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Heat Shock Protein 60 in Human Diseases and Disorders pp 269–276Cite as

Hsp60 in Skeletal Muscle: From Molecular Anatomy to Pathophysiology

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Part of the book series: Heat Shock Proteins ((HESP,volume 18))

Abstract

The chaperoning system of an organism is composed of the entire set of chaperones, co-chaperones, and chaperone co-factors and their interactors and receptors. Its functions pertain typically to protein homeostasis but also to many other activities inside and outside cells. In the skeletal muscle, with its multi-molecular structures rich in proteins and their continuous rearrangements, the chaperoning system plays a crucial role. However, little is known about the details of the workings of the chaperoning system in skeletal muscle development and during exercise and disease. Molecular chaperones are surely involved in muscle formation and maintenance under physiologic conditions and under stress but if abnormal or involved in a pathogenic pathway can cause disease, a chaperonopathy. There are many genetic and acquired chaperonopathies affecting muscles primarily. For these reasons, we have begun to study chaperones in skeletal muscle, focusing on Hsp60. This chaperone is essential for muscle activity since it maintains the functionality of the respiratory chain inside the mitochondria, among other critical functions such as defense against oxidative stress. In addition, in skeletal muscle, Hsp60 occurs in the cytosol and the extracellular space but its functions in these non-canonical locations remain to be elucidated.

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Abbreviations

EDL:

extensor digitorum longus

HSP:

heat shock proteins

MHC:

myosin heavy chain

PGC-1α:

Peroxisome proliferator-activated receptor gamma coactivator 1 alpha

ROS:

reactive oxygen species

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Acknowledgements

This study was funded by “Ministero dell’Istruzione, dell’Università e della Ricerca” (PRIN2012-prot. 2012N8YJC3- Prof. Daniela Caporossi/Prof. Felicia Farina). A.J.L.M was partially supported by IMET. This work was done under the agreement between IEMEST (Italy) and IMET (USA) (this is IMET contribution number IMET 19-005).

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Authors and Affiliations

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

    Rosario Barone & Valentina Di Felice

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

    Rosario Barone, Valentina Di Felice & Alberto J. L. Macario

  3. Department of Anatomical, Histological, Forensic & Orthopaedic Sciences, Section of Histology & Medical Embryology, Sapienza University of Rome, Rome, Italy

    Dario Coletti

  4. Sorbonne University, B2A Biological Adaptation and Aging, Paris, France

    Dario Coletti

  5. School of Medicine, Department of Microbiology and Immunology, University of Maryland at Baltimore-Institute of Marine and Environmental Technology (IMET), Columbus Center, Baltimore, MD, USA

    Alberto J. L. Macario

Authors
  1. Rosario Barone
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  2. Valentina Di Felice
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  3. Dario Coletti
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  4. Alberto J. L. Macario
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Editor information

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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Barone, R., Di Felice, V., Coletti, D., Macario, A.J.L. (2019). Hsp60 in Skeletal Muscle: From Molecular Anatomy to Pathophysiology. 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_17

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