Expression of the stress proteins, ubiquitin, heat shock protein 72, and myofibrillar protein content after 12 weeks of leg cycling in persons with spinal cord injury

Willoughby, Darryn S.; Priest, Joe W.; Nelson, Matt

doi:10.1053/apmr.2002.31184

Cited by 34 publications

(27 citation statements)

References 31 publications

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“…Noteworthy, several different genes for HSP70 exist (25), but our probe only recognizes HSP70A (HSP70-1) and HSP70C (HSP70-2), collectively referred to as HSP72. These isoforms have, however, repeatedly been reported to undergo the regulation in skeletal muscle in response to exercise (27,54,56). Thompson et al (48) measured HSP70A, HSP70B, and HSP70C and found only increased HSP70C in biceps brachii muscle after maximal eccentric exercise, and only HSP70B to be increased in vastus lateralis muscle after downhill running.…”

Section: Discussionmentioning

confidence: 99%

Maximal eccentric exercise induces a rapid accumulation of small heat shock proteins on myofibrils and a delayed HSP70 response in humans

Paulsen¹,

Vissing²,

Kalhovde³

et al. 2007

American Journal of Physiology-Regulatory, Integrative and Comp

135

154

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In this study the stress protein response to unaccustomed maximal eccentric exercise in humans was investigated. Eleven healthy males performed 300 maximal eccentric actions with the quadriceps muscle. Biopsies from vastus lateralis were collected at 30 min and 4, 8, 24, 96, and 168 h after exercise. Cellular regulation and localization of heat shock protein (HSP) 27, αB-crystallin, and HSP70 were analyzed by immunohistochemistry, ELISA technique, and Western blotting. Additionally, mRNA levels of HSP27, αB-crystallin, and HSP70 were quantified by Northern blotting. After exercise (30 min), 81 ± 8% of the myofibers showed strong HSP27 staining ( P < 0.01) that gradually decreased during the following week. αB-Crystallin mimicked the changes observed in HSP27. After exercise (30 min), the ELISA analysis showed a 49 ± 13% reduction of the HSP27 level in the cytosolic fraction ( P < 0.01), whereas Western blotting revealed a 15-fold increase of the HSP27 level in the myofibrillar fraction ( P < 0.01). The cytosolic HSP70 level increased to 203 ± 37% of the control level 24 h after exercise ( P < 0.05). After 4 days, myofibrillar-bound HSP70 had increased ∼10-fold ( P < 0.01) and was accompanied by strong staining on cross sections. mRNA levels of HSP27, αB-crystallin, and HSP70 were all elevated the first day after exercise ( P < 0.01); HSP70 mRNA showed the largest increase (20-fold at 8 h). HSP27 and αB-crystallin seemed to respond immediately to maximal eccentric exercise by binding to cytoskeletal/myofibrillar proteins, probably to function as stabilizers of disrupted myofibrillar structures. Later, mRNA and total HSP protein levels, especially HSP70, increased, indicating that HSPs play a role in skeletal muscle recovery and remodeling/adaptation processes to high-force exercise.

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Section: Discussionmentioning

confidence: 99%

Maximal eccentric exercise induces a rapid accumulation of small heat shock proteins on myofibrils and a delayed HSP70 response in humans

Paulsen¹,

Vissing²,

Kalhovde³

et al. 2007

American Journal of Physiology-Regulatory, Integrative and Comp

135

154

View full text Add to dashboard Cite

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“…To date previous research has only attempted to examine the mechanisms of skeletal muscle wasting in animal tissue [4,5,12] or specific pathological conditions [1,33,39], with no focus being given to a healthy aging population, which comprises a much larger percentage of the older adult population than those with a diagnosed pathological condition. This research examined, for the first time, possible mechanisms of skeletal wasting leading to a decrease in skeletal muscle strength, size, and function that accompanies the aging process.…”

Section: Introductionmentioning

confidence: 99%

Contributions of the ubiquitin–proteasome pathway and apoptosis to human skeletal muscle wasting with age

Whitman

Wacker

Richmond

et al. 2005

Pflugers Arch - Eur J Physiol

145

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The primary mechanism that contributes to decreasing skeletal muscle strength and size with healthy aging is not presently known. This study examined the contribution of the ubiquitin-proteasome pathway and apoptosis to skeletal muscle wasting in older adults (n = 21; mean age = 72.76 +/- 8.31 years) and young controls (n = 21; mean age = 21.48 +/- 2.93 years). Subjects underwent a percutaneous muscle biopsy of the vastus lateralis to determine: (1) ubiquitin ligase gene expression (MAFbx and MuRF1); (2) frequency of apoptosis; and (3) individual fiber type and cross-sectional area. In addition, a whole muscle strength test was also performed. A one-way ANOVA revealed significant increases in the number of positive TUNEL cells in older adults (87%; p < 0.05), although no significant increase in caspase-3/7 activity was detected. Additionally, ubiquitin ligase gene expression, individual muscle fiber type and CSA were not different between old and young subjects. Muscle strength was also significantly lower in old compared to young subjects (p < 0.05). In conclusion, this study indicates a preferential role for apoptosis contributing to decreases in muscle function with age.

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“…16 Heat shock proteins (HSPs), also referred to as stress response proteins, are elevated in skeletal muscle following a single bout of exercise 39 but also after multiple training sessions in animals and humans. 29,35,47 It has been suggested that HSPs are upregulated in response to exercise to protect the muscle cells from damage or decrease protein degradation. Indeed, heat stress prior to ischemia-reperfusion improved the survival of skeletal muscle cells 27 and upregulation of HSP70 by prior heat stress-attenuated muscle atrophy induced by hindlimb unloading.…”

mentioning

confidence: 99%

Exercise‐induced gene expression in soleus muscle is dependent on time after spinal cord injury in rats

et al. 2003

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Cycling exercise attenuates atrophy in hindlimb muscles and causes changes in spinal cord properties after spinal cord injury in rats. We hypothesized that exercising soleus muscle expresses genes that are potentially beneficial to the injured spinal cord. Rats underwent spinal cord injury at T10 and were exercised on a motor-driven bicycle. Soleus muscle and lumbar spinal cord tissue were used for messenger RNA (mRNA) analysis. Gene expression of brain-derived neurotrophic factor (BDNF) and glial cell line-derived neurotrophic factor (GDNF) was elevated 11- and 14-fold, respectively, in soleus muscle after one bout of exercise performed 5 days after spinal cord transection. Also, c-fos and heat shock protein-27 (HSP27) mRNA abundance were increased 11- and 7-fold, respectively. When exercise was started 2 days after the injury, the changes in gene expression were not observed. By contrast, at 2 but not at 5 days after transection, expression of the HSP27 gene was elevated sixfold in the lumbar spinal cord, independent of exercise. Electromyographic activity in soleus muscles was also decreased at 2 days, indicating that the spinal cord was less permissive to exercise at this early time. Long-term exercise for 4 weeks attenuated muscle atrophy equally well in rats started at 2 days or 5 days after injury. We conclude that BDNF and GDNF released from exercising muscle may be involved in exercise-induced plasticity of the spinal cord. Furthermore, the data suggest that the lumbar spinal cord undergoes time-dependent changes that temporarily impede the ability of the muscle to respond to exercise.

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Expression of the stress proteins, ubiquitin, heat shock protein 72, and myofibrillar protein content after 12 weeks of leg cycling in persons with spinal cord injury

Cited by 34 publications

References 31 publications

Maximal eccentric exercise induces a rapid accumulation of small heat shock proteins on myofibrils and a delayed HSP70 response in humans

Maximal eccentric exercise induces a rapid accumulation of small heat shock proteins on myofibrils and a delayed HSP70 response in humans

Contributions of the ubiquitin–proteasome pathway and apoptosis to human skeletal muscle wasting with age

Exercise‐induced gene expression in soleus muscle is dependent on time after spinal cord injury in rats

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