytes

mtHSP60:

Mitochondrial form

PAMP:

Pathogen associated molecular pattern

RBP:

Rubisco binding protein

sHSP60:

Soluble HSP60

Th:

Helper T lymphocytes

Treg:

Regulatory T lymphocytes

TriC:

TCP-1 Complex ring

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Acknowledgements

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Authors and Affiliations

  1. Université de La Réunion, INSERM, UMR 1188 Diabète athérothombose Thérapies Réunion Océan Indien (DéTROI), Saint-Denis de La Réunion, France

    Brice Nativel, Cynthia Planesse, Christine Robert Da Silva & Olivier Meihac

  2. Université de La Réunion, CNRS UMR9192, INSERM U1187, IRD UMR249, Unité Mixte Processus Infectieux en Milieu Insulaire Tropical (PIMIT), Plateforme Technologique CYROI, Sainte-Clotilde, La Reunion, France

    Philippe Gasque & Wildriss Viranaïcken

  3. Laboratoire de biologie, Secteur Laboratoire d’immunologie clinique et expérimentale de la zone de l’océan indien (LICE-OI) CHU La Réunion site Félix Guyon, Saint-Denis, La Reunion, France

    Philippe Gasque

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  1. Brice Nativel
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  2. Cynthia Planesse
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Correspondence to Wildriss Viranaïcken .

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  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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Nativel, B., Planesse, C., Gasque, P., Da Silva, C.R., Meihac, O., Viranaïcken, W. (2019). Biology of Extracellular HSP60. In: Asea, A., Kaur, P. (eds) Chaperokine Activity of Heat Shock Proteins . Heat Shock Proteins, vol 16. Springer, Cham. https://doi.org/10.1007/978-3-030-02254-9_3

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