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AbstractWe employed counterweighted single‐leg cycling as a unique model to investigate the role of exercise intensity in human skeletal muscle remodelling. Ten young active men performed unilateral graded‐exercise tests to measure single‐leg and peak power ( W peak). Each leg was randomly assigned to complete six sessions of high‐intensity interval training (HIIT) 4 × (5 min at 65% W peak and 2.5 min at 20% W peak) or moderate‐intensity continuous training (MICT) (30 min at 50% W peak), which were performed 10 min apart on each day, in an alternating order. The work performed per session was matched for MICT (143 ± 8.4 kJ) and HIIT (144 ± 8.5 kJ, P 0.05).
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Post‐training, citrate synthase (CS) maximal activity (10.2 ± 0.8 vs. 8.4 ± 0.9 mmol kg protein −1 min −1) and mass‐specific pmol O 2.(s.mg wet weight) −1 oxidative phosphorylation capacities (complex I: 23.4 ± 3.2 vs. 17.1 ± 2.8; complexes I and II: 58.2 ± 7.5 vs. 42.2 ± 5.3) were greater in HIIT relative to MICT (interaction effects, P 0.05). In whole muscle, the protein content of COXIV (24%), NDUFA9 (11%) and mitofusin 2 (MFN2) (16%) increased similarly across groups (training effects, P 0.05).
Single‐leg was also unaffected by training ( P 0.05). In summary, single‐leg cycling performed in an interval compared to a continuous manner elicited superior mitochondrial adaptations in human skeletal muscle despite equal total work. IntroductionSkeletal muscle mitochondrial content impacts fuel use and endurance capacity (Holloszy and Coyle, ), as well as aspects of metabolic health and ageing (Joseph et al.; Goodpaster, ).
Mitochondrial content increases after aerobic‐based exercise training (Holloszy,; Morgan et al. ) and is markedly greater in the skeletal muscle of endurance‐trained compared to untrained individuals (Hoppeler et al.; Jacobs and Lundby, ). Short‐term training programmes, involving moderate‐ to vigorous‐intensity exercise and performed in a continuous or intermittent manner, rapidly increase mitochondrial content in untrained humans (Saltin et al.; MacDougall et al.; Talanian et al.; Burgomaster et al. Relatively few studies have compared work‐matched programmes that differ in exercise intensity, and the precise role of exercise intensity in mediating mitochondrial adaptations to training in humans is equivocal (Bishop et al. ).Exercise intensity mediates many acute responses to aerobic exercise, with higher intensities typically inducing greater neuromuscular fatigue (Theurel and Lepers, ), greater type II muscle fibre recruitment (Kristensen et al. ) and augmenting the activation of molecular pathways linked to mitochondrial biogenesis (Egan et al.; Di Donato et al.; Kristensen et al. Skeletal muscle adaptations to exercise training may therefore be linked to relative work intensity, although surprisingly few data are available to directly address this hypothesis.
High‐intensity interval training (HIIT) and sprint interval training (SIT) elicit adaptations similar to moderate‐intensity continuous training (MICT) despite lower total work (Gibala et al.; Burgomaster et al. ); however, the few studies that have compared MICT, HIIT and/or SIT protocols matched for total work have yielded inconsistent findings, with higher exercise intensities eliciting greater adaptations in some comparisons (Daussin et al.; Granata et al. ) but not others (Henriksson and Reitman,; Saltin et al.; Granata et al. Most training studies have exclusively examined adaptations in whole muscle; however, training‐induced mitochondrial adaptations might occur in a fibre type‐dependent manner (Henriksson and Reitman, ). For example, relative to continuous exercise, the greater AMP‐kinase activity induced by a single bout of interval exercise was also fibre type‐dependent (Kristensen et al. ) and, in response to 6 weeks of MICT, type II fibres demonstrated greater increases in mitochondrial volume than type I fibres (Howald et al. Furthermore, most of the previous studies have progressively increased the duration and/or intensity of the exercise training, complicating any interpretation of the results.
Accordingly, an examination of the short‐term effect of aerobic exercise intensity on human skeletal muscle mitochondrial content is warranted.Single‐leg cycling permits the comparison of training adaptations to two different exercise training protocols within the same subject, controlling for individual variability in training responsiveness and increasing statistical power. The addition of a counterweight to the contralateral pedal assists with the upstroke phase of the revolution, making the perceptual ‘feel’ of counterweighted single‐leg cycling similar to double‐legged cycling (Burns et al.; Bini et al. Gis training courses maine. There is no evidence to suggest that mitochondrial adaptations to single‐leg cycling transfer to the non‐exercising leg, meaning that the contralateral limb can be trained in a different manner or serve as a non‐exercise control (Saltin et al.; Henriksson, ).
Furthermore, the adaptations induced by single‐leg cycling are potentially greater than those induced by double‐legged cycling, as a result of increased relative workloads (Abbiss et al. ).The present study aimed to compare mitochondrial adaptations in human skeletal muscle following six sessions of HIIT or MICT, matched for total work and session duration. The legs of subjects were randomly assigned to one of the two training interventions and exercised separately but consecutively on six training sessions over a 2 week period. Resting skeletal muscle needle biopsies were collected from each leg before and after training to measure mitochondrial content.
We hypothesized that HIIT would elicit greater mitochondrial adaptations than MICT as a result of the cumulative effect of greater metabolic stress induced over the course of the training sessions. Training interventionAll training was performed on the same cycle ergometer adapted for single‐leg cycling as that used for baseline testing.
Using an allocation concealment procedure, each leg was randomly assigned to complete six sessions of work‐ and duration‐matched HIIT or MICT over 2 weeks (essentially every second day). Training began 3–4 days after the muscle biopsy procedures.Exercise prescriptions were based on the average W peak obtained during the two single‐leg tests. Legs in the HIIT group performed four 5 min bouts of cycling at 65% average W peak, each followed by a 2.5 min recovery period at 20% of average W peak.
Legs in the MICT group performed 30 min of cycling at 50% W peak to match the total work total work (kJ) = average power (W) × time (s)/1000 of the HIIT group. For two subjects who could not complete the prescribed HIIT protocol, the loads were reduced to 60% and 15% of average W peak for HIIT and 45% of average W peak for MICT. All training sessions were preceded by a 5 min warm‐up at 25 W.
Subjects were instructed to cycle at the same cadence (∼80 rpm) throughout each session. The legs of each subject were trained consecutively on the same day, following a 10 min rest period, with the order alternating each day. Training intensities were held constant for the entire study.To determine acute responses to each protocol, heart rate was measured continuously (Polar Electro, Kempele, Finland) and ratings of perceived exertion and dyspnoea were measured periodically (Borg Category‐Ratio Scale, 0–10). Heart rate data were averaged for the entire session and for each of the 5 min intervals (or the corresponding period of the MICT protocol), whereas subjective ratings of exertion and dyspnoea were recorded following each interval (or the corresponding period of the MICT protocol). Blood lactate was measured via finger prick during the final 2 min of the first session of each training programme only (Lactate Plus; Nova Biomedical, Mississauga, ON, Canada). Citrate synthase (CS) maximal activityOne piece of muscle was homogenized for the determination of CS maximal activity.
Briefly, ∼25 mg of muscle was homogenized in 20 volumes of buffer (70 m m sucrose, 220 m m mannitol, 10 m m Hepes and 1 m m EGTA, supplemented with protease inhibitors; Complete Mini®; Roche Applied Science, Laval, PQ, Canada) using Lysing Matrix D tubes (MP Biomedicals, Solon, OH, USA) and the FastPrep‐24 Tissue and Cell Homogenizer (MP Biomedicals). Enzyme activity was determined by measuring the formation of the thionitrobenzoate anion at a wavelength of 412 nm using a spectrophotometer (Cary Bio‐300; Varion, Inc., Palo Alto, CA, USA), as previously described (Carter et al. CS maximal activity was expressed relative to total protein measured with a BCA Assay Kit (Pierce, Rockford, IL, USA). Mitochondrial respiration in permeabilized muscle fibresMitochondrial respiration was simultaneously measured in permeabilized muscle from the left and right legs of subjects using the two chambers of an Oxygraph‐2K respirometer (Oroboros, Innsbruck, Austria). The protocol is based on the general protocol described by Pesta and Gnaiger ( ). After being sectioned from the biopsy sample, ∼10 mg of muscle tissue was immediately placed in ice‐cold biopsy preservation solution (BIOPS) (10 m m Ca‐EGTA buffer, 0.1 μ m free calcium, 20 m m imidazole, 20 m m taurine, 50 m m K‐MES, 0.5 m m DTT, 6.56 m m MgCl 2, 5.77 m m ATP and 15 m m phosphocreatine, pH 7.1).
Within 1 h of the biopsy procedure, bundles of muscle fibres were suspended in an aliquot of BIOPS and mechanically separated under a microscope using jeweler's forceps. Samples were then transferred to BIOPS containing saponin (50 μg ml −1) and incubated on a rocker at 4°C for 30 min to permeabilize muscle fibres. Samples were then transferred to ice‐cold mitochondrial respiration medium (MiR05; 0.5 m m EGTA, 3 m m MgCl 2.6H 20, 60 m m K‐lactobionate, 20 m m taurine, 10 m m KH 2PO 4, 20 m m Hepes, 110 m m sucrose and 1 g l −1 bovine serum albumin, pH 7.1) and washed on a rocker at 4°C for 15 min. Finally, samples were blotted dry with filter paper, and a piece of muscle, with a wet weight of between 1.5 and 2 mg (1.8 ± 0.2 mg), was added to the chamber of the respirometer, which contained 2 ml of MiR05 with blebbistatin to inhibit contractions.
All measurements were performed at 37°C and at an oxygen concentration between 100 and 200 nmol ml −1.A substrate uncoupler inhibitor titration protocol was used to examine mitochondrial respiration in permeabilized fibres. First, malate (2 m m) and glutamate (10 m m) were added consecutively in the absence of ADP to measure leak respiration. ADP (5 m m) was added to measure oxidative phosphorylation (oxidative phosphorylation capacity; P) through complex I (P CI) followed by succinate (10 m m) to measure oxidative phosphorylation through complexes I and II (P CI&CII).
The electron transfer system capacity ( E) was assessed through the serial addition of 1 μl aliquots (in steps of 0.5 μ m) of the protonophore, carbonyl cyanide p‐(trifluoromethoxy) phenyl‐hydrazone. The addition of rotenone (0.5 μ m), an inhibitor of complex I, allowed for the measurement of E CII. Cytochrome c (10 μ m) was then added to ensure the functional integrity of the outer mitochondrial membrane and, finally, anti‐mycin A (2.5 μ m), which is an inhibitor of complex III, was added to measure the residual oxygen consumption that remains when electron flow through complexes I, II, and III is inhibited.For analysis of mitochondrial respiration, oxygen flux ( J O2) was calculated from the derivative of the oxygen concentration of the chamber, using DatLab 4.1.08 (Oroboros) and expressed as mass‐specific J O2 (pmol O 2.s.mg wet weight −1).
All values were corrected by subtracting the corresponding residual oxygen consumption value for the sample. To address the possibility that exercise training can increase J O2 independent of mitochondrial content, J O2 was normalized to CS activity (pmol O 2.s.CS −1) to yield mitochondria‐specific J O2 (Jacobs and Lundby,; Jacobs et al. Data are reported for P CI, P CI&CII and E. Whole muscle western blottingFrozen pieces of whole muscle (12 ± 5.0 mg) were cut into 10 μm sections at –20°C, placed in loading buffer, vortexed, incubated at room temperature for 1 h and frozen at –80°C until analysis.
All samples were run on 4–15% Criterion TGX Stain‐Free protein gels (BioRad, Hercules, CA, USA) at 200 V for 45 min. A protein ladder (Fermentas PageRuler Prestained Ladder, ThermoFisher Scientific, Waltham, MA, USA) and a calibration curve (e.g. 2, 4, 8, 16 μl) (Fig. ) of pooled whole muscle homogenates were run on every gel. The total protein loaded was visualized using ultraviolet (UV) activation of the gel and analysed with Image Lab 5.2.1 (Bio‐Rad, Hercules, CA, USA). Proteins were then wet‐transferred to nitrocellulose at 100 V for 30 min in circulating 4°C transfer buffer (25 m m Tris, 192 m m glycine, 0.1% SDS and 20% methanol, pH 8.3). Proper transfer was visualized with UV activation of the gel and membrane post‐transfer (StainFree Imager; Bio‐Rad).
Membranes were treated with Miser solution (Pierce) and placed in blocking buffer (5% skim milk in Tris‐buffered saline‐Tween; TBST) for 2 h at room temperature. After rinsing in TBST, sections of membranes were placed in solutions of primary antibodies (see below) and then incubated for 2 h at room temperature and overnight at 4°C on rockers. After washing in blocking buffer, membranes were incubated in goat anti‐mouse IgG HRP secondary antibody (PIE31430; dilution 1:20 000 in blocking buffer; ThermoFisher Scientific) or goat anti‐rabbit IgG HRP (PIE31460; dilution 1:60 000 in blocking buffer; ThermoFisher Scientific) for 1 h at room temperature. Following a final wash in TBST, membranes were exposed to Supersignal West Femto (Pierce), imaged (ChemiDoc MP; Bio‐Rad) and analysed (ImageLab, version 5.2.1; Bio‐Rad).
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When required, membranes were washed in TBST for 1 h (but were not stripped) before being re‐probed with another primary antibody. The abundance of proteins of interest were normalized to total protein for analysis, using the calibration curve from each gel (Mollica et al.
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