Overexpression of inducible 70-kDa heat shock protein in mouse improves structural and functional recovery of skeletal muscles from atrophy
- 6 March 2012
- journal article
- research article
- Published by Springer Science and Business Media LLC in Pflügers Archiv - European Journal of Physiology
- Vol. 463 (5), 733-741
- https://doi.org/10.1007/s00424-012-1087-x
Abstract
Heat shock proteins play a key regulatory role in cellular defense. To investigate the role of the inducible 70-kDa heat shock protein (HSP70) in skeletal muscle atrophy and subsequent recovery, soleus (SOL) and extensor digitorum longus (EDL) muscles from overexpressing HSP70 transgenic mice were immobilized for 7 days and subsequently released from immobilization and evaluated after 7 days. Histological analysis showed that there was a decrease in cross-sectional area of type II myofiber from EDL and types I and II myofiber from SOL muscles at 7-day immobilization in both wild-type and HSP70 mice. At 7-day recovery, EDL and SOL myofibers from HSP70 mice, but not from wild-type mice, recovered their size. Muscle tetanic contraction decreased only in SOL muscles from wild-type mice at both 7-day immobilization and 7-day recovery; however, it was unaltered in the respective groups from HSP70 mice. Although no effect in a fatigue protocol was observed among groups, we noticed a better contractile performance of EDL muscles from overexpressing HSP70 groups as compared to their matched wild-type groups. The number of NCAM positive-satellite cells reduced after immobilization and recovery in both EDL and SOL muscles from wild-type mice, but it was unchanged in the muscles from HSP70 mice. These results suggest that HSP70 improves structural and functional recovery of skeletal muscle after disuse atrophy, and this effect might be associated with preservation of satellite cell amount.Keywords
This publication has 48 references indexed in Scilit:
- Overexpression of HSP10 in skeletal muscle of transgenic mice prevents the age-related fall in maximum tetanic force generation and muscle cross-sectional areaAmerican Journal of Physiology-Regulatory, Integrative and Comparative Physiology, 2010
- Effect of xanthine oxidase-generated extracellular superoxide on skeletal muscle force generationAmerican Journal of Physiology-Regulatory, Integrative and Comparative Physiology, 2010
- FOXO signaling is required for disuse muscle atrophy and is directly regulated by Hsp70American Journal of Physiology-Cell Physiology, 2010
- Rehabilitation in the Intensive Care UnitSeminars in Respiratory and Critical Care Medicine, 2009
- Hsp27 inhibits IKKβ‐induced NF‐κΕ activity and skeletal muscle atrophyThe FASEB Journal, 2009
- Hsp70 prevents disuse muscle atrophy in senescent ratsBiogerontology, 2008
- Radicicol activates heat shock protein expression and cardioprotection in neonatal rat cardiomyocytesAmerican Journal of Physiology-Heart and Circulatory Physiology, 2004
- POSSIBLE RELATIONSHIP BETWEEN HEAT SHOCK PROTEIN 70, CARDIAC HEMODYNAMICS, AND SURVIVAL IN THE EARLY PERIOD AFTER HEART TRANSPLANTATION1Transplantation, 1998
- Overexpression of the rat inducible 70-kD heat stress protein in a transgenic mouse increases the resistance of the heart to ischemic injury.JCI Insight, 1995
- THE HEAT-SHOCK PROTEINSAnnual Review of Genetics, 1988