| Autor: |
Cuthbert RL; Department of Health and Kinesiology, University of Nebraska, Omaha, NE, USA., Shute RJ; Department of Health and Kinesiology, University of Nebraska, Omaha, NE, USA., Slivka DR; Department of Health and Kinesiology, University of Nebraska, Omaha, NE, USA. |
| Jazyk: |
angličtina |
| Zdroj: |
Temperature (Austin, Tex.) [Temperature (Austin)] 2018 Dec 16; Vol. 6 (1), pp. 77-84. Date of Electronic Publication: 2018 Dec 16 (Print Publication: 2019). |
| DOI: |
10.1080/23328940.2018.1555414 |
| Abstrakt: |
The response of cold shock proteins to exercise and environmental temperature in human skeletal muscle is not known. The purpose of this study was to determine the early mRNA response of human stress proteins to endurance exercise and environmental temperatures. Seven recreationally trained males cycled for 1 hour at 60% VO 2peak in 7°C, 20°C, and 33°C with biopsies taken pre- and 3 hours post-exercise. Gene expression for heat shock and cold shock proteins were analyzed using qRT-PCR on muscle biopsy samples from the vastus lateralis . RBM3 mRNA was reduced 1.43 ± 0.10 fold (p = 0.006) while there was a trend for CIRP to decrease1.27 ± 0.14 fold (p = 0.059) from pre- to 3 h post-exercise. CIRP and RBM3 mRNA were not different between temperatures (p = 0.273 and p = 0.686, respectively). HSP70 mRNA was 2.27 ± 0.23 fold higher 3 h post-exercise when compared to pre-exercise (p = 0.002) but was not significantly different between temperatures (p = 0.103). HSP27, HSP90, and HSF1 mRNA did not change from pre- to post-exercise (p = 0.052, p = 0.324, p = 0.795) and were not different between temperatures (p = 0.247, p = 0.134, p = 0.808). These data indicate that exposure to mild heat and cold during aerobic exercise have limited effect on the skeletal muscle mRNA expression of heat shock and cold shock proteins. However, skeletal muscle mRNA of cold shock proteins decrease, while HSP70 mRNA increases in response to a low to moderate intensity aerobic exercise bout. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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