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Potential Cytoprotective Effects of Heat Shock Proteins to Skeletal Muscle
Book chapter

Potential Cytoprotective Effects of Heat Shock Proteins to Skeletal Muscle

John P. Vardiman, Philip M. Gallagher and Jacob A. Siedlik
Heat Shock Protein-Based Therapies, pp.119-127
Heat Shock Proteins, volume 9, Springer Nature
01/01/2015
DOI: https://doi.org/10.1007/978-3-319-17211-8_7
Web of Science ID: WOS:000376969800008

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Abstract

Heat shock proteins (HSP) are chaperone molecules that are known to facilitate protein synthesis, protein assembly, provide cellular protection and regulate intracellular signaling. These cytoprotective effects have been linked to increases in HSP70 and HSP27p concentrations but there has been little progress in determining the specific role of HSP in human skeletal muscle adaptations. Short wave diathermy (SWD) and ultrasound are treatments commonly used to stimulate deep heat increases in skeletal muscle with limited research examining the effects of increased muscle temperature on muscle damage induced injury severity. Current research cannot definitively identify the mechanistic roles of HSP in mitigation of muscle damage even though they are commonly cited as mechanism of action for prevention of damage in heat-treated muscle. This article will examine the role of HSP induction in skeletal muscle as a therapeutic countermeasure for reduction of muscle atrophy during prolonged periods of immobilization as well as mechanisms for accelerated repair of injured muscle fibers through increased total protein concentrations.

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