Exercise‐induced HSP27, HSP70 and MAPK responses in human skeletal muscle

Thompson, H. S.; Maynard, Elizabeth; Morales, Ever; Scordilis, Stylianos P.

doi:10.1046/j.1365-201x.2003.01112.x

Cited by 117 publications

(114 citation statements)

References 48 publications

(160 reference statements)

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“…An increased amount of HSP27 and HSP70 on both the mRNA and protein level after eccentric exercise has been found by others (47,48,50). We found increased mRNA levels of HSP27 and ␣B-crystallin, but our data do not support a substantial increase in protein levels of HSP27.…”

Section: Discussioncontrasting

confidence: 56%

“…In support of this assumption, we found increased protein levels of HSP70 in the days after exercise and a positive correlation between reduced force-generating capacity immediately after exercise and the increased HSP70 levels. Thus, with increasing initial damage, correspondingly more HSP70 for refolding of denatured proteins and for correct folding of newly synthesized proteins is required (36,46,48). The increased amount of HSP70 molecules found in the myofibrillar fraction at 96 h after exercise could indicate that HSP70 play a role in the assembly and incorporation of new proteins in the myofibrillar framework.…”

Section: Discussionmentioning

confidence: 99%

“…Increased mRNA and protein levels of HSP27, HSP70, and ubiquitin in human skeletal muscle after high-force eccentric exercise have been reported in recent studies (6,7,42,(47)(48)(49)(50)57), with the interpretation that the HSPs seem to be involved in remodeling and adaptation processes after high-force exercise (6,48). In contrast to HSP27 and ␣B-crystallin, an acute HSP70 response is also seen after nondamaging, aerobic exercise protocols (20,33).…”

mentioning

confidence: 95%

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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: Discussioncontrasting

confidence: 56%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 95%

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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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“…156,157 However, a significant effect of exercise on HSP70 protein expression in human skeletal muscle has been observed as early as 8 h post exercise 158 and expression remains elevated up to 7 d after exercise termination. [158][159][160][161][162][163][164][165][166] When examining exercise training effects on HSP70 protein expression in humans, it has been shown that a 7-d heat acclimation protocol consisting of 2 50-min exercise bouts in a warm environmental chamber elevates subjects' core temperature to 39 C and results in a significant increase in HSP70 protein expression in peripheral leukocytes at 4-h post-exercise. 144 Similarly, a 10-d acclimation program involving treadmill walking or running in a hot environment augments HSP70 content in peripheral blood mononuclear cells.…”

Section: Exercise and Hsp70 Protein Expression In Animalsmentioning

confidence: 99%

Heat shock response and autophagy—cooperation and control

2015

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Abbreviations: AKT, v-akt murine thymoma viral oncogene homolog 1; AMPK, adenosine monophosphate-activated protein kinase; ATG, autophagy-related; BECN1, Beclin 1, autophagy related; EIF4EBP1, eukaryotic translation initiation factor 4E binding protein 1; ER, endoplasmic reticulum; FOXO, forkhead box O; HSF1, heat shock transcription factor 1; HSP, heat shock protein; HSPA8/ HSC70, heat shock 70kDa protein 8; IL, interleukin; LC3, MAP1LC3, microtubule-associated protein 1 light chain 3; MTMR14/ hJumpy, myotubularin related protein 14; MTOR, mechanistic target of rapamycin; NR1D1/Rev-Erb-a, nuclear receptor subfamily 1, group D, member 1; PBMC, peripheral blood mononuclear cell; PPARGC1A/PGC-1a, peroxisome proliferator-activated receptor, gamma, coactivator 1 a; RHEB, Ras homolog enriched in brain; SOD, superoxide dismutase; SQSTM1/p62, sequestosome 1; TPR, translocated promoter region, nuclear basket protein; TSC, tuberous sclerosis complex; ULK1, unc-51 like autophagy activating kinase 1.Protein quality control (proteostasis) depends on constant protein degradation and resynthesis, and is essential for proper homeostasis in systems from single cells to whole organisms. Cells possess several mechanisms and processes to maintain proteostasis. At one end of the spectrum, the heat shock proteins modulate protein folding and repair. At the other end, the proteasome and autophagy as well as other lysosome-dependent systems, function in the degradation of dysfunctional proteins. In this review, we examine how these systems interact to maintain proteostasis. Both the direct cellular data on heat shock control over autophagy and the time course of exercise-associated changes in humans support the model that heat shock response and autophagy are tightly linked. Studying the links between exercise stress and molecular control of proteostasis provides evidence that the heat shock response and autophagy coordinate and undergo sequential activation and downregulation, and that this is essential for proper proteostasis in eukaryotic systems.

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“…Resistance 3 x 10 @ 70% 1-RM 1) H-CHO 2) L-CHO ERK-P 1) 120% 2) 120% p90 RSK-P 1) 290% 2) 550% Resistance 4 x 10 @ 80% 1-RM 1) BCAA 2) water ERK-P -700% p38-P -400% (no effect with BCAA) Nielsen et al (2003) Cycle 20 min @ 80% VO 2peak 1) Sed 2) Trained ERK-A 1) 40% 2) 38% p38-P 1) 1000% 2) 950% Thompson et al (2003) 1) 50 eccentric contractions 2) 30 min -10% downhill treadmill ERK-P 1) 200% 2) -53% ERK-T 1) 424% 2) no change Thong et al (2003) 60 min 1-leg kicks (alt 5 min @ 75 & 100% PWC) p38-P up 40% compared with rest leg Williamson et al (2003) Resistance 3 x 10 (KE) @ 70% 1-RM 1) old 2) young ERK-P 1) -48% 2) 75% p90-P 1) -60% 2) 100% p38-P 1) -17% 2) 18%…”

Section: Creer Et Al (2005)mentioning

confidence: 99%