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- Title
SIRT1, AMP-activated protein kinase phosphorylation and downstream kinases in response to a single bout of sprint exercise: influence of glucose ingestion.
- Authors
Guerra, Borja; Guadalupe-Grau, Amelia; Fuentes, Teresa; Ponce-González, Jesús; Morales-Alamo, David; Olmedillas, Hugo; Guillén-Salgado, José; Santana, Alfredo; Calbet, José A. L.; Ponce-González, Jesús Gustavo; Guillén-Salgado, José; Calbet, José A L
- Abstract
This study was designed to examine potential in vivo mechanisms of AMP-activated protein kinase (AMPK) phosphorylation inhibition and its downstream signaling consequences during the recovery period after a single bout of sprint exercise. Sprint exercise induces Thr(172)-AMPK phosphorylation and increased PGC-1alpha mRNA, by an unknown mechanism. Muscle biopsies were obtained in 15 young healthy men in response to a 30-s sprint exercise (Wingate test) randomly distributed into two groups: the fasting (n = 7, C) and the glucose group (n = 8, G), who ingested 75 g of glucose 1 h before exercising to inhibit AMPKalpha phosphorylation. Exercise elicited different patterns of Ser(221)-ACCbeta, Ser(473)-Akt and Thr(642)-AS160 phosphorylation, during the recovery period after glucose ingestion. Thirty minutes after the control sprint, Ser(485)-AMPKalpha1/Ser(491)-AMPKalpha2 phosphorylation was reduced by 33% coinciding with increased Thr(172)-AMPKalpha phosphorylation (both, P < 0.05). Glucose abolished the 30-min Thr(172)-AMPKalpha phosphorylation. Ser(221)-ACCbeta phosphorylation was elevated immediately following and 30 min after exercise in C and G, implying a dissociation between Thr(172)-AMPKalpha and Ser(221)-ACCbeta phosphorylation. Two hours after the sprint, PGC-1alpha protein expression remained unchanged while SIRT1 (its upstream deacetylase) was increased. Glucose ingestion abolished the SIRT1 response without any significant effect on PGC-1alpha protein expression. In conclusion, glucose ingestion prior to a sprint exercise profoundly affects Thr(172)-AMPKalpha phosphorylation and its downstream signaling during the recovery period.
- Subjects
PROTEIN kinases; PHOSPHORYLATION; GLUCOSE; INGESTION; MESSENGER RNA; PROTEIN metabolism; ENZYME metabolism; BIOPSY; BLOOD sugar; CELLULAR signal transduction; COMPARATIVE studies; CONVALESCENCE; CYCLING; EXERCISE; HEAT shock proteins; INSULIN; LACTIC acid; RESEARCH methodology; MEDICAL cooperation; PHOSPHOTRANSFERASES; RESEARCH; TIME; TRANSCRIPTION factors; TRANSFERASES; SERINE; EVALUATION research; QUADRICEPS muscle; THREONINE
- Publication
European Journal of Applied Physiology, 2010, Vol 109, Issue 4, p731
- ISSN
1439-6319
- Publication type
journal article
- DOI
10.1007/s00421-010-1413-y