Effect of an acute dose of omega-3 fish oil following exercise-induced muscle damage.

PURPOSE: The purpose of this double-blind, placebo-controlled study was to examine the effect of two fish oil supplements, one high in EPA (750 mg EPA, 50 mg DHA) and one low in EPA (150 mg EPA, 100 mg DHA), taken acutely as a recovery strategy following EIMD. METHODS: Twenty-seven physically active males (26 ± 4 year, 1.77 ± 0.07 m, 80 ± 10 kg) completed 100 plyometric drop jumps to induce muscle damage. Perceptual (perceived soreness) and functional (isokinetic muscle strength at 60° and 180° s-1, squat jump performance and countermovement jump performance) indices of EIMD were recorded before, and 1, 24, 48, 72, and 96h after the damaging protocol. Immediately after the damaging protocol, volunteers ingested either a placebo (Con), a low-EPA fish oil (Low EPA) or a high-EPA fish oil (High EPA) at a dose of 1 g per 10 kg body mass. RESULTS: A significant group main effect was observed for squat jump, with the High EPA group performing better than Con and Low EPA groups (average performance decrement, 2.1, 8.3 and 9.8%, respectively), and similar findings were observed for countermovement jump performance, (average performance decrement, 1.7, 6.8 and 6.8%, respectively, p = 0.07). Significant time, but no interaction main effects were observed for all functional and perceptual indices measured, although large effect sizes demonstrate a possible ameliorating effect of high dose of EPA fish supplementation (effect sizes ≥0.14). CONCLUSION: This study indicates that an acute dose of high-EPA fish oil may ameliorate the functional changes following EIMD.

Effects of reduced-volume of sprint interval training and the time course of physiological and performance adaptations.

This study sought to determine the time course of training adaptations to two different sprint interval training programmes with the same sprint: rest ratio (1:8) but different sprint duration. Nine participants (M: 7; F: 2) were assigned to 15-second training group (15TG) consisting of 4-6 × 15-second sprints interspersed with 2-minute recovery, whereas eight participants (M: 5; F: 3) were assigned to 30-second training group (30TG) consisting of 4-6 × 30 second sprints interspersed with 4-minute recovery. Both groups performed their respective training twice per week over 9 weeks and changes in peak oxygen uptake (V˙O2peak) and time to exhaustion (TTE) were assessed every 3 weeks. Additional eight healthy active adults (M: 6; F: 2) completed the performance assessments 9 weeks apart without performing training (control group, CON). Following 9 weeks of training, both groups improved V˙O2peak (15TG: 12.1%; 30TG: 12.8%, P<.05) and TTE (15TG: 16.2%; 30TG: 12.8%, P<.01) to a similar extent. However, while both groups showed the greatest gains in V˙O2peak at 3 weeks (15TG: 16.6%; 30TG: 17.0%, P<.001), those in TTE were greatest at 9 weeks. CON did not change any of performance variables following 9 weeks. This study demonstrated that while the changes in cardiorespiratory function plateau within several weeks with sprint interval training, endurance capacity (TTE) is more sensitive to such training over a longer time frame in moderately-trained individuals. Furthermore, a 50% reduction in sprint duration does not diminish overall training adaptations over 9 weeks.

Using systems biology to define the essential biological networks responsible for adaptation to endurance exercise training.

We predict that RNA level regulation is as diverse and powerful as protein level regulation when considering physiological adaptation. Non-coding RNA molecules, such as miRNAs (microRNAs), have emerged as a powerful mechanism for post-transcriptional regulation of mRNA. In an effort to define the role of miRNA in human skeletal-muscle biology, we have initiated profiling of muscle RNA before and after endurance exercise training. The robust molecular phenotype of muscle is established using unbiased analysis strategies of the raw data, reflecting the statistical power of gene ontology and network analysis. We can thus determine the structural features of the skeletal-muscle transcriptome, identify discrete networks activated by training and utilize bioinformatics predictions to establish the interaction between non-coding RNA modulation and Affymetrix expression profiles.

Collagen synthesis in human musculoskeletal tissues and skin.

We have developed a direct method for the measurement of human musculoskeletal collagen synthesis on the basis of the incorporation of stable isotope-labeled proline or leucine into protein and have used it to measure the rate of synthesis of collagen in tendon, ligament, muscle, and skin. In postabsorptive, healthy young men (28 +/- 6 yr) synthetic rates for tendon, ligament, muscle, and skin collagen were 0.046 +/- 0.005, 0.040 +/- 0.006, 0.016 +/- 0.002, and 0.037 +/- 0.003%/h, respectively (means +/- SD). In postabsorptive, healthy elderly men (70 +/- 6 yr) the rate of skeletal muscle collagen synthesis is greater than in the young (0.023 +/- 0.002%/h, P < 0.05 vs. young). The rates of synthesis of tendon and ligament collagen are similar to those of mixed skeletal muscle protein in the postabsorptive state, whereas the rate for muscle collagen synthesis is much lower in both young and elderly men. After nutrient provision, collagen synthesis was unaltered in tendon and skeletal muscle, remaining at postabsorptive values (young: tendon, 0.045 +/- 0.008%/h; muscle, 0.016 +/- 0.003%/h; elderly: muscle, 0.024 +/- 0.003%/h). These results demonstrate that the rate of human musculoskeletal tissue collagen synthesis can be directly and robustly measured using stable isotope methodology.

Selective activation of AMPK-PGC-1alpha or PKB-TSC2-mTOR signaling can explain specific adaptive responses to endurance or resistance training-like electrical muscle stimulation.

Endurance training induces a partial fast-to-slow muscle phenotype transformation and mitochondrial biogenesis but no growth. In contrast, resistance training mainly stimulates muscle protein synthesis resulting in hypertrophy. The aim of this study was to identify signaling events that may mediate the specific adaptations to these types of exercise. Isolated rat muscles were electrically stimulated with either high frequency (HFS; 6x10 repetitions of 3 s-bursts at 100 Hz to mimic resistance training) or low frequency (LFS; 3 h at 10 Hz to mimic endurance training). HFS significantly increased myofibrillar and sarcoplasmic protein synthesis 3 h after stimulation 5.3- and 2.7-fold, respectively. LFS had no significant effect on protein synthesis 3 h after stimulation but increased UCP3 mRNA 11.7-fold, whereas HFS had no significant effect on UCP3 mRNA. Only LFS increased AMPK phosphorylation significantly at Thr172 by approximately 2-fold and increased PGC-1alpha protein to 1.3 times of control. LFS had no effect on PKB phosphorylation but reduced TSC2 phosphorylation at Thr1462 and deactivated translational regulators. In contrast, HFS acutely increased phosphorylation of PKB at Ser473 5.3-fold and the phosphorylation of TSC2, mTOR, GSK-3beta at PKB-sensitive sites. HFS also caused a prolonged activation of the translational regulators p70 S6k, 4E-BP1, eIF-2B, and eEF2. These data suggest that a specific signaling response to LFS is a specific activation of the AMPK-PGC-1alpha signaling pathway which may explain some endurance training adaptations. HFS selectively activates the PKB-TSC2-mTOR cascade causing a prolonged activation of translational regulators, which is consistent with increased protein synthesis and muscle growth. We term this behavior the "AMPK-PKB switch." We hypothesize that the AMPK-PKB switch is a mechanism that partially mediates specific adaptations to endurance and resistance training, respectively.

Protein synthesis rates in human muscles: neither anatomical location nor fibre-type composition are major determinants.

In many animals the rate of protein synthesis is higher in slow-twitch, oxidative than fast-twitch, glycolytic muscles. To discover if muscles in the human body also show such differences, we measured [13C]leucine incorporation into proteins of anatomically distinct muscles of markedly different fibre-type composition (vastus lateralis, triceps, soleus) after an overnight fast and during infusion of a mixed amino acid solution (75 mg amino acids kg(-1) h(-1)) in nine healthy, young men. Type-1 fibres contributed 83 +/- 4% (mean +/-s.e.m.) of total fibres in soleus, 59 +/- 3% in vastus lateralis and 22 +/- 2% in triceps. The basal myofibrillar and sarcoplasmic protein fractional synthetic rates (FSR, % h(-1)) were 0.034 +/- 0.001 and 0.064 +/- 0.001 (soleus), 0.031 +/- 0.001 and 0.060 +/- 0.001 (vastus), and 0.027 +/- 0.001 and 0.055 +/- 0.001 (triceps). During amino acid infusion, myofibrillar protein FSR increased to 3-fold, and sarcoplasmic to 2-fold basal values (P < 0.001). The differences between muscles, although significant statistically (triceps versus soleus and vastus lateralis, P < 0.05), were within approximately 15%, biologically probably insignificant. The rates of collagen synthesis were not affected by amino acid infusion and varied by < 5% between muscles and experimental conditions.

Sequential extracts of human bone show differing collagen synthetic rates.

Type I collagen is the major bone protein. Little is known quantitatively about human bone collagen synthesis in vivo, despite its importance for the understanding of bone formation and turnover. Our aim was to develop a method that could be used for the physiological and pathophysiological investigation of human bone collagen synthesis. We have carried out preliminary studies in patients undergoing hip replacement and in pigs to validate the use of the flooding dose method using (13)C- or (15)N-labelled proline and we have now refined our techniques to allow them to be used in a normal clinical or physiological setting. The results show that the application of a flooding dose causes bone free-proline labelling to equilibrate with that of blood in pigs and human beings, so that only 150 mg of bone will provide enough sample to prepare and measure the labelling of three fractions of bone collagen (dissolved in NaCl, acetic acid and pepsin/acetic acid) which have the same relative labelling (1.0:0.43:0.1) as measured by GC-combustion-isotope ratio MS. The rates of incorporation were substantially faster than in skeletal muscle samples taken at the same time. The results suggest that different fractions of human bone collagen turnover at markedly higher rates than had been previously considered. This approach should allow us to discover how growth and development, food, activity and drugs affect bone collagen turnover and to measure the effects on it of ageing and bone disease.