Skeletal muscle composition in dietary obesity-susceptible and dietary obesity-resistant rats

1992 ◽  
Vol 262 (4) ◽  
pp. R684-R688 ◽  
Author(s):  
J. Abou Mrad ◽  
F. Yakubu ◽  
D. Lin ◽  
J. C. Peters ◽  
J. B. Atkinson ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Fiber ◽  
Gastrocnemius Muscle ◽  
Fiber Type ◽  
Type I ◽  
Total Weight Gain ◽  
Bottom Quartile ◽  
Male Wistar Rats ◽  
Dietary Obesity ◽  
Type I Fibers

The intent of this study was to determine whether a relationship exists between susceptibility to high-fat diet (HFD)-induced obesity and skeletal muscle fiber type. Forty-four adult male Wistar rats were given ad libitum access to a HFD (60% of calories from fat) for 4 wk. Rats were then grouped into quartiles for total weight gain, and the top-quartile [obesity prone (OP)] rats were compared with the bottom-quartile [obesity resistant (OR)] rats. OP rats gained 1.5 times as much weight as OR rats. OR rats had a significantly higher proportion of type I muscle fibers in the medial head of the gastrocnemius muscle than OP rats both before (determined from a muscle biopsy) and after the HFD feeding period. A greater proportion of type I fibers may be associated with a greater capacity for fat oxidation, which would favor resistance to body fat accumulation. Preexisting differences in muscle fiber composition may play a role in determining susceptibility to dietary obesity.

Gene Polymorphisms and Fiber-Type Composition of Human Skeletal Muscle

2012 ◽  
Vol 22 (4) ◽  
pp. 292-303 ◽  
Author(s):  
Ildus I. Ahmetov ◽  
Olga L. Vinogradova ◽  
Alun G. Williams
Keyword(s):  
Skeletal Muscle ◽  
Muscle Fiber ◽  
Human Skeletal Muscle ◽  
Fiber Type ◽  
Vastus Lateralis Muscle ◽  
Type I ◽  
Fiber Types ◽  
Fiber Type Composition ◽  
Type Composition ◽  
Type I Fibers

The ability to perform aerobic or anaerobic exercise varies widely among individuals, partially depending on their muscle-fiber composition. Variability in the proportion of skeletal-muscle fiber types may also explain marked differences in aspects of certain chronic disease states including obesity, insulin resistance, and hypertension. In untrained individuals, the proportion of slow-twitch (Type I) fibers in the vastus lateralis muscle is typically around 50% (range 5–90%), and it is unusual for them to undergo conversion to fast-twitch fibers. It has been suggested that the genetic component for the observed variability in the proportion of Type I fibers in human muscles is on the order of 40–50%, indicating that muscle fiber-type composition is determined by both genotype and environment. This article briefly reviews current progress in the understanding of genetic determinism of fiber-type proportion in human skeletal muscle. Several polymorphisms of genes involved in the calcineurin–NFAT pathway, mitochondrial biogenesis, glucose and lipid metabolism, cytoskeletal function, hypoxia and angiogenesis, and circulatory homeostasis have been associated with fiber-type composition. As muscle is a major contributor to metabolism and physical strength and can readily adapt, it is not surprising that many of these gene variants have been associated with physical performance and athlete status, as well as metabolic and cardiovascular diseases. Genetic variants associated with fiber-type proportions have important implications for our understanding of muscle function in both health and disease.

Capillary and size interrelationships in developing rat diaphragm, EDL, and soleus muscle fiber types

1989 ◽  
Vol 256 (1) ◽  
pp. C50-C58 ◽  
Author(s):  
D. Smith ◽  
H. Green ◽  
J. Thomson ◽  
M. Sharratt
Keyword(s):  
Muscle Fiber ◽  
Time Course ◽  
Fiber Type ◽  
Capillary Density ◽  
Muscle Fiber Types ◽  
Type I ◽  
Fiber Types ◽  
Fiber Area ◽  
Male Wistar Rats ◽  
Type I Fibers

The effects of maturation on the interrelationship between skeletal muscle fiber area and capillarization was investigated in specific fiber types (I, IIa, IIb, IIc) of male Wistar rats at seven developmental periods ranging from 8 to 85 days postnatal. Fiber type specific developmental properties were compared in three different muscles, the diaphragm (DIA), extensor digitorum longus (EDL), and soleus (SOL), which are known to differ widely in function. All fiber types in each of the three muscles examined exhibited large increases in area (FA), the magnitude and time course of the increase being related to both the type of fiber and the muscle in which the fiber was located. For type I fibers, areas increased from 3- to 18-fold (SOL greater than EDL greater than DIA), whereas in type IIa fibers, area increased ranged between 5- to 11-fold (SOL greater than EDL greater than DIA). Growth rates in IIb fibers were more homogeneous between muscles ranging from 11- to 14-fold. Capillarization, as indicated by the capillary contacts per fiber (CC), increased in all fiber types regardless of muscle origin. These increases ranged between 1.7- and 2.2-fold for type I fibers, between 2.4- and 2.5-fold for type IIa fibers, and between 2.0- and 3.0-fold for type IIb fibers. In general, capillary density expressed as the ratio of the number of capillary contacts divided by the fiber area (CC/FA) progressively declined in all fiber types with age. The rate of the decline in CC/FA was mediated in large part by the changes in fiber area.(ABSTRACT TRUNCATED AT 250 WORDS)

Genetic and other determinants of AMP deaminase activity in healthy adult skeletal muscle

1998 ◽  
Vol 85 (4) ◽  
pp. 1273-1278 ◽  
Author(s):  
Barbara Norman ◽  
Donna K. Mahnke-Zizelman ◽  
Amy Vallis ◽  
Richard L. Sabina
Keyword(s):  
Skeletal Muscle ◽  
Enzyme Activity ◽  
Mutant Allele ◽  
Fiber Type ◽  
Type I ◽  
Training Status ◽  
Amp Deaminase ◽  
Normal Allele ◽  
Relative Percentage ◽  
Type I Fibers

AMPD1 genotype, relative fiber type composition, training status, and gender were evaluated as contributing factors to the reported variation in AMP deaminase enzyme activity in healthy skeletal muscle. Multifactorial correlative analyses demonstrate that AMPD1 genotype has the greatest effect on enzyme activity. An AMPD1 mutant allele frequency of 13.7 and a 1.7% incidence of enzyme deficiency was found across 175 healthy subjects. Homozygotes for the AMPD1 normal allele have high enzyme activities, and heterozygotes display intermediate activities. When examined according to genotype, other factors were found to affect variability as follows: AMP deaminase activity in homozygotes for the normal allele exhibits a negative correlation with the relative percentage of type I fibers and training status. Conversely, residual AMP deaminase activity in homozygotes for the mutant allele displays a positive correlation with the relative percentage of type I fibers. Opposing correlations in different homozygous AMPD1 genotypes are likely due to relative fiber-type differences in the expression of AMPD1 and AMPD3 isoforms. Gender also contributes to variation in total skeletal muscle AMP deaminase activity, with normal homozygous and heterozygous women showing only 85–88% of the levels observed in genotype-matched men.

Changes in skeletal muscle biochemistry and histology relative to fiber type in rats with heart failure

1997 ◽  
Vol 83 (4) ◽  
pp. 1291-1299 ◽  
Author(s):  
Michael D. Delp ◽  
Changping Duan ◽  
John P. Mattson ◽  
Timothy I. Musch
Keyword(s):  
Myocardial Infarction ◽  
Heart Failure ◽  
Skeletal Muscle ◽  
Enzyme Activities ◽  
Fiber Type ◽  
Left Ventricular ◽  
Type I ◽  
Fiber Composition ◽  
Muscle Biochemistry ◽  
Type I Fibers

Delp, Michael D., Changping Duan, John P. Mattson, and Timothy I. Musch. Changes in skeletal muscle biochemistry and histology relative to fiber type in rats with heart failure. J. Appl. Physiol. 83(4): 1291–1299, 1997.—One of the primary consequences of left ventricular dysfunction (LVD) after myocardial infarction is a decrement in exercise capacity. Several factors have been hypothesized to account for this decrement, including alterations in skeletal muscle metabolism and aerobic capacity. The purpose of this study was to determine whether LVD-induced alterations in skeletal muscle enzyme activities, fiber composition, and fiber size are 1) generalized in muscles or specific to muscles composed primarily of a given fiber type and 2) related to the severity of the LVD. Female Wistar rats were divided into three groups: sham-operated controls ( n = 13) and rats with moderate ( n = 10) and severe ( n = 7) LVD. LVD was surgically induced by ligating the left main coronary artery and resulted in elevations ( P < 0.05) in left ventricular end-diastolic pressure (sham, 5 ± 1 mmHg; moderate LVD, 11 ± 1 mmHg; severe LVD, 25 ± 1 mmHg). Moderate LVD decreased the activities of phosphofructokinase (PFK) and citrate synthase in one muscle composed of type IIB fibers but did not modify fiber composition or size of any muscle studied. However, severe LVD diminished the activity of enzymes involved in terminal and β-oxidation in muscles composed primarily of type I fibers, type IIA fibers, and type IIB fibers. In addition, severe LVD induced a reduction in the activity of PFK in type IIB muscle, a 10% reduction in the percentage of type IID/X fibers, and a corresponding increase in the portion of type IIB fibers. Atrophy of type I fibers, type IIA fibers, and/or type IIB fibers occurred in soleus and plantaris muscles of rats with severe LVD. These data indicate that rats with severe LVD after myocardial infarction exhibit 1) decrements in mitochondrial enzyme activities independent of muscle fiber composition, 2) a reduction in PFK activity in type IIB muscle, 3) transformation of type IID/X to type IIB fibers, and 4) atrophy of type I, IIA, and IIB fibers.

Carnitine metabolism in human muscle fiber types during submaximal dynamic exercise

1996 ◽  
Vol 80 (3) ◽  
pp. 1061-1064 ◽  
Author(s):  
D. Constantin-Teodosiu ◽  
S. Howell ◽  
P. L. Greenhaff
Keyword(s):  
Muscle Fiber ◽  
Fiber Type ◽  
Vastus Lateralis ◽  
Group Formation ◽  
Free Carnitine ◽  
Muscle Fiber Types ◽  
Type I ◽  
Fiber Types ◽  
Carnitine Metabolism ◽  
Type I Fibers

The effect of prolonged exhaustive exercise on free carnitine and acetylcarnitine concentrations in mixed-fiber skeletal muscle and in type I and II muscle fibers was investigated in humans. Needle biopsy samples were obtained from the vastus lateralis of six subjects immediately after exhaustive one-legged cycling at approximately 75% of maximal O2 uptake from both the exercised and nonexercised (control) legs. In the resting (control) leg, there was no difference in the free carnitine concentration between type I and II fibers (20.36 +/- 1.25 and 20.51 +/- 1.16 mmol/kg dry muscle, respectively) despite the greater potential for fat oxidation in type I fibers. However, the acetylcarnitine concentration was slightly greater in type I fibers (P < 0.01). During exercise, acetylcarnitine accumulation occurred in both muscle fiber types, but accumulation was greatest in type I fibers (P < 0.005). Correspondingly, the concentration of free carnitine was significantly lower in type I fibers at the end of exercise (P < 0.001). The sum of free carnitine and acetylcarnitine concentrations in type I and II fibers at rest was similar and was unchanged by exercise. In conclusion, the findings of the present study support the suggestion that carnitine buffers excess acetyl group formation during exercise and that this occurs in both type I and II fibers. However, the greater accumulation of acetylcarnitine in type I fibers during prolonged exercise probably reflects the greater mitochondrial content of this fiber type.

scholarly journals Overexpression of TRB3 in muscle alters muscle fiber type and improves exercise capacity in mice

2014 ◽  
Vol 306 (12) ◽  
pp. R925-R933 ◽  
Author(s):  
Ding An ◽  
Sarah J. Lessard ◽  
Taro Toyoda ◽  
Min-Young Lee ◽  
Ho-Jin Koh ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Exercise Capacity ◽  
Muscle Fiber ◽  
Wheel Running ◽  
Fiber Type ◽  
Muscle Fiber Type ◽  
Acid Oxidation ◽  
Peroxisome Proliferator ◽  
Type I ◽  
Pronounced Increase

Increasing evidence suggests that TRB3, a mammalian homolog of Drosophila tribbles, plays an important role in cell growth, differentiation, and metabolism. In the liver, TRB3 binds and inhibits Akt activity, whereas in adipocytes, TRB3 upregulates fatty acid oxidation. In cultured muscle cells, TRB3 has been identified as a potential regulator of insulin signaling. However, little is known about the function and regulation of TRB3 in skeletal muscle in vivo. In the current study, we found that 4 wk of voluntary wheel running (6.6 ± 0.4 km/day) increased TRB3 mRNA by 1.6-fold and protein by 2.5-fold in the triceps muscle. Consistent with this finding, muscle-specific transgenic mice that overexpress TRB3 (TG) had a pronounced increase in exercise capacity compared with wild-type (WT) littermates (TG: 1,535 ± 283; WT: 644 ± 67 joules). The increase in exercise capacity in TRB3 TG mice was not associated with changes in glucose uptake or glycogen levels; however, these mice displayed a dramatic shift toward a more oxidative/fatigue-resistant (type I/IIA) muscle fiber type, including threefold more type I fibers in soleus muscles. Skeletal muscle from TRB3 TG mice had significantly decreased PPARα expression, twofold higher levels of miR208b and miR499, and corresponding increases in the myosin heavy chain isoforms Myh7 and Myb7b, which encode these microRNAs. These findings suggest that TRB3 regulates muscle fiber type via a peroxisome proliferator-activated receptor-α (PPAR-α)-regulated miR499/miR208b pathway, revealing a novel function for TRB3 in the regulation of skeletal muscle fiber type and exercise capacity.

Genetic effects in human skeletal muscle fiber type distribution and enzyme activities

1986 ◽  
Vol 64 (9) ◽  
pp. 1245-1251 ◽  
Author(s):  
C. Bouchard ◽  
J. A. Simoneau ◽  
G. Lortie ◽  
M. R. Boulay ◽  
M. Marcotte ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Fiber ◽  
Enzyme Activities ◽  
Fiber Type ◽  
Genetic Effect ◽  
Genetic Effects ◽  
Type I ◽  
Type Distribution ◽  
Fiber Type Distribution ◽  
Mz Twins

The purpose of the study was to estimate the genetic effect for skeletal muscle characteristics using pairs of nontwin brothers (n = 32), dizygotic (DZ) twins (n = 26), and monozygotic (MZ) twins (n = 35). They were submitted to a needle biopsy of the vastus lateralis for the determination of fiber type distribution (I, IIa, IIb) and the following enzymes were assayed for maximal activity: creatine kinase, hexokinase, phosphofructokinase (PFK), lactate dehydrogenase, malate dehydrogenase, 3-hydroxyacyl CoA dehydrogenase, and oxoglutarate dehydrogenase (OGDH). For the percentage of type I fibers, intraclass correlations were 0.33 (p < 0.05), 0.52 (p < 0.01), and 0.55 (p < 0.01) in brothers and DZ and MZ twins, respectively. MZ twins exhibited significant within-pair resemblance for all enzyme activities (0.30 ≤ r ≤ 0.68). In spite of these correlations, genetic analyses performed with the twin data alone indicated that there was no significant genetic effect for muscle fiber type I, IIa, and IIb distribution and fiber areas. Although there were significant correlations in MZ twins for all muscle enzyme activities, the often nonsignificant intraclass coefficients found in brothers and DZ twins suggest that variations in enzyme activities are highly related to common environmental conditions and nongenetic factors. However, genetic factors appear to be involved in the variation of regulatory enzymes of the glycolytic (PFK) and citric acid cycle (OGDH) pathways and in the variation of the oxidative to glycolytic activity ratio (PFK/OGDH ratio). Data show that these genetic effects reach only about 25–50% of the total phenotypic variation when data are adjusted for age and sex differences.

scholarly journals Satellite cell content is specifically reduced in type II skeletal muscle fibers in the elderly

2007 ◽  
Vol 292 (1) ◽  
pp. E151-E157 ◽  
Author(s):  
Lex B. Verdijk ◽  
René Koopman ◽  
Gert Schaart ◽  
Kenneth Meijer ◽  
Hans H. C. M. Savelberg ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Fiber ◽  
Fiber Type ◽  
The Elderly ◽  
Type I ◽  
Type Ii ◽  
Fiber Area ◽  
Muscle Fiber Atrophy ◽  
Fiber Atrophy ◽  
Type Ii Fibers

Satellite cells (SC) are essential for skeletal muscle growth and repair. Because sarcopenia is associated with type II muscle fiber atrophy, we hypothesized that SC content is specifically reduced in the type II fibers in the elderly. A total of eight elderly (E; 76 ± 1 yr) and eight young (Y; 20 ± 1 yr) healthy males were selected. Muscle biopsies were collected from the vastus lateralis in both legs. ATPase staining and a pax7-antibody were used to determine fiber type-specific SC content (i.e., pax7-positive SC) on serial muscle cross sections. In contrast to the type I fibers, the proportion and mean cross-sectional area of the type II fibers were substantially reduced in E vs. Y. The number of SC per type I fiber was similar in E and Y. However, the number of SC per type II fiber was substantially lower in E vs. Y (0.044 ± 0.003 vs. 0.080 ± 0.007; P < 0.01). In addition, in the type II fibers, the number of SC relative to the total number of nuclei and the number of SC per fiber area were also significantly lower in E. This study is the first to show type II fiber atrophy in the elderly to be associated with a fiber type-specific decline in SC content. The latter is evident when SC content is expressed per fiber or per fiber area. The decline in SC content might be an important factor in the etiology of type II muscle fiber atrophy, which accompanies the loss of skeletal muscle with aging.

Histochemical and Morphometric Evaluation of Skeletal Muscle of Cachectic Sheep

1981 ◽  
Vol 18 (3) ◽  
pp. 279-298 ◽  
Author(s):  
T. J. Hulland
Keyword(s):  
Skeletal Muscle ◽  
Muscle Fiber ◽  
Succinic Dehydrogenase ◽  
Adult Life ◽  
Biological Behavior ◽  
Type I ◽  
Fiber Types ◽  
Type Ii ◽  
Atrophy And Hypertrophy ◽  
Type I Fibers

Skeletal muscle of sheep was examined histochemically in an attempt to define muscle fiber populations capable of distinctive biological behavior. ATPase at alkaline and acid pH, NADH-TR, and succinic dehydrogenase showed at least 12 fiber types, but only three often enough to be considered biologically important muscle fiber populations. The proportions of the three major types altered during early life, but not perceptibly during adult life. Proportions of Type I and Type II fibers were different, sometimes significantly, from breed to breed. Histochemical techniques and morphometric analyses of fiber cross-sectional area were used to study muscle fiber changes in moderate to marked cachectic atrophy. Progressive reduction of gross muscle volume was attended by complex interrelationships between the two major muscle fiber types, including alternate episodes of atrophy and hypertrophy, resulting in marked inequality of mean fiber size between the fiber types. The patterns appeared to be different but characteristic for each muscle. The usual pattern of cachectic atrophy shows atrophy resistance of Type I fibers, but here a Type II-dominant atrophy also was seen. It is concluded that the large muscle fibers often seen in advanced cachectic atrophy are those Type I fibers that are more labile in both atrophy and hypertrophy than most.

Muscle Fiber Type Distribution in the Normal Human Levator Veli Palatini Muscle

1998 ◽  
Vol 35 (5) ◽  
pp. 419-424 ◽  
Author(s):  
Jerald B. Moon ◽  
Sue Ann Thompson ◽  
Elise Jaeckel ◽  
John W. Canady
Keyword(s):  
Muscle Tissue ◽  
Muscle Fiber ◽  
Fiber Type ◽  
Type I ◽  
Type Ii ◽  
Type Distribution ◽  
Levator Veli Palatini ◽  
Fiber Type Distribution ◽  
Type I Fibers ◽  
Type Ii Fibers

Objective This study examined the muscle fiber type distribution within the normal adult levator veli palatini muscle. Methods Levator veli palatini muscle tissue was harvested from the palates of 12 (seven female, five male) adult noncleft cadavers. Adjacent sections were stained for adenosine triphosphatase at pH 10.4 or 4.2. After mounting, magnifying, and photographing, Type I versus Type II fiber types were differentiated by the intensity of, or by the inhibition of, staining of matched fibers at each pH level. Type I fibers stained light at pH 10.4 and dark at pH 4.2, while Type II fibers stained light at pH 4.2 and dark at pH 10.4. Main outcome Measures The number of fibers counted for each specimen ranged from 60 to 616. The numbers of Type I and Type II stained fibers appearing in each muscle tissue sample were determined and expressed as a percentage of the total number of fibers identified. A few identified fibers could not be labelled as either Type I or Type II. Results The overall proportion of Type I fibers, averaged across all specimens, was 59.8%. Male specimens had 67.4% Type I fibers and 31.8% Type II fibers, while female specimens had 54.4% Type I fibers and 44.4% Type II fibers. Conclusions Observed fiber type distributions were similar to those reported for other articulatory muscles, but differed slightly from previously reported distributions for normal levator veli palatini. The distributions observed in this study provide a baseline against which to relate fiber type data from the levator veli palatini of cleft palates to the functional status of the velopharyngeal mechanism.

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