Non-technical summary A single bout of resistance exercise stimulates the synthesis of new muscle proteins. Chronic performance of resistance exercise (i.e. weight training) is what makes your muscles grow bigger; a process known as hypertrophy. However, it is unknown if increasing the time that muscle is under tension will lead to greater increases in muscle protein synthesis. We report that leg extension exercise at 30% of the best effort (which is a load that is comparatively light), with a slow lifting movement (6 s up and 6 s down) performed to fatigue produces greater increases in rates of muscle protein synthesis than the same movement performed rapidly (1 s up and 1 s down). These results suggest that the time the muscle is under tension during exercise may be important in optimizing muscle growth; this understanding enables us to better prescribe exercise to those wishing to build bigger muscles and/or to prevent muscle loss that occurs with ageing or disease.Abstract We aimed to determine if the time that muscle is under loaded tension during low intensity resistance exercise affects the synthesis of specific muscle protein fractions or phosphorylation of anabolic signalling proteins. Eight men (24 ± 1 years (SEM), BMI = 26.5 ± 1.0 kg m −2 ) performed three sets of unilateral knee extension exercise at 30% of one-repetition maximum strength involving concentric and eccentric actions that were 6 s in duration to failure (SLOW) or a work-matched bout that consisted of concentric and eccentric actions that were 1 s in duration (CTL). Participants ingested 20 g of whey protein immediately after exercise and again at 24 h recovery. Needle biopsies (vastus lateralis) were obtained while fasted at rest and after 6, 24 and 30 h post-exercise in the fed-state following a primed, constant infusion of L-[ring -13 C 6 ]phenylalanine. Myofibrillar protein synthetic rate was higher in the SLOW condition versus CTL after 24-30 h recovery (P < 0.001) and correlated to p70S6K phosphorylation (r = 0.42, P = 0.02). Exercise-induced rates of mitochondrial and sarcoplasmic protein synthesis were elevated by 114% and 77%, respectively, above rest at 0-6 h post-exercise only in the SLOW condition (both P < 0.05). Mitochondrial protein synthesis rates were elevated above rest during 24-30 h recovery in the SLOW (175%) and CTL (126%) conditions (both P < 0.05). Lastly, muscle PGC-1α expression was increased at 6 h post-exercise compared to rest with no difference between conditions (main effect for time, P < 0.001). These data show that greater muscle time under tension increased the acute amplitude of mitochondrial and sarcoplasmic protein synthesis and also resulted in a robust, but delayed stimulation of myofibrillar protein synthesis 24-30 h after resistance exercise.

We aimed to determine if any mechanistic differences exist between a single set (1SET) and multiple sets (i.e. 3 sets; 3SET) of resistance exercise by utilizing a primed constant infusion of [ring-13 C 6 ]phenylalanine to determine myofibrillar protein synthesis (MPS) and Western blot analysis to examine anabolic signalling molecule phosphorylation following an acute bout of resistance exercise. Eight resistance-trained men (24 ± 5 years, BMI = 25 ± 4 kg m −2 ) were randomly assigned to perform unilateral leg extension exercise at 70% concentric one repetition maximum (1RM) until volitional fatigue for 1SET or 3SET. Biopsies from the vastus lateralis were taken in the fasted state (Fast) and fed state (Fed; 20 g of whey protein isolate) at rest, 5 h Fed, 24 h Fast and 29 h Fed post-exercise. Fed-state MPS was transiently elevated above rest at 5 h for 1SET (2.3-fold) and returned to resting levels by 29 h post-exercise. However, the exercise induced increase in MPS following 3SET was superior in amplitude and duration as compared to 1SET at both 5 h (3.1-fold above rest) and 29 h post-exercise (2.3-fold above rest). Phosphorylation of 70 kDa S6 protein kinase (p70S6K) demonstrated a coordinated increase with MPS at 5 h and 29 h post-exercise such that the extent of p70S6K phosphorylation was related to the MPS response (r = 0.338, P = 0.033). Phosphorylation of 90 kDa ribosomal S6 protein kinase (p90RSK) and ribosomal protein S6 (rps6) was similar for 1SET and 3SET at 24 h Fast and 29 h Fed, respectively. However, 3SET induced a greater activation of eukaryotic translation initiation factor 2Bε (eIF2Bε) and rpS6 at 5 h Fed. These data suggest that 3SET of resistance exercise is more anabolic than 1SET and may lead to greater increases in myofibrillar protein accretion over time.

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Muscle fatigue is a temporary decline in the force and power capacity of skeletal muscle resulting from muscle activity. Because control of muscle is realized at the level of the motor unit (MU), it seems important to consider the physiological properties of motor units when attempting to understand and predict muscle fatigue. Therefore, we developed a phenomenological model of motor unit fatigue as a tractable means to predict muscle fatigue for a variety of tasks and to illustrate the individual contractile responses of MUs whose collective action determines the trajectory of changes in muscle force capacity during prolonged activity. An existing MU population model was used to simulate MU firing rates and isometric muscle forces and, to that model, we added fatigue-related changes in MU force, contraction time, and firing rate associated with sustained voluntary contractions. The model accurately estimated endurance times for sustained isometric contractions across a wide range of target levels. In addition, simulations were run for situations that have little experimental precedent to demonstrate the potential utility of the model to predict motor unit fatigue for more complicated, real-world applications. Moreover, the model provided insight into the complex orchestration of MU force contributions during fatigue, that would be unattainable with current experimental approaches.

Quantification of subcellular glycogen in resting human muscle: granule size, number, and location. J Appl Physiol 93: 1598-1607, 2002. First published July 12, 2002 10.1152/ japplphysiol.00585.2001.-A few qualitative investigations suggested that location of muscle glycogen (G) granules in specific sites may be associated with distinct metabolic roles. Similarly, it has been suggested that the acid-soluble and -insoluble G fractions (macro-and proglycogen, respectively) are different metabolic pools and also could exist as separate entities. We employed a transmission electron microscopic technique to quantify subcellular G particle size, number, and location in human vastus lateralis biopsies of 11 resting men. The intra-and interobserver variability for the various measures was generally Ͻ4%. Granule size and number were quantified in subcellular compartments (subsarcolemmal, intra-and intermyofibrillar). Subcellular location was critical: G was more densely concentrated in the subsarcolemmal than in the myofibrillar space, whereas the single-particle volume was greater in the latter. Single-particle diameter ranged from 10 to 44 m and followed a continuous, normal distribution. This implies that proglycogen is not a distinct entity, but rather that pro-and macroglycogen are divisions of smaller and larger molecules. These results demonstrate a compartmentalized pattern of subcellular G deposition in human skeletal muscle for both the size and density of granules.glycosome; metabolic compartments; electron microscopy; carbohydrate; glycogen regulation; proglycogen; macroglycogen SINCE THE DISCOVERY OF GLYCOGEN by Claude Bernard, numerous investigators have addressed many aspects of its metabolism. Although muscle glycogen concentration has been routinely quantified biochemically, the subcellular organization of glycogen particles has been studied much less frequently and only with qualitative, descriptive transmission electron microscopy (TEM) methods. Wanson and Drochmans (31) performed the first comprehensive description of rabbit skeletal muscle glycogen in its particulate ␤-form. Drochmans (5) had previously examined negatively stained liver glycogen by using TEM and described three glycogen structures in liver: ␣-, ␤-, and ␥-particles. The ␣-particles were the typical liver rosettes, and the ␤-particles were the 20-to 30-m spheroid units forming the ␣-rosettes. The ␥-particles were identified as 3-m subunits of both ␣-and ␤-structures. The single ␤-particles described in muscles by Wanson and Drochmans (31) corresponded in size and shape to the ␤-subunits that constituted the ␣-rosettes in liver.Scott and Still (28) proposed that particulate glycogen was not a molecule in the traditional static sense but rather a dynamic organelle. In 1970, Meyer et al. (21) were among the first to suggest that glycogen was complexed with proteins and represented a structural and functional unit of the muscle cells. Using TEM, they estimated the diameter of this glycogen particle to be 20-30 m. This value was in agree...

Fifteen male subjects performed a repetitive elbow flexion/extension task with a 7-kg mass until exhaustion. Average joint angle, angular velocity, and biceps brachii surface electromyographic (EMG) amplitude (aEMG) and mean power frequency (MPF) were calculated with each consecutive 250-ms segment of data during the entire trial. Data were separated into concentric or eccentric phases and into seven 20 degree-ranges from 0 to 140 degrees of elbow flexion. A regression analysis was used to estimate the rested and fatigued aEMG and MPF values. aEMG values were expressed as a percentage of amplitudes from maximum voluntary contractions (MVC). Under rested dynamic conditions, the average concentric aEMG amplitude was 10% MVC higher than average eccentric values. Rested MPF values were similar for concentric and eccentric phases, although values increased approximately 20 Hz from the most extended to flexed joint angles. Fatigue resulted in an average increase in concentric and eccentric aEMG of 35 and 10% MVC, respectively. The largest concentric aEMG increases (up to 58% MVC) were observed at higher joint velocities, whereas eccentric increases appeared to be related to decreases in velocity. Fatigue had a similar effect on MPF during both concentric and eccentric phases. Larger MPF decreases were observed at shorter muscle lengths such that values within each angle range were very similar by the end of the trial. It was hypothesized that this finding may reflect a biological minimum in conduction velocity before propagation failure occurs.

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Few studies have been carried out on the changes in biomechanical loading on low-back tissues during prolonged lifting. The purpose of this paper was to develop a model for continuously estimating erector spinae muscle loads during repetitive lifting and lowering tasks. The model was based on spine kinematics and bilateral lumbar and thoracic erector spinae electromyogram (EMG) signals and was developed with the data from eight male subjects. Each subject performed a series of isometric contractions to develop extensor moments about the low back. Maximum voluntary contractions (MVCs) were used to normalize all recorded EMG and moment time-histories. Ramp contractions were used to determine the non-linear relationship between extensor moments and EMG amplitudes. In addition, the most appropriate low-pass filter cut-off frequencies were calculated for matching the rectified EMG signals with the moment patterns. The mean low-pass cut-off frequency was 2.7 (0.4) Hz. The accuracy of the non-linear EMG-based estimates of isometric extensor moment were tested with data from a series of six rapid contractions by each subject. The mean error over the duration of these contractions was 9.2 (2.6)% MVC. During prolonged lifting sessions of 20 min and of 2 h, a model was used to calculate changes in muscle length based on monitored spine kinematics. EMG signals were first processed according to the parameters determined from the isometric contractions and then further processed to account for the effects of instantaneous muscle length and velocity. Simple EMG estimates were found to underestimate peak loading by 9.1 (4.0) and 25.7 (11.6)% MVC for eccentric and concentric phases of lifting respectively, when compared to load estimates based on the mechanically corrected EMG. To date, the model has been used to analyze over 5300 lifts.