Applied Physiology Nutrition and Metabolism · 2017 · 25 citations · 54 references
Life SciencesEndocrinologyPhysiologyExercise PhysiologyMetabolic RegulationPhysical ActivityAerobic ExerciseMetabolic Adaptation To ExerciseMetabolic Responses To ExerciseMuscle PhysiologyPhysical FitnessStrength TrainingMetabolic Adaptation To TrainingMuscle Oxidative CapacitySkeletal AdaptationsSkeletal Muscle AnatomySkeletal Muscle BioenergeticsSkeletal Muscle Oxidative AdaptationSkeletal Muscle PhysiologySprint Interval Training
The purpose of the present study was to determine if acute responses in PGC-1α, VEGFA, SDHA, and GPD1–2 mRNA expression predict their associated chronic skeletal muscle molecular (SDH–GPD activity and substrate storage) and morphological (fibre-type composition and capillary density) adaptations following training. Skeletal muscle biopsies were collected from 14 recreationally active men (age: 22.0 ± 2.4 years) before (PRE) and 3 h after (3HR) the completion of an acute bout of sprint interval training (SIT) (eight 20-s intervals at ∼170% peak oxygen uptake work rate separated by 10 s of recovery). Participants then completed 6 weeks of SIT 4 times per week with additional biopsies after 2 (MID) and 6 (POST) weeks of training. Acute increases in PGC-1α mRNA strongly predicted increases in SDH activity (a marker of oxidative capacity) from PRE and MID to POST (PRE–POST: r = 0.81, r 2 = 0.65, p < 0.01; MID–POST: r = 0.79, r 2 = 0.62, p < 0.01) and glycogen content from MID to POST (r = 0.60, r 2 = 0.36, p < 0.05). No other significant relationships were found between acute responses in PGC-1α, VEGFA, SDHA, and GPD1–2 mRNA expression and chronic adaptations to training. These results suggest that acute upregulation of PGC-1α mRNA relates to the magnitude of subsequent training-induced increases in oxidative capacity, but not other molecular and morphological chronic skeletal muscle adaptations. Additionally, acute mRNA responses in PGC-1α correlated with VEGFA, but not SDHA, suggesting a coordinated upregulation between PGC-1α and only some of its proposed targets in human skeletal muscle.
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