Journal article
Calpain and caspase-3 play required roles in immobilization-induced limb muscle atrophy
Journal of applied physiology (1985), Vol.114(10), pp.1482-1489
05/01/2013
DOI: 10.1152/japplphysiol.00925.2012
PMID: 23471945
Abstract
Prolonged skeletal muscle inactivity results in a rapid decrease in fiber size, primarily due to accelerated proteolysis. Although several proteases are known to contribute to disuse muscle atrophy, the ubiquitin proteasome system is often considered the most important proteolytic system during many conditions that promote muscle wasting. Emerging evidence suggests that calpain and caspase-3 may also play key roles in inactivity-induced atrophy of respiratory muscles, but it remains unknown if these proteases are essential for disuse atrophy in limb skeletal muscles. Therefore, we tested the hypothesis that activation of both calpain and caspase-3 is required for locomotor muscle atrophy induced by hindlimb immobilization. Seven days of immobilization (i.e., limb casting) promoted significant atrophy in type I muscle fibers of the rat soleus muscle. Independent pharmacological inhibition of calpain or caspase-3 prevented this casting-induced atrophy. Interestingly, inhibition of calpain activity also prevented caspase-3 activation, and, conversely, inhibition of caspase-3 prevented calpain activation. These findings indicate that a regulatory cross talk exists between these proteases and provide the first evidence that the activation of calpain and caspase-3 is required for inactivity-induced limb muscle atrophy.
Details
- Title: Subtitle
- Calpain and caspase-3 play required roles in immobilization-induced limb muscle atrophy
- Creators
- Erin E. Talbert - University of FloridaAshley J. Smuder - University of FloridaKisuk Min - University of FloridaOh Sung Kwon - University of FloridaScott K. Powers - University of Florida
- Resource Type
- Journal article
- Publication Details
- Journal of applied physiology (1985), Vol.114(10), pp.1482-1489
- Publisher
- Amer Physiological Soc
- DOI
- 10.1152/japplphysiol.00925.2012
- PMID
- 23471945
- ISSN
- 8750-7587
- eISSN
- 1522-1601
- Number of pages
- 8
- Language
- English
- Date published
- 05/01/2013
- Academic Unit
- Fraternal Order of Eagles Diabetes Research Center; Health and Human Physiology; Internal Medicine
- Record Identifier
- 9984259640302771
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