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At least 19 recordsLinked to original sources

PubMed1979

Mechanical efficiency of fast- and slow-twitch muscle fibers in man during cycling.

The influence of different percentages of slow-twitch (ST) and fast-twitch (FT) fibers in vastus lateralis on delta efficiency expressed by delta work (x)/delta energy liberation (y) in y = a + bx was studied in six subjects during cycling on an ergometer at 60 or 100 rpm at work loads below 80% of VO2max. Three subjects had an average of 78% ST fibers (ST group) and the other subjects had an average of 76% FT fibers (FT group). There was no difference between the two groups in delta efficiency at 60 rpm, but at 100 rpm the efficiency of the ST group was significantly lower than that of the FT group (19.6 vs. 28.8%, P less than 0.01). In the ST group respiratory exchange ratio (R) was higher at 100 rpm than at 60 rpm, but the FT group had similar R values at both pedal revolution rates. The most important finding was the reduced efficiency when pedaling frequency was increased from 60 to 100 rpm in the ST group (23.3 to 19.6%). Predominant use of ST fibers at rapid pedal rates may require a substantial increase in energy expenditure.

Adult↗

PubMed1977

Morphological and histochemical organization of the flexor carpi radialis muscle in the cat.

Most studies concerning the structure and function of skeletal muscle have utilized the hind limb of the experimental animal. However, it has been shown that the number of behavioral tasks performed by the cat's forelimb is greater than that of the hind limb. In addition, the forelimb muscles exhibit a functional complexity not observed in hind-limb musculature. The purpose of this study was to investigate the distribution of fast-twitch and slow-twitch muscle fibers and muscle spindles in the flexor carpi radialis muscle (FCR) and to correlate the distributional patterns in these structures with muscle tendon architecture and muscle function. It was found that the FCR, a wrist flexor, contains 37% slow-twitch fibers and 63% fast-twitch fibers. However, the slow-twitch fibers were concentrated in the deep region located between the tendons of origin and insertion, while the fast-twitch-glycolytic fibers were concentrated more peripherally. Muscle spindles were associated with the slow-twitch region and were never found in the region containing high concentrations of fast-twitch-glycolytic fibers. Fast-twitch-oxidative-glycolytic fibers were uniformly distributed throughout the muscle. It is proposed that the association of muscle spindles with slow-twitch fibers and the differential distribution of muscle fibers into slow-twitch and fast-twitch regions might allow these regions to function independently of one another when called upon to perform complex behavioral tasks.

Adenosine Triphosphatases↗

PubMed1976

Enzymatic changes in hypertrophied fast-twitch skeletal muscle.

Fast-twitch plantaris muscles of female rats were subjected to unilateral compensatory overload, induced by partial excision of synergistic muscles. One group of rats remained sedentary whereas another was subjected to a supplemental program of treadmill exercise consisting of walking 3 m/min, 65% grade, 2 h/day, 5 days/week. Groups of rats were sacrificed after 1, 2, 4, and 8 weeks and their muscles were weighed and analyzed for protein, citrate synthase, phosphofructokinase (PFK) and myofibril ATPase. Absolute and relative (muscle weight/body weight) muscle weights were much greater in both overloaded groups as compared to contralateral controls. However, treadmill exercise also increased the absolute and relative muscle mass of control plantaris muscles in the exercising group as compared tonormal sedentary contralateral controls. Citrate synthase activity was decreased in overloaded, sedentary muscles as compared to contralateral controls, but after 8 weeks of exercise, it returned to normal levels. PFK was decreased in both sedentary and exercised overloaded muscles throughout the 8 week period. Myofibril ATPase showed a tendency to be reduced in sedentary, overloaded muscles, and was significantly reduced in overloaded, exercising muscles. These results collectively suggest that certain fibers of overloaded fast-patterns take on similar in certain aspects to that normally seen in differentiated slow-twitch muscle fibers.

Adenosine Triphosphatases↗

PubMed1978

Cellular adaptations of the ventilatory muscles to a chronic increased respiratory load.

It is not known whether cellular adaptations of the ventilatory muscles are induced by increased respiratory loads. A chronic respiratory load was produced in rats by tracheal banding. Five weeks after the imposition of this increased load, biochemical and histochemical analyses were performed on the diaphragm and intercostal muscles. The oxidative capacity, as indicated by succinate dehydrogenase (SDH) activity, increased 38% in the diaphragm. The capacity for beta-oxidation fatty acids, as indicated by 3-hydroxy-acyl-CoA dehydrogenase (HADH) activity, increased 29%. The glycolytic capacity, as indicated by phosphofructokinase (PFK) activity, did not change. Similar enzymatic adaptations were observed in the intercostal muscles. The proportion of slow-twitch muscle fibers, as indicated by the myofibrillar adenosine triphosphatase (ATPase) stain, increased in the diaphragm, but not in the intercostal muscles. Thus, these ventilatory muscles responded with an increase in their oxidative capacity, and the diaphragm reponded with an increase in the proportion of muscle fibers having the myofibriller ATPase staining characteristic of slow-twich fibers. We conclude that cellular adaptations are induced in the ventilatory muscles by chronic increased respiratory loads.

3-Hydroxyacyl CoA Dehydrogenases↗

PubMed1975

Histochemical properties of skeletal muscle fibers in streptozotocin-diabetic rats.

The response of rat gastrocnemius muscle fibers to chronic streptozotocindiabetes was studied. Transverse sections of this muscle from normal and diabetic rats were histochemically assayed for reduced diphosphopyridine nucleotide-diaphorase, myofibrillar adenosine triphosphatase, mitochondrial alpha-glycerophosphate dehydrogenase, beta-hydroxybutyrate dehydrogenase, and alkaline phosphatase activities. Cross-sectional areas of the fiber types were measured, and fiber capillarization and populations estimated. Chemically-induced diabetes appeared to have little effect on the metabolic or morphological properties of slow-twitch fibers. However, a general dedifferentiation occurred in the 2 fast-twitch fiber populations. There was a loss of oxidative potential in the fast-twitch-oxidative-glycolytic fibers, and a significant decrease in size in the fast-twitch-glycolytic fibers. No change in the proportions of slow- and fast-twitch fibers in the muscles of diabetic rats occurred. It is concluded that hypoinsulinism has differential effects on the 3 fiber types in heterogeneous rat skeletal muscle, and that slow-twitch fibers are least affected by the diabetic condition.

Adenosine Triphosphatases↗

PubMed1976

Decay of succinate dehydrogenase activity in rat skeletal muscle following streptozotocin injection.

Succinate dehydrogenase activities of 4 skeletal muscles with widely divergent fiber compositions were determined in rats that recieved either 70 or 80 mg streptozotocin per kg body wt at various time intervals following injection. Enzyme activities in all muscles declined to a lower final level and exhibited a more rapid decay in animals receiving the larger dosage. White gastrocnemius muscle, which contains no slow-twitch fibers, experienced the greatest relative loss of activity, and soleus muscle, possessing the highest proportion of slow-twitch fibers, the smallest loss. The findings indicate that extrapancreatic effects of the drug may have been partially responsible for the differential effects of the 2 dosages on the muscles.

Animals↗

PubMed1975

Isometric training of young rats--effects upon hind limb muscles. Histochemical, morphometric, and electron microscopic studies.

The soleus, rectus femoris, and gastrocnemius muscles of young rats trained isometrically for 4 weeks were studied by light and electron microscopy.--The percentage of fast-twitch oxidative muscle fibers decreased at the cost of the fast-twitch glycolytic fibers in the rectus femoris muscle. The percentages of the slow-twitch oxidative fibers did not change significantly in any of the muscles studied. The changes in the areas of the muscle fibers were specific for the muscle and the fiber type and indicate geometrical rearrangements of the fibers in the trained muscles. The Z and M lines were broader in the soleus (containing about 85% slow-twitch oxidative fibers) than in the rectus femoris muscle (containing about 90% fast-twitch glycolytic fibers), while the sarcomere length and the pseudo-H zone were similar. The length of the myosin filaments appeared to be slightly shorter in the fast rectus femoris than in the slow soleus muscle.--The hypothesis on the temporal progress of muscle adaptation to training (Müller, 1974) was substantiated. Correlations between biochemical (Exner et al., 1973a) and histochemical parameters measuring the oxidative capacity were preserved during adaptation to training. The comparison of the histochemical results with the physiological data on similar animals (Exner et al., 1973a) suggests a complex relationship between the contraction time and the percentage of fast-twitch muscle fibers.

Adaptation, Physiological↗

PubMed1979

Distribution of myosin isoenzymes among skeletal muscle fiber types.

Using an immunocytochemical approach, we have demonstrated a preferential distribution of myosin isoenzymes with respect to the pattern of fiber types in skeletal muscles of the rat. In an earlier study, we had shown that fluorescein-labeled antibody against "white" myosin from the chicken pectoralis stained all the white, intermediate and about half the red fibers of the rat diaphragm, a fast-twitch muscle (Gauthier and Lowey, 1977). We have now extended this study to include antibodies prepared against the "head" (S1) and "rod" portions of myosin, as well as the alkali- and 5,5'dithiobis (2-nitrobenzoic acid) (DTNB)-light chains. Antibodies capable of distinguishing between alkali 1 and alkali 2 type myosin were also used to localize these isoenzymes in the same fast muscle. We observed, by both direct and indirect immunofluorescence, that the same fibers which had reacted previously with antibodies against white myosin reacted with antibodies to the proteolytic subfragments and to the low molecular-weight subunits of myosin. These results confirm our earlier conclusion that the myosins of the reactive fibers in rat skeletal muscle are sufficiently similar to share antigenic determinants. The homology, furthermore, is not confined to a limited region of the myosin molecule, but includes the head and rod portions and all classes of light chains. Despite the similarities, some differences exist in the protein compositions of these fibers: antibodies to S1 did not stain the reactive (fast) red fiber as strongly as they did the white and intermediate fibers. Non-uniform staining was also observed with antibodies specific for A2 myosin; the fast red fiber again showed weaker fluorescence than did the other reactive fibers. These results could indicate a variable distribution of myosin isoenzymes according to their alkali-light chain composition among fiber types. Alternatively, there may exist yet another myosin isoenzyme which is localized in the fast red fiber. Those red fibers which did not react with any of the antibodies to pectoralis myosin, did react strongly with an antibody against myosin isolated from the anterior latissimus dorsi (ALD), a slow red muscle of the chicken. The myosin in these fibers (slow red fibers) is, therefore, distinct from the other myosin isoenzymes. In the rat soleus, a slow-twitch muscle, the majority of the fibers reacted only with antibody against ALD myosin. A minority, however, reacted with antiboddies to pectoralis as well as ALD myosin, which indicates that both fast and slow myosin can coexist within the same fiber of a normal adult muscle. These immunocytochemical studies have emphasized that a wide range of isoenzymes may contribute to the characteristic physiological properties of individual fiber types in a mixed muscle.

Adenosine Triphosphatases↗

PubMed1977

In vitro studies of skeletal muscle membranes. Effects of denervation on the macromolecular components of cation transport in red and white skeletal muscle.

The effects of denervation on the macromolecular components of active monovalent cation transport in skeletal muscle have been studied using purified sarcolemma membranes. A comparison of membrane activities of fast-twitch, slow-twitch, and mixed-fiber muscles was made to determine what role, if any, the motor nerve has in regulating this important aspect of muscle metabolism. A dramatic increase in the basal sarcolemmal Mg++ ATPase activity (three- to fourfold) was found for both major muscle types. An increase in the ouabain-inhibitable (Na+ + K+)-stimulated enzyme was also found, but the effect was substantially less (1.5- to twofold). [3H]-ouabain binding, as an index of glycoside receptor sites, also increased (two- to threefold) midway in the course of denervation. On the other hand, the phosphorylated intermediate activity, a functional component of the transport system, clearly decreased over the same time course and remained below control values for the remainder of the course. This resulted in a two- to threefold increase in the turnover number, suggesting that active transport of cations should increase dramatically with denervation. The membrane protein patterns on SDS gels were less obvious than the changes observed in the functional components. The major effects appeared after only one week and seemed to be restricted to high molecular weight membrane proteins, especially in the 100,000 to 250,000 daltons range. This effect was more prominent in slow-twitch membranes with an apparent semiquantitative decrease in stain at 240,000 daltons. In gels of membranes from fast-twitch muscles a decreased stain in the range of 100,000 to 110,000 daltons occurred, and this became more obvious with longer periods of denervation. The results suggest that considerable influence on the macromolecular components of active cation transport in skeletal muscle is exerted by the motor nerve. No appreciable difference was found in this effect when the two major types of skeletal muscle, fast-twitch and slow-twitch, were compared, suggesting that motor nerve regulation of this membrane property is qualitatively the same.

Adenosine Triphosphatases↗

PubMedDate not supplied

Morphology and physiology of skeletal muscle in aging rodents.

Aging in the rodent is accompanied by a progressive loss of skeletal muscle fibers. The muscle twitch also becomes slower, probably as a result of fiber-type conversion from "fast-twitch" to "slow-twitch." The loss of muscle fibers precedes signs of obvious weakness and appears to involve the loss of entire functioning motor units. In the mouse, this loss of motor units correlated with a loss of axons from the innervating nerve trunks.

Adenosine Triphosphatases↗

PubMed1977

Polymorphism of myosin among skeletal muscle fiber types.

An immunocytochemical approach was used to localize myosin with respect to individual fibers in rat skeletal muscle. Transverse cryostat sections of rat diaphragm, a fast-twitch muscle, were exposed to fluorescein-labeled immunoglobulin against purified chicken pectoralis myosin. Fluorescence microscopy revealed a differential response among fiber types, identified on the basis of mitochondrial content. All white and intermediate fiber but only about half of the red fiber reacted with his antimyosin. In addition, an alkali-stable ATPase had the same pattern of distribution among fibers, which is consistent with the existence of two categories of red fibers. The positive response of certain red fibers indicates either that their myosin has antigenic determinants in common with "white" myosin, or that the immunogen contained a "red" myosin. Myosin, extracted from a small region of the pectorlis which consists entirely of white fibers, was used to prepare an immunoadsorbent column to isolate antibodies specific for white myosin. This purified anti-white myosin reacted with the same fibers of the rat diaphragm that had reacted with the white, intermediate, and some red fibers are sufficiently homologous to share antigenic determinants. In a slow-twitch muscle, the soleus, only a minority of the fiber reacted with antipectoralis myosin. The majority failed to respond; hence, they are not equivalent to intermediate fibers of the diaphragm; despite their intermediate mitochondrial content. Immunocytochemical analysis of two different musles of the rat has demonstrated that more than one isoenzyme of myosin can exist in a single muscle, and that individual fiber types can be recognized by immunological differences in their myosin. We conclude that, in the rat diaphragm, there are at least two immunochemically distinct types of myosin and four types of muscle fibers: white, intermediate, and two red. We suggest that these fibers correspond to the four types of motor units described by Burke et al. (Burke, R. E., D. N. Levine, P. Tsairis, and F. E. Zajac, III 1973. J. Physiol. (Lond) 234:723-748.)in the cat gastrocnemius.;

Adenosine Triphosphatases↗

PubMed1978

Developmental pattern of muscle fiber types in human ventilatory muscles.

Premature infants tolerate respiratory loads poorly. This may reflect incomplete development of the ventilatory muscles (VM) causing poor resistance to fatigue. To study the developmental pattern of human VM, 31 postmortem specimens of diaphragm and intercostal muscles were obtained. Individual muscle fibers were classified as type I (slow-twitch, high-oxidative) or type II (fast-twich, low-oxidative) using histochemical staining methods for myofibrillar adenosine triphosphatase (M-ATPase) (pH 10.30) and nicotinamide adenine dinucleotide (NADH) tetrazolium reductase. In the diaphragm, premature infants (less than 37 wk gestation) had only 9.7 +/- 1.3% type I fibers, full-term newborns 25.0 +/- 1.1%, and older subjects (greater than 2 yr of age) 54.9 +/- 1.3%. There was no further increase after 8 mo postpartum. In the intercostal muscles, premature infants had only 19.0 +/- 4.8% type I fibers, full-term newborns 45.7 +/- 1.3%, and older subjects 65.2 +/- 2.6%. There was no further increase after 2 mo postpartum. These findings suggest the ventilatory muscles of newborn infants are more susceptible to fatigue than those of older subjects. This may contribute significantly to respiratory problems in the neonate.

Adenosine Triphosphatases↗

PubMed1977

Compensatory hypertrophy of skeletal muscle fibers in streptozotocin-diabetic rats.

Previous studies have demonstrated an apparent differential response of the fiber types in mixed skeletal muscles of rats to streptozotocin diabetes. The purpose of the present study was to examine the ability of the different fiber types to hypertrophy in muscles from diabetic rats, which should further clarify the apparent differential trophic influence of insulin on the fibers. One group of rats was injected with streptozotocin to induce diabetes. The gastrocnemius muscle was then removed from one hindlimb of rats of both the diabetic and a second, normal group, resulting in compensatory growth of ipsilateral plantaris muscle. Rats were sacrificed 60 days following the surgery. Experimental muscles in normal and diabetic rats enlarged 79% and 61% over control muscles, respectively. In normal hypertrophied muscles there was an 8% increase in relative cross-sectional area composed of slow-twitch fibers, whereas in diabetic rats the slow-twitch component increased 17%. The results indicate that slow-twitch fibers in diabetic rats were capable of responding to the chronic power overloaded condition, but that the fast-twitch fibers had a reduced capacity to undergo compensatory growth. These findings support our previous observations suggesting that insulin may exert a differential trophic effect upon the muscle fiber types.

Animals↗

PubMed1979

Torque-velocity relationships and muscle fiber composition in elite female athletes.

The relationship between the predominance of fast and slow muscle fibers of the vastus lateralis and "in vivo" torque velocity properties in 22 female athletes was studied. Fiber types were classified according to the histochemical myofibrillar adenosine triphosphatase technique at a basic pH. Maximal extensor troques were recorded at 30 degrees from full extension at four selected velocities. While results confirm earlier reports on muscle fiber type and performance, an additional finding was that as knee extension velocities increased from 0 to 95 degrees/s angle specific extensor torque production did not decline as seen in in vitro muscle preparations. The difference in extensor torque between 0 and 96 degrees/s appeared far more critical than the differences observed between 96 and 288 degrees/s. Significant differences in torque were seen at 96, 192, and 288 degrees/s in thos with greater than 50% and less than 50% slow-twitch fibers. When expressed per kilogram of body weight the subjects with greater than 50% fast-twitch fiber produced the greatest torque at 192 degrees/s. These results suggest that the velocity at which torque begins to decline in vivo is related to the proportion of slow-twitch fibers in the vastus lateralismuscle.

Adolescent↗

PubMed1977

Muscle fiber types in women athletes and non-athletes.

Muscle biopsies were obtained from the vastus lateralis muscle of 5 female collegiate field hockey players and 5 untrained female students. The fibers were classified histochemically as fast-twitch-oxidative-glycolytic (FOG), fast-twitch-glycolytic (FG) and slow-twitch-oxidative (SO). The fibers were found to be similar to those of males in distribution and histochemical properties, but were smaller. In the women athletes all 3 fiber types were larger than the respective fibers in the controls. Also, the athletes had a much higher percentage of oxidative fibers (SO + FOG), 83% vs. 46%. A direct relationship between fiber size and oxidative activity was observed in fast-twitch fibers, whereas the reverse was found in slow-twitch fibers.

Adenosine Triphosphatases↗

PubMed1977

Time course adaptations in cardiac and skeletal muscle to different running programs.

The effects of chronic "steady-state" and high-speed interval running were investigated on time-course changes in certain biochemical properties of cardiac and skeletal muscle fiber types of rats. Nine weeks of the interval program resulted in significant increased (15%) in both cardiac enlargement and ATPase activity of myofibrils; whereas increases in these parameters were only transient and not significant at the termination of the program involving steady-state running. Neither program induced appreciable alterations in citrate synthase and phosphofructokinase activity in cardiac muscle. In fast-twitch white fibers, "steady-state" training induced only a transient 45% increase in citrate synthase activity in contrast to a progressive twofold change with interval training. Both programs resulted in similar increases (45-50%) in citrate synthase activity in fast-twitch and slow-twitch red fibers. However, the patterns of increase for both fiber types differed between the two programs. These findings suggest that training programs incorporating elements of both "steady-state" incline and high-speed interval running can potentially induce respiratory enzyme adaptations in the greatest spectrum of rodent skeletal muscle fibers in addition to inducing adaptations to enhance contractile potential in cardiac muscle.

Adenosine Triphosphatases↗

PubMedDate not supplied

Experimental autoimmune myasthenia gravis in the rat: a preliminary report.

In chronic experimental myasthenia gravis (EAMG) in rat, the decrement of electrical and mechanical responses evoked by maximal repetitive (3-167/sec) stimuli to the nerve was greater in the slow-twitch soleus (SOL) than in the fast-twitch extensor digitorum longus (EDL) muscle. Excitation-contraction coupling was impaired in moderate to severe EAMG, as evidenced by a diminished staircase phenomenon and by diminished posttetanic potentiation (PTP) of twitch tension in two EDLs. The only morphologic abnormality observed was an increase in length of the endplates in the EDLs of those animals that had had an acute phase of EAMG. The latter had more than a 90% reduction in the amplitude of the action potential and in the twitch tension of the EDL when stimuli were applied to the nerve. Stimuli applied directly to the muscle evoked a tetanic tension that was one-third of normal. The staircase and PTP were normal. Necrosis occurred in the endplate and in the adjacent segment of muscle fiber; outside the endplate region, the muscle fiber was normal.

Animals↗

PubMed1979

Localization of sarcoplasmic reticulum proteins in rat skeletal muscle by immunofluorescence.

Ca++-Mg++-dependent ATPase and calsequestrin, the major intrinsic and extrinsic proteins, respectively, of the sarcoplasmic reticulum, were localized in cryostat sections of adult rat skeletal muscle by immunofluorescent staining and phase-contrast microscopy. Relatively high concentrations of both the ATPase and calsequestrin were found in fast-twitch myofibers while a very low concentration of the ATPase and a moderate concentration of calsequestrin were found in slow-twitch myofibers. These findings are consistent with previous biochemical studies of the isolated sarcoplasmic reticulum of slow-twitch and fast-twitch mammalian muscles. The distribution of the ATPase in muscle fibers is distinctly different from that of calsequestrin. While calsequestrin is present only near the interface between the I- and A-band regions of the sarcomere, the ATPase is found throughout the I-band region as well as in the center of the A-band region. In comparing these results with in situ ultrastructural studies of the distribution of sarcoplasmic reticulum in fast-twitch muscle, it appears that the ATPase is rather uniformly distributed throughout the sarcoplasmic reticulum while calsequestrin is almost exclusively confined to those regions of the membrane system which correspond to terminal cisternae. Fluorescent staining with these antisera was not observed in vascular smooth muscle cells present in the cryostat sections of the mammalian skeletal muscle used in this study.

Animals↗