Publication:
Autophagy-lysosomal signaling responses to heat stress in tenotomy-induced rat skeletal muscle atrophy

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Issued Date

2021

Resource Type

Article

Language

eng

File Type

application/pdf

ISSN

243205

DOI

10.1016/j.lfs.2021.119352

Other identifier(s)

2-s2.0-85104900034

Rights Holder(s)

มหาวิทยาลัยศรีนครินทรวิโรฒ

Bibliographic Citation

Life Sciences. Vol 275, No. (2021)

Suggested Citation

Hirunsai M., Srikuea R. Autophagy-lysosomal signaling responses to heat stress in tenotomy-induced rat skeletal muscle atrophy. Life Sciences. Vol 275, No. (2021). doi:10.1016/j.lfs.2021.119352 Retrieved from: https://hdl.handle.net/20.500.14740/7233

Title

Autophagy-lysosomal signaling responses to heat stress in tenotomy-induced rat skeletal muscle atrophy

Author(s)

Hirunsai M.
 Srikuea R.

Abstract

Aims: The autophagy-lysosomal system plays a crucial role in maintaining muscle proteostasis. Excessive stimulation of the autophagic machinery is a major contributor to muscle atrophy induced by tendon transection. Hyperthermia is known to attenuate muscle protein loss during disuse conditions; however, little is known regarding the response of the autophagy pathway to heat stress following tenotomy-induced muscle atrophy. The purpose of this study was to evaluate whether heat stress would have a beneficial impact on the activation of autophagy in tenotomized soleus and plantaris muscles. Main methods: Male Wistar rats were divided into control, control plus heat stress, tenotomy, and tenotomy plus heat stress groups. The effects of tenotomy were evaluated at 8 and 14 days with heat treatment applied using thermal blankets (30 min. day−1, at 40.5–41.5 °C, for 7 days). Key findings: Heat stress could normalize tenotomy-induced muscle loss and over-activation of autophagy-lysosomal signaling; this effect was evidently observed in soleus muscle tenotomized for 14 days. The autophagy-related proteins LC3B-II and LC3B-II/I tended to decrease, and lysosomal cathepsin L protein expression was significantly suppressed. While p62/SQSTM1 was not altered in response to intermittent heat exposure in tenotomized soleus muscle at day 14. Phosphorylation of the 4E-BP1 protein was significantly increased in tenotomized plantaris muscle; whereas heat stress had no impact on phosphorylation of Akt and FoxO3a proteins in both tenotomized muscles examined. Significance: Our results provide evidence that heat stress associated attenuation of tenotomy-induced muscle atrophy is mediated through limiting over-activation of the autophagy-lysosomal pathway in oxidative and glycolytic muscles. © 2021

Subject(s)

Cathepsin L
 Initiation factor 4E binding protein 1
 Protein kinase B
 Sequestosome 1
 Transcription factor FKHRL1
 Myosin heavy chain
 Animal cell
 Animal experiment
 Animal model
 Animal tissue
 Article
 Autophagy (cellular)
 Cell activation
 Controlled study
 Evaluation study
 Heat stress
 Heat treatment
 Light chain
 Lysosome
 Male
 Muscle atrophy
 Nonhuman
 Oxidative stress
 Plantaris muscle
 Protein expression
 Protein phosphorylation
 Rat
 Signal transduction
 Skeletal muscle
 Soleus muscle
 Tenotomy
 Thermal exposure
 Upregulation
 Wistar rat
 Achilles tendon
 Adverse event
 Animal
 Autophagy
 Heat shock response
 Human
 Lysosome
 Metabolism
 Muscle atrophy
 Pathophysiology
 Physiology
 Polyacrylamide gel electrophoresis
 Signal transduction
 Surgery
 Tenotomy
 Achilles Tendon
 Animals
 Autophagy
 Electrophoresis, Polyacrylamide Gel
 Heat-Shock Response
 Humans
 Lysosomes
 Male
 Muscular Atrophy
 Myosin Heavy Chains
 Rats
 Rats, Wistar
 Signal Transduction
 Tenotomy

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URI

https://hdl.handle.net/20.500.14740/7233

Collections

Scopus: Year 1983-2021

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