Time course and differential responses of the major heat shock protein families in human skeletal muscle following acute nondamaging treadmill exercise

Abstract

The exercise-induced expression of heat shock proteins (HSPs) in rodent models is relatively well defined. In contrast, comparable data from human studies are limited and the exercise-induced stress response of human skeletal muscle is far from understood. This study has characterized the time course and magnitude of the HSP response in the skeletal muscles of a healthy active, but untrained, young male population following a running exercise protocol. Eight subjects performed 45 min of treadmill running at a speed corresponding to their lactate threshold (11.7 +/- 0.5 km/h; 69.8 +/- 4.8% maximum O2 uptake). Muscle biopsies were obtained from the vastus lateralis muscle immediately before and at 24 h, 48 h, 72 h, and 7 days postexercise. Exercise induced a significant (P < 0.05) but variable increase in HSP70, heat shock cognate (HSC) 70, and HSP60 expression with peak increases (typically occurring at 48 h postexercise) to 210, 170, and 139% of preexercise levels, respectively. In contrast, exercise did not induce a significant increase in either HSP27, alphaB-crystallin, SOD 2 (MnSOD) protein content, or the activity of SOD and catalase. When examining baseline protein levels, HSC70, HSP27, and alphaB-crystallin appeared consistently expressed between subjects, whereas HSP70 and MnSOD displayed marked individual variation of up to 3- and 1.5-fold, respectively. These data are the first to define the time course and extent of HSP production in human skeletal muscle following a moderately demanding and nondamaging running exercise protocol. Data demonstrate a differential effect of aerobic exercise on specific HSPs.

Heat shock response and autophagy—cooperation and control

“…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.…”

Fatiguing stimulation of one skeletal muscle triggers heat shock proteins activation in several rat organs: the role of muscle innervation

“…The exercise-induced expression of heat shock proteins (HSPs) in skeletal muscle is well documented in rodents (Huey et al, 2010;Locke et al, 1990;McArdle et al, 2001;Skidmore et al, 1995) and also humans (Morton et al, 2006;Paulsen et al, 2007;Tupling et al, 2007). Plasma HSP levels also increase after static (BrerroSaby et al, 2010) and dynamic exercise ) in healthy subjects.…”

Influences of temperature, oxidative stress, and phosphorylation on binding of heat shock proteins in skeletal muscle fibers

“…oxidation; stress response; skinned fiber; chaperones HEAT SHOCK PROTEINS (HSPs) are highly conserved and ubiquitously expressed proteins that act as protein chaperones and in stress situations bind and interact with various proteins to help preserve or restore their function (23,32). A great deal of work in skeletal muscle has focused on the increase in HSP protein and/or mRNA expression levels occurring in hours to days after various stressful stimuli, such as eccentric exercise (11,17,26,27,39), oxidative stress (50), heat (4,35), and glycogen depletion (12). The present study focuses instead on the acute responses of HSPs to stresses, examining the effects of heat, contraction, and oxidative stress on the distribution and binding of three important HSPs present in rat skeletal muscle fibers, namely ␣B-crystallin, HSP25 (also known as HSP27), and HSP72 (also known as HSP70).…”