The effect of exercise-intensity on skeletal muscle stress kinase and insulin protein signaling.
BACKGROUND:Stress and mitogen activated protein kinase (SAPK) signaling play an important role in glucose homeostasis and the physiological adaptation to exercise. However, the effects of acute high-intensity interval exercise (HIIE) and sprint interval exercise (SIE) on activation of these signalin...
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doaj-2ec223d15fda48d6959cdca3147ed1b12020-11-24T22:11:46ZengPublic Library of Science (PLoS)PLoS ONE1932-62032017-01-01122e017161310.1371/journal.pone.0171613The effect of exercise-intensity on skeletal muscle stress kinase and insulin protein signaling.Lewan ParkerAdam TrewinItamar LevingerChristopher S ShawNigel K SteptoBACKGROUND:Stress and mitogen activated protein kinase (SAPK) signaling play an important role in glucose homeostasis and the physiological adaptation to exercise. However, the effects of acute high-intensity interval exercise (HIIE) and sprint interval exercise (SIE) on activation of these signaling pathways are unclear. METHODS:Eight young and recreationally active adults performed a single cycling session of HIIE (5 x 4 minutes at 75% Wmax), SIE (4 x 30 second Wingate sprints), and continuous moderate-intensity exercise work-matched to HIIE (CMIE; 30 minutes at 50% of Wmax), separated by a minimum of 1 week. Skeletal muscle SAPK and insulin protein signaling were measured immediately, and 3 hours after exercise. RESULTS:SIE elicited greater skeletal muscle NF-κB p65 phosphorylation immediately after exercise (SIE: ~40%; HIIE: ~4%; CMIE; ~13%; p < 0.05) compared to HIIE and CMIE. AS160Ser588 phosphorylation decreased immediately after HIIE (~-27%; p < 0.05), and decreased to the greatest extent immediately after SIE (~-60%; p < 0.05). Skeletal muscle JNK (~42%; p < 0.05) and p38 MAPK (~171%; p < 0.05) phosphorylation increased, and skeletal muscle AktSer473 phosphorylation (~-32%; p < 0.05) decreased, to a similar extent immediately after all exercise protocols. AS160Ser588 phosphorylation was similar to baseline three hours after SIE (~-12%; p > 0.05), remained lower 3 hours after HIIE (~-34%; p < 0.05), and decreased 3 hours after CMIE (~-33%; p < 0.05). CONCLUSION:Despite consisting of less total work than CMIE and HIIE, SIE proved to be an effective stimulus for the activation of stress protein kinase signaling pathways linked to exercise-mediated adaptation of skeletal muscle. Furthermore, post-exercise AS160Ser588 phosphorylation decreased in an exercise-intensity and post-exercise time-course dependent manner.http://europepmc.org/articles/PMC5300197?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Lewan Parker Adam Trewin Itamar Levinger Christopher S Shaw Nigel K Stepto |
spellingShingle |
Lewan Parker Adam Trewin Itamar Levinger Christopher S Shaw Nigel K Stepto The effect of exercise-intensity on skeletal muscle stress kinase and insulin protein signaling. PLoS ONE |
author_facet |
Lewan Parker Adam Trewin Itamar Levinger Christopher S Shaw Nigel K Stepto |
author_sort |
Lewan Parker |
title |
The effect of exercise-intensity on skeletal muscle stress kinase and insulin protein signaling. |
title_short |
The effect of exercise-intensity on skeletal muscle stress kinase and insulin protein signaling. |
title_full |
The effect of exercise-intensity on skeletal muscle stress kinase and insulin protein signaling. |
title_fullStr |
The effect of exercise-intensity on skeletal muscle stress kinase and insulin protein signaling. |
title_full_unstemmed |
The effect of exercise-intensity on skeletal muscle stress kinase and insulin protein signaling. |
title_sort |
effect of exercise-intensity on skeletal muscle stress kinase and insulin protein signaling. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS ONE |
issn |
1932-6203 |
publishDate |
2017-01-01 |
description |
BACKGROUND:Stress and mitogen activated protein kinase (SAPK) signaling play an important role in glucose homeostasis and the physiological adaptation to exercise. However, the effects of acute high-intensity interval exercise (HIIE) and sprint interval exercise (SIE) on activation of these signaling pathways are unclear. METHODS:Eight young and recreationally active adults performed a single cycling session of HIIE (5 x 4 minutes at 75% Wmax), SIE (4 x 30 second Wingate sprints), and continuous moderate-intensity exercise work-matched to HIIE (CMIE; 30 minutes at 50% of Wmax), separated by a minimum of 1 week. Skeletal muscle SAPK and insulin protein signaling were measured immediately, and 3 hours after exercise. RESULTS:SIE elicited greater skeletal muscle NF-κB p65 phosphorylation immediately after exercise (SIE: ~40%; HIIE: ~4%; CMIE; ~13%; p < 0.05) compared to HIIE and CMIE. AS160Ser588 phosphorylation decreased immediately after HIIE (~-27%; p < 0.05), and decreased to the greatest extent immediately after SIE (~-60%; p < 0.05). Skeletal muscle JNK (~42%; p < 0.05) and p38 MAPK (~171%; p < 0.05) phosphorylation increased, and skeletal muscle AktSer473 phosphorylation (~-32%; p < 0.05) decreased, to a similar extent immediately after all exercise protocols. AS160Ser588 phosphorylation was similar to baseline three hours after SIE (~-12%; p > 0.05), remained lower 3 hours after HIIE (~-34%; p < 0.05), and decreased 3 hours after CMIE (~-33%; p < 0.05). CONCLUSION:Despite consisting of less total work than CMIE and HIIE, SIE proved to be an effective stimulus for the activation of stress protein kinase signaling pathways linked to exercise-mediated adaptation of skeletal muscle. Furthermore, post-exercise AS160Ser588 phosphorylation decreased in an exercise-intensity and post-exercise time-course dependent manner. |
url |
http://europepmc.org/articles/PMC5300197?pdf=render |
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