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Hsp60 in Skeletal Muscle: From Molecular Anatomy to Pathophysiology

  • Rosario Barone
  • Valentina Di Felice
  • Dario Coletti
  • Alberto J. L. Macario
Chapter
Part of the Heat Shock Proteins book series (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.

Keywords

Atrophy Chaperonopathies Dystrophy Exercise Hsp60 Myosin heavy chain Skeletal muscle 

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

Notes

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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Copyright information

© Springer Nature Switzerland AG 2019

Authors and Affiliations

  • Rosario Barone
    • 1
    • 2
  • Valentina Di Felice
    • 1
    • 2
  • Dario Coletti
    • 3
    • 4
  • Alberto J. L. Macario
    • 2
    • 5
  1. 1.Department of Biomedicine, Neurosciences and Advanced Diagnostics (BiND)University of PalermoPalermoItaly
  2. 2.Euro-Mediterranean Institute of Science and Technology (IEMEST)PalermoItaly
  3. 3.Department of Anatomical, Histological, Forensic & Orthopaedic Sciences, Section of Histology & Medical EmbryologySapienza University of RomeRomeItaly
  4. 4.Sorbonne University, B2A Biological Adaptation and AgingParisFrance
  5. 5.School of Medicine, Department of Microbiology and ImmunologyUniversity of Maryland at Baltimore-Institute of Marine and Environmental Technology (IMET), Columbus CenterBaltimoreUSA

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