Hideki Matoba

The muscle fiber composition of skeletal muscle as a predictor of athletic success An overview

Human skeletal muscle is composed of varying percentages of fiber types. This percent composition varies widely between muscles and among individuals. The fiber composition of some skeletal muscle could be construed as being advantageous to successful performance in selected athletic event. However, this relationship is not sufficiently close to warrant the conclusion that the fiber composition of the muscle per se is the determinant of the superior performance of elite athletes. Reasonably good evidence exists to support the position that the fiber composition of a muscle is the result of a genetic endowment. Although muscle fibers are mutable, present evidence is equivocal as to whether habitual participation in given type of physical activity is responsible for high percentages of a given fiber type being present in the muscles of some athletes. Although considerable knowledge has come from the study of muscle samples obtained from sedentary individuals, athletes of a wide range of performance capacity, and individuals before and after training, a considerable gap remains for a full understanding of how the characteristics of muscle are related to performance capacity. The observation that considerable variation exists in the percent distribution of the fibers within a muscle and that athletes with a wide range of fiber populations in their muscles can be successful in the same athletic event cautions against the routine application of the biopsy technique to estimate the fiber distribution of muscles and also to use such data as a routine screening procedure for predicting athletic success. The point, as was made in an earlier paper, that the biopsy technique for studying muscle is a research tool, will probably continue to be true for the near future.

Response of Skeletal Muscle to Training

SummaryPhysical training induces adaptive changes in skeletal muscle. These changes are localised to the active muscle with their magnitude depending upon the nature, i.e. time and intensity, of the training regimen. The most notable changes are increased concen-trations of mitochondria and glycogen.With endurance training there are major changes in metabolism in that there is a greater contribution of fat to the total metabolism during submaximal exercise. This re-sults in a conservation of the stores of glycogen with the net result of increasing total exercise capacity. This increased use of fat during submaximal exercise appears to be more closely related to the elevations in the concentration of mitochondria in muscle than to changes in total body maximal oxygen uptake. The combination of a greater contri-bution of fat to the metabolism and the elevated concentration of stored glycogen are prime factors contributing to the enhanced endurance capacity after endurance training.The mechanism for the greater use of fat after endurance training is discussed. Evi-dence now supports the hypothesis that this is due to a tighter control over the Embden-Meyerhof pathway as a result of the greater concentration of mitochondria. The effect of heavy resistance exercise on the size and strength of skeletal muscle is discussed. Some attention is focused on the recently revived controversy concerning whether muscle en-largement is the result of a hypertrophy of pre-existing fibres or of hyperplasia. It is con-cluded that although there is considerable evidence to support the development of hyper-trophy in response to heavy resistance exercise, the contention that a splitting of fibres occurs to produce a greater fibre number is presently poorly supported.

Changes in myosin heavy chain isoform expression of overloaded rat skeletal muscles.

1. The effect of functional overload produced by tenotomy of synergistic gastrocnemius muscle on the expression of myosin heavy chain (MHC) isoforms in the plantaris and soleus muscles of the rat was studied using gradient sodium dodecyl sulfate-acrylamide gel electrophoresis. 2. Five weeks tenotomy, the plantaris and soleus muscle weights induced by tenotomy of the gastrocnemius muscle were 44.3% (P < 0.005) and 37.4% (P < 0.005), respectively, heavier than the contralateral control muscles. 3. Although four types of MHC isoforms were observed in both control and experimental plantaris, the percentage of MHC isoforms in the control and experimental muscles differed; the hypertrophied plantaris muscle contained more HCI (P < 0.05), HCIIa and HCIId (P < 0.05) and less HCIIb (P < 0.05) than the control muscle. 4. The control soleus muscle contained two MHC isoforms, HCI and HCIIa. However, there was only a single HCI isoform in the hypertrophied soleus muscle. 5. These results indicate that overloading a skeletal muscle by removing its synergists produces not only the muscle hypertrophy but also the changes in the expression of MHC isoforms.

Comparison of fiber types in skeletal muscles from ten animal species based on sensitivity of the myofibrillar actomyosin ATPase to acid or copper

SummaryComparisons were made of the histochemical characteristics of skeletal muscle from 10 animal species. The basic comparison was made from the staining patterns for the myofibrillar actomyosin ATPase produced by preincubation of fresh frozen cross-sections of muscle at alkaline pH (10.30) or acid pH (4.60) with those produced by preincubation in media containing Cu2+ at alkaline pH (10.30), near neutral pH (7.40), or acid pH (4.60). Muscle sections were also stained for reduced nicotinamide adenine dinucleotide tetrazolium reductase and alpha-glycerophosphate dehydrogenase to provide an indication of the relative oxidative and glycolytic capacity of the different fiber types. Type II fibers in mixed fibered muscles were either very sensitive, moderately sensitive, or relatively insensitive to inactivation of the myofibrillar actomyosin ATPase after acid preincubation. These fibers were identified as type IIA1, IIA2, and IIA3, respectively. The myofibrillar actomyosin ATPase of the type I fibers of these muscles, with the exception of those in mouse muscle, was activated by pretreatment with acid. A separation of animal species was possible based on the stability of the IIA1 fibers to inclusion of Cu2+ in the preincubation medium. For one group of animals (rat, mouse, monkey, man, dog, rabbit, and cow), a reciprocal relationship existed between lability to acid and stability to Cu2+ for type IIA1 and IIA3 fibers, respectively. For the second group of animals (horse, ass, and cat) there was a parallel relationship between lability or stability of the type IIA1 and IIA3 fibers to pretreatment with either acid or Cu2+

Influence of ionic composition, buffering agent, and pH on the histochemical demonstration of myofibrillar actomyosin ATPase.

SummaryThe influence of the composition of the preincubation medium on the histochemical demonstration of myofibrillar actomyosin ATPase, including a variety of carboxylic acid and non-carboxylic acid buffering compounds and neutral salts, was studied. In inorganic salt-free systems the rate of the activation of type I fibers and inactivation of type II fibers was accelerated when the carboxylic acids had longer chain length or multiple carobxyl groups. Of these factors, the number of carboxyl groups was dominant with a 100 mM citrate buffer producing a sharp differentiation between fiber types. In contrast, the time course of the response was exceptionally long in an acetate buffer. The time course of the ATPase reaction was also modified by other buffers at pH 4.60. The most notable were an ascorbate — glycine buffer system which produced little or no deviation from the alkaline preincubation staining pattern after prolonged preincubation and a pyrophosphate system which produced a rapid change. Neutral salts in the preincubation medium accelerated the time course of the inactivation — activation process with the order for the halogen salts of K+ being F−<Cl−<Br−<I−, which is a progression by molecular weight. The only sequence for cations on the myofibrillar actomyosin ATPase was Li+< Na+<K+. The response to salts was concentration dependent. An interaction existed between buffering compound, type of salt, and pH. These experiments demonstrate that the histochemical differentiation of fiber types by the myofibrillar actomyosin ATPase reaction depends upon a modification of some component(s) of the myofibrillar complex that can be influenced by a number of factors.

Identification of fiber types in rat skeletal muscle based on the sensitivity of myofibrillar actomyosin ATPase to copper

SummaryExperiments are reported demonstrating that differential rates of inactivation of the histochemical staining for myofibrillar actomyosin ATPase in rat skeletal muscle fibers exist following inclusion of low concentrations of Cu2+ in the preincubation medium. This response of rat muscle occurs at near neutral (7.40), acid (4.60), and alkaline (10.30) pH. The response to Cu2+ appears to result from a binding of Cu2+ onto the myofibrillar complex, probably on myosin itself, as it can be reversed by soaking of the pretreated muscle sections in sodium cyanide or the Cu2+ chelator diethyldithiocarbamate. The pattern of modification of the staining pattern following pretreatment with Cu2+ is the mirror image of that produced by pretreatment with acid. The results demonstrate that the inclusion of Cu2+ in the preincubation media for the myofibrillar actomyosin ATPase can be a useful tool to differentiate fiber types. They also support the earlier conclusion that three distinct types of type II fibers can be identified in rat skeletal muscle based on the histochemical staining for myofibrillar actomyosin ATPase.

Influence of exercise on the fiber composition of skeletal muscle

SummaryBiopsy samples from the vastus lateralis muscle (VLM) of man were examined for fiber composition at rest and at selected intervals during prolonged exercise ranging in intensity from 40% to 75% of the total body maximal oxygen uptake (VO2max) and one-min bouts of exercise at 150%VO2max. Because of the heterogeneity of fibers in human VLM, studies were also completed where the effect of exercise on the fiber composition of the rat soleus muscle (SM) was examined. In some animals the SM from one hindlimb was removed 9 days prior to their being exercised after which the remaining SM was removed. Exercise reduced muscle glycogen in all experiments. In the studies with man, blood lactate exceeded 17 mmoles/l after the heavy exercise but was largely unchanged by endurance exercise. Colonic temperature of the exercised rats exceeded 40° C. In studies where fibers were identified only as type I and type II, type II fibers in the VLM of all samples (16) taken at rest averaged 61.2±12.5% as compared to 59.0±12.0% after exercise (54 biopsy samples). In a second series of studies with man where the subtypes of type II fibers were identified, there were also no differences in fiber composition of the VLM after varying periods of exercise. Glycogen content and percent fiber composition were the same in right and left SM obtained from rested rats. Exercise (30 to 40 min) did not alter the fiber composition of the rat SM. These data demonstrate that the histochemically demonstratable myofibrillar actomyosin ATPase of skeletal muscle is not altered by a single exercise bout.

Does prolonged exercise alter diet-induced thermogenesis ?

Diet-induced thermogenesis (DIT) is mainly an insulin-mediated response and the result of fat and glycogen synthesis. We investigated DIT at rest and after exercise to clarify the mechanism of exercise-induced changes in DIT in 6 healthy men (mean age 36 ± 16 years). Subjects exercised for 1 h at 58% of maximal O2 consumption on a bicycle ergometer and then rested for 8 h sitting in a comfortable chair (exercise experiment). On a different day, subjects rested for 8 h without preceding exercising (non-exercise experiment). At 12.30 h, the subjects were given their second meal. DIT to individual meal did not differ significantly between the exercise and non-exercise days. Increased insulin sensitivity and increased free fatty acid oxidation by exercise may facilitate the conversion of glucose to glycogen in muscle. On the other hand, insulin secretion expressed as the ratio of plasma levels of insulin to glucose after the meal was significantly decreased in the exercise experiment (p < 0.05). Study of heart rate variability showed that sympathetic tone, a primary hormonal determinant of glucose metabolism during exercise, was increased and parasympathetic tone was decreased during the recovery period in the exercise experiment (p < 0.05). These findings suggest that changes in DIT are affected by many factors and may be related to the balance between these counteracting factors.

Vitamin C supplementation does not alter high-intensity endurance training-induced mitochondrial biogenesis in rat epitrochlearis muscle

The purpose of this study was to investigate whether vitamin C supplementation prevents high-intensity intermittent endurance training-induced mitochondrial biogenesis in the skeletal muscle. Male Wistar-strain rats were assigned to one of five groups: a control group, training group, small dose vitamin C supplemented training group, middle dose vitamin C supplemented training group, and large dose vitamin C supplemented training group. The rats of the trained groups were subjected to intense intermittent swimming training. The vitamin C supplemented groups were administrated vitamin C for the pretraining and training periods. High-intensity intermittent swimming training without vitamin C supplementation significantly increased peroxisome proliferator-activated receptor-γ coactivator-1α protein content and citrate synthase activity in the epitrochlearis muscle. The vitamin C supplementation did not alter the training-induced increase of these regardless of the dose of vitamin C supplementation. The results demonstrate that vitamin C supplementation does not prevent high-intensity intermittent training-induced mitochondrial biogenesis in the skeletal muscle.

Myosin light chain patterns in histochemically typed single fibers of the rat skeletal muscle

1. This study was conducted to investigate the relationship between histochemical fiber types and myosin light chain patterns in rat single muscle fibers. 2. The hybrid of fast and slow light chains was observed in type I and II fibers of the soleus and type II fibers of the red portion of lateral head of the gastrocnemius muscles. 3. We also observed 7 types of light chain composition. Of the 7 types, 5 types were explainable by assuming the coexistence of isomyosins with either fast or slow light chains. However, the other 2 types could not be accounted for without hypothesizing the presence of isomyosins with promiscuous light chain distribution.