scholarly journals Muscle-Fiber Type and Blood Oxidative Stress After Eccentric Exercise

2011 ◽  
Vol 21 (6) ◽  
pp. 462-470 ◽  
Author(s):  
John Quindry ◽  
Lindsey Miller ◽  
Graham McGinnis ◽  
Megan Irwin ◽  
Charles Dumke ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Muscle Fiber ◽  
Fiber Type ◽  
Muscle Fiber Type ◽  
Vastus Lateralis Muscle ◽  
Type I ◽  
Oxidative Stress Biomarkers ◽  
Stress Biomarkers ◽  
Fast Twitch Muscle ◽  
Fast Twitch

Acute strength exercise elicits a transient oxidative stress, but the factors underlying the magnitude of this response remain unknown. The purpose of this investigation was to determine whether muscle-fiber type relates to the magnitude of blood oxidative stress after eccentric muscle activity. Eleven college-age men performed 3 sets of 50 eccentric knee-extensions. Blood samples taken pre-, post-, and 24, 48, 72, and 96 hr postexercise were assayed for comparison of muscle damage and oxidative-stress biomarkers including protein carbonyls (PCs). Vastus lateralis muscle biopsies were assayed for relative percentage of slow- and fast-twitch muscle fibers. There was a mixed fiber composition (Type I = 39.6% ± 4.5%, Type IIa = 35.7% ± 3.5%, Type IIx = 24.8% ± 3.8%; p = .366). PCs were elevated 24, 48, and 72 hr (p = .032) postexercise, with a peak response of 126% (p = .012) above baseline, whereas other oxidative-stress biomarkers were unchanged. There are correlations between Type II muscle-fiber type and postexercise PC. Further study is needed to understand the mechanisms responsible for the observed fast-twitch muscle-fiber oxidative-stress relationship.

Skeletal muscle histochemical and biochemical characteristics in sedentary male and female subjects

1985 ◽  
Vol 63 (1) ◽  
pp. 30-35 ◽  
Author(s):  
J. A. Simoneau ◽  
G. Lortie ◽  
M. R. Boulay ◽  
M.-C. Thibault ◽  
G. Thériault ◽  
...  
Keyword(s):  
Muscle Fiber ◽  
Enzyme Activities ◽  
Fiber Type ◽  
Muscle Fiber Type ◽  
Vastus Lateralis Muscle ◽  
Type I ◽  
Male And Female ◽  
Type Distribution ◽  
Fiber Type Distribution ◽  
Female Subjects

The purpose of this study was to assess the relationship between muscle fiber type distribution and enzymatic characteristics in sedentary male and female subjects. Muscle biopsy samples from the vastus lateralis muscle of 38 females and 37 males were analyzed to determine the fiber type composition (I, IIa, and IIb), the fiber size, and maximal activities of enzyme markers of energy metabolic pathways. Significant correlations were found (p < 0.05) between percent fiber type I area and hexokinase (r = −0.39), phosphofructokinase (r = −0.39), lactate dehydrogenase (r = −0.41), and oxoglutarate dehydrogenase (r = 0.33) activities, whereas such correlations with total phosphorylase (r = −0.02), malate dehydrogenase (r = 0.12), and 3-hydroxyacyl CoA dehydrogenase (r = 0.12) activities were not significant. The results of the present study also suggest the presence of a significant but low covariation of less than 30% between the fiber type distribution and muscle enzyme activities. They confirm the presence of an important metabolic heterogeneity independent of the muscle fiber type distribution in sedentary male and female subjects. Moreover, these results indicate that sedentary males exhibit a lower mean value of percent fiber type I and higher glycolytic enzyme activities than sedentary females.

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.

Ferulic acid regulates muscle fiber type formation through the Sirt1/AMPK signaling pathway

2019 ◽  
Vol 10 (1) ◽  
pp. 259-265 ◽  
Author(s):  
Xiaoling Chen ◽  
Yafei Guo ◽  
Gang Jia ◽  
Hua Zhao ◽  
Guangmang Liu ◽  
...  
Keyword(s):  
Ferulic Acid ◽  
Signaling Pathway ◽  
Muscle Fiber ◽  
Fiber Type ◽  
Muscle Fiber Type ◽  
Ampk Signaling ◽  
Slow Twitch ◽  
Fast Twitch

Ferulic acid promotes slow-twitch and inhibits fast-twitch myofiber formation via Sirt1/AMPK.

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.

scholarly journals The influence of training status, age, and muscle fiber type on cycling efficiency and endurance performance

2013 ◽  
Vol 115 (5) ◽  
pp. 723-729 ◽  
Author(s):  
James G. Hopker ◽  
Damian A. Coleman ◽  
Hannah C. Gregson ◽  
Simon A. Jobson ◽  
Tobias Von der Haar ◽  
...  
Keyword(s):  
Muscle Fiber ◽  
Power Output ◽  
Fiber Type ◽  
Muscle Fibers ◽  
Cycling Performance ◽  
Muscle Fiber Type ◽  
Type I ◽  
Maximal Heart Rate ◽  
Training Status ◽  
Cycling Efficiency

The purpose of this study was to assess the influence of age, training status, and muscle fiber-type distribution on cycling efficiency. Forty men were recruited into one of four groups: young and old trained cyclists, and young and old untrained individuals. All participants completed an incremental ramp test to measure their peak O2 uptake, maximal heart rate, and maximal minute power output; a submaximal test of cycling gross efficiency (GE) at a series of absolute and relative work rates; and, in trained participants only, a 1-h cycling time trial. Finally, all participants underwent a muscle biopsy of their right vastus lateralis muscle. At relative work rates, a general linear model found significant main effects of age and training status on GE ( P < 0.01). The percentage of type I muscle fibers was higher in the trained groups ( P < 0.01), with no difference between age groups. There was no relationship between fiber type and cycling efficiency at any work rate or cadence combination. Stepwise multiple regression indicated that muscle fiber type did not influence cycling performance ( P > 0.05). Power output in the 1-h performance trial was predicted by average O2 uptake and GE, with standardized β-coefficients of 0.94 and 0.34, respectively, although some mathematical coupling is evident. These data demonstrate that muscle fiber type does not affect cycling efficiency and was not influenced by the aging process. Cycling efficiency and the percentage of type I muscle fibers were influenced by training status, but only GE at 120 revolutions/min was seen to predict cycling performance.

Muscle fiber type specificity in insulin signal transduction

1999 ◽  
Vol 277 (6) ◽  
pp. R1690-R1696 ◽  
Author(s):  
Xiao Mei Song ◽  
Jeffrey W. Ryder ◽  
Yuichi Kawano ◽  
Alexander V. Chibalin ◽  
Anna Krook ◽  
...  
Keyword(s):  
Insulin Receptor ◽  
Tyrosine Phosphorylation ◽  
Muscle Fiber ◽  
Fiber Type ◽  
Insulin Response ◽  
Muscle Fiber Type ◽  
Specific Response ◽  
Type I ◽  
Akt Kinase ◽  
Sustained Activity

We determined the muscle fiber type-specific response of intracellular signaling proteins to insulin. Epitrochlearis (Epi; 15% type I, 20% type IIa, and 65% type IIb), soleus (84, 16, and 0%), and extensor digitorum longus (EDL; 3, 57, and 40%) muscles from Wistar rats were incubated without or with 120 nM insulin (3–40 min). Peak insulin receptor (IR) tyrosine phosphorylation was reached after 6 (soleus) and 20 (Epi and EDL) min, with sustained activity throughout insulin exposure (40 min). Insulin increased insulin receptor substrate (IRS)-1 and IRS-2 tyrosine phosphorylation and phosphotyrosine-associated phosphatidylinositol (PI)-3-kinase activity to a maximal level after 3–10 min, with subsequent downregulation. Akt kinase phosphorylation peaked at 20 min, with sustained activity throughout insulin exposure. Importantly, the greatest insulin response for all signaling intermediates was observed in soleus, whereas the insulin response between EDL and Epi was similar. Protein expression of the p85α-subunit of PI 3-kinase and Akt kinase, but not IR, IRS-1, or IRS-2, was greater in oxidative versus glycolytic muscle. In conclusion, increased function and/or expression of key proteins in the insulin-signaling cascade contribute to fiber type-specific differences in insulin action in skeletal muscle.

Interrelationships between muscle morphology, insulin action, and adiposity

1996 ◽  
Vol 270 (6) ◽  
pp. R1332-R1339 ◽  
Author(s):  
A. D. Kriketos ◽  
D. A. Pan ◽  
S. Lillioja ◽  
G. J. Cooney ◽  
L. A. Baur ◽  
...  
Keyword(s):  
Insulin Resistance ◽  
Body Fat ◽  
Muscle Fiber ◽  
Insulin Action ◽  
Fiber Type ◽  
Oxidative Capacity ◽  
Muscle Fiber Type ◽  
Type I ◽  
Fa Composition ◽  
Type I Fibers

There is evidence that insulin resistance and obesity are associated with relative increases in the proportion of glycolytic type IIb muscle fibers and decreases in the proportion of oxidative type I fibers. Futhermore, insulin resistance and obesity are associated with the fatty acid (FA) profile of structural membrane lipids. The present study was undertaken to define interrelationships between muscle fiber type and oxidative capacity, muscle membrane FA composition, and insulin action and obesity. Muscle morphology, insulin action, and body fat content were measured in 48 male nondiabetic Pima Indians. Percent body fat (pFAT, determined by hydrodensitometry) correlated negatively with percentage of type I fibers (r = -0.44, P = 0.002) and positively with percentage of type IIb fibers (r = 0.40, P = 0.005). Consistent with this finding, pFAT was also significantly related to oxidative capacity of muscle, as assessed by NADH staining (r = -0.47, P = 0.0007) and citrate synthase (CS) activity (r = -0.43, P = 0.008). Insulin action was correlated with oxidative capacity (CS; r = 0.41, P = 0.01) and weakly correlated with percentage of type IIb fibers (r = -0.29, P = 0.05). In addition, relationships were shown between muscle fiber type and FA composition (e.g., percentage of type I fibers related to n-3 FA; r = 0.37, P = 0.01). Thus leaness and insulin sensitivity are associated with increased oxidative capacity and unsaturation of membranes in skeletal muscle. Present studies support the hypothesis that muscle oxidative capacity and fiber type may play a genetically determined or an environmentally modified role in development of obesity and insulin resistance.

Cold-induced PGC-1α expression modulates muscle glucose uptake through an insulin receptor/Akt-independent, AMPK-dependent pathway

2004 ◽  
Vol 287 (4) ◽  
pp. E686-E695 ◽  
Author(s):  
Rachel L. G. S. Oliveira ◽  
Mirian Ueno ◽  
Cláudio T. de Souza ◽  
Márcio Pereira-da-Silva ◽  
Alessandra L. Gasparetti ◽  
...  
Keyword(s):  
Insulin Receptor ◽  
Glucose Uptake ◽  
Tyrosine Phosphorylation ◽  
Muscle Fiber ◽  
Cold Exposure ◽  
Antisense Oligonucleotide ◽  
Fiber Type ◽  
Muscle Fiber Type ◽  
Membrane Localization ◽  
Type I

Peroxisome proliferator-activated receptor-γ coactivator-1α (PGC-1α) participates in control of expression of genes involved in adaptive thermogenesis, muscle fiber type differentiation, and fuel homeostasis. The objective of the present study was to evaluate the participation of cold-induced PGC-1α expression in muscle fiber type-specific activity of proteins that belong to the insulin-signaling pathway. Rats were exposed to 4°C for 4 days and acutely treated with insulin in the presence or absence of an antisense oligonucleotide to PGC-1α. Cold exposure promoted a significant increase of PGC-1α and uncoupling protein-3 protein expression in type I and type II fibers of gastrocnemius muscle. In addition, cold exposure led to higher glucose uptake during a hyperinsulinemic clamp, which was accompanied by higher expression and membrane localization of GLUT4 in both muscle fiber types. Cold exposure promoted significantly lower insulin-induced tyrosine phosphorylation of the insulin receptor (IR) and Ser473 phosphorylation of acute transforming retrovirus thymoma (Akt) and an insulin-independent increase of Thr172 phosphorylation of adenosine 5′-monophosphate-activated protein kinase (AMPK). Inhibition of PGC-1α expression in cold-exposed rats by antisense oligonucleotide treatment diminished glucose clearance rates during a hyperinsulinemic clamp and reduced expression and membrane localization of GLUT4. Reduction of PGC-1α expression resulted in no modification of insulin-induced tyrosine phosphorylation of the IR and Ser473 phosphorylation of Akt. Finally, reduction of PGC-1α resulted in lower Thr172 phosphorylation of AMPK. Thus cold-induced hyperexpression of PGC-1α participates in control of skeletal muscle glucose uptake through a mechanism that controls GLUT4 expression and subcellular localization independent of the IR and Akt activities but dependent on AMPK.

scholarly journals ACTN3 (R577X) genotype is associated with fiber type distribution

2007 ◽  
Vol 32 (1) ◽  
pp. 58-63 ◽  
Author(s):  
Barbara Vincent ◽  
Katrien De Bock ◽  
Monique Ramaekers ◽  
Els Van den Eede ◽  
Marc Van Leemputte ◽  
...  
Keyword(s):  
Muscle Fiber ◽  
Muscle Power ◽  
Control Function ◽  
Stop Codon ◽  
Fiber Type ◽  
Premature Stop Codon ◽  
Muscle Fiber Type ◽  
Vastus Lateralis Muscle ◽  
Type Distribution ◽  
Fiber Type Distribution

α-Actinin-3 is a Z-disc structural protein found only in type II muscle fibers. The X allele of the R577X polymorphism in the ACTN3 gene results in a premature stop codon and α-actinin-3 deficiency in XX homozygotes. Associations between the R577X polymorphism and the muscle-power performance of elite athletes have been described earlier. About 45% of the fiber type proportions are determined by genetic factors. The ACTN3 variant could be one of the contributing genes in the heritability of fiber type distribution through its interaction with calcineurin. The aim of this study was to quantify the association between the polymorphism and muscle fiber type distribution and fast-velocity knee extension strength. Ninety healthy young men (18–29 y) were genotyped for ACTN3 R577X. Knee extensor strength was measured isometrically (45°) and at different dynamic velocities (100–300°/s) on a programmable dynamometer. Twenty-two XX and twenty-two RR subjects underwent a biopsy of the right vastus lateralis muscle. Fiber type composition was determined by immunohistochemistry. Homozygotes for the R allele show significantly higher relative dynamic quadriceps torques at 300°/s, compared with XX carriers ( P < 0.05). Fiber type characteristics differed significantly between the two genotype groups. The percentage surface and number of type IIx fibers were greater in the RR than the XX genotype group ( P < 0.05), and α-actinin-3 protein content is systematically higher in type IIx compared with type IIa fibers (staining intensity ratio IIx to IIa = 1.17). This study shows that the mechanism, by which the ACTN3 polymorphism has its effect on muscle power, might rely on a control function of fiber type proportions.

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