RESUMO
Insulin-like growth factor-1 (IGF1) is crucial for regulating post-natal growth and, along with myostatin (MSTN), regulates muscle size. Here, we sought to clarify the roles of these two genes in regulating sexually dimorphic growth of body and muscle mass. In the first study, we established that Igf1 mRNA was increased to a greater extent and Igf1 receptor mRNA increased earlier in male, than in female, gastrocnemius muscles during the rapid phase of growth (from 2 to 6 weeks) were unchanged, thereafter, to 32 weeks of age in WT mice (P < 0.001). In the second study, we sought to determine if supplemental IGF1 could overcome the sexual dimorphism of muscle and body mass, when myostatin is absent. We crossed myostatin null (Mstn-/-) mice with mice over-expressing Igf1 in skeletal muscle (Igf1+) to generate six genotypes; control (Mstn+/+), Mstn+/-, Mstn-/-, Mstn+/+:Igf1+, Mstn+/-:Igf1+ and Mstn-/-:Igf1+ (n = 8 per genotype and sex). In both sexes, body mass at 12 weeks was increased by at least 1.6-fold and muscle mass by at least 3-fold in Mstn-/-:Igf1+ compared with Mstn+/+ mice (P < 0.001). The abundance of AKT was increased in muscles of mice transgenic for Mstn, while phosphorylation of AKTS473 was increased in both male and female mice transgenic for Igf1+. The ratio of phosphorylated to total AKT was 1.9-fold greater in male mice (P < 0.001). Thus, despite increased growth of skeletal muscle and body size when myostatin was absent and IGF1 was in excess, sexual dimorphism persisted, an effect consistent with greater IGF1-induced activation of AKT in skeletal muscles of males.
Assuntos
Fator de Crescimento Insulin-Like I/metabolismo , Músculo Esquelético/crescimento & desenvolvimento , Miostatina/fisiologia , Proteínas Proto-Oncogênicas c-akt/metabolismo , Caracteres Sexuais , Animais , Feminino , Masculino , Camundongos Transgênicos , Músculo Esquelético/metabolismo , Receptor IGF Tipo 1/metabolismoRESUMO
Little is known about the molecular responses to power resistance exercise that lead to skeletal muscle remodeling and enhanced athletic performance. We assessed the expression of titin-linked putative mechanosensing proteins implicated in muscle remodeling: muscle ankyrin repeat proteins (Ankrd 1, Ankrd 2, and Ankrd 23), muscle-LIM proteins (MLPs), muscle RING-finger protein-1 (MuRF-1), and associated myogenic proteins (MyoD1, myogenin, and myostatin) in skeletal muscle in response to power resistance exercise with or without a postexercise meal, in fed, resistance-trained men. A muscle sample was obtained from the vastus lateralis of seven healthy men on separate days, 3 h after 90 min of rest (Rest) or power resistance exercise with (Ex + Meal) or without (Ex) a postexercise meal to quantify mRNA and protein levels. The levels of phosphorylated HSP27 (pHSP27-Ser15) and cytoskeletal proteins in muscle and creatine kinase activity in serum were also assessed. The exercise increased (P ≤ 0.05) pHSP27-Ser15 (â¼6-fold) and creatine kinase (â¼50%), whereas cytoskeletal protein levels were unchanged (P > 0.05). Ankrd 1 (â¼15-fold) and MLP (â¼2-fold) mRNA increased, whereas Ankrd 2, Ankrd 23, MuRF-1, MyoD1, and myostatin mRNA were unchanged. Ankrd 1 (â¼3-fold, Ex) and MLPb (â¼20-fold, Ex + Meal) protein increased, but MLPa, Ankrd 2, Ankrd 23, and the myogenic proteins were unchanged. The postexercise meal did not affect the responses observed. Power resistance exercise, as performed in practice, induced subtle early responses in the expression of MLP and Ankrd 1 yet had little effect on the other proteins investigated. These findings suggest possible roles for MLP and Ankrd 1 in the remodeling of skeletal muscle in individuals who regularly perform this type of exercise.NEW & NOTEWORTHY This is the first study to assess the early changes in the expression of titin-linked putative mechanosensing proteins and associated myogenic regulatory factors in skeletal muscle after power resistance exercise in fed, resistance-trained men. We report that power resistance exercise induces subtle early responses in the expression of Ankrd 1 and MLP, suggesting these proteins play a role in the remodeling of skeletal muscle in individuals who regularly perform this type of exercise.
Assuntos
Treinamento Resistido , Conectina , Exercício Físico , Humanos , Masculino , Músculo Esquelético , MiogeninaRESUMO
Muscle ankyrin repeat proteins (MARPs) are a family of titin-associated, stress-response molecules and putative transducers of stretch-induced signaling in skeletal muscle. In cardiac muscle, cardiac ankyrin repeat protein (CARP) and diabetes-related ankyrin repeat protein (DARP) reportedly redistribute from binding sites on titin to the nucleus following a prolonged stretch. However, it is unclear whether ankyrin repeat domain protein 2 (Ankrd 2) shows comparable stretch-induced redistribution to the nucleus. We measured the following in rested human skeletal muscle: 1) the absolute amount of MARPs and 2) the distribution of Ankrd 2 and DARP in both single fibers and whole muscle preparations. In absolute amounts, Ankrd 2 is the most abundant MARP in human skeletal muscle, there being ~3.1 µmol/kg, much greater than DARP and CARP (~0.11 and ~0.02 µmol/kg, respectively). All DARP was found to be tightly bound at cytoskeletal (or possibly nuclear) sites. In contrast, ~70% of the total Ankrd 2 is freely diffusible in the cytosol [including virtually all of the phosphorylated (p)Ankrd 2-Ser99 form], ~15% is bound to non-nuclear membranes, and ~15% is bound at cytoskeletal sites, likely at the N2A region of titin. These data are not consistent with the proposal that Ankrd 2, per se, or pAnkrd 2-Ser99 mediates stretch-induced signaling in skeletal muscle, dissociating from titin and translocating to the nucleus, because the majority of these forms of Ankrd 2 are already free in the cytosol. It will be necessary to show that the titin-associated Ankrd 2 is modified by stretch in some as-yet-unidentified way, distinct from the diffusible pool, if it is to act as a stretch-sensitive signaling molecule.
Assuntos
Repetição de Anquirina/fisiologia , Proteínas Musculares/metabolismo , Músculo Esquelético/metabolismo , Proteínas Nucleares/metabolismo , Proteínas Repressoras/metabolismo , Adulto , Animais , Feminino , Humanos , Ratos , Ratos Sprague-Dawley , Distribuição TecidualRESUMO
Insulin-like growth factors (IGFs) and myostatin have opposing roles in regulating the growth and size of skeletal muscle, with IGF1 stimulating, and myostatin inhibiting, growth. However, it remains unclear whether these proteins have mutually dependent, or independent, roles. To clarify this issue, we crossed myostatin null (Mstn-/-) mice with mice overexpressing Igf1 in skeletal muscle (Igf1+) to generate six genotypes of male mice; wild type (Mstn+/+ ), Mstn+/-, Mstn-/-, Mstn+/+:Igf1+, Mstn+/-:Igf1+ and Mstn-/-:Igf1+ Overexpression of Igf1 increased the mass of mixed fibre type muscles (e.g. Quadriceps femoris) by 19% over Mstn+/+ , 33% over Mstn+/- and 49% over Mstn-/- (P < 0.001). By contrast, the mass of the gonadal fat pad was correspondingly reduced with the removal of Mstn and addition of Igf1 Myostatin regulated the number, while IGF1 regulated the size of myofibres, and the deletion of Mstn and Igf1+ independently increased the proportion of fast type IIB myosin heavy chain isoforms in T. anterior (up to 10% each, P < 0.001). The abundance of AKT and rpS6 was increased in muscles of Mstn-/-mice, while phosphorylation of AKTS473 was increased in Igf1+mice (Mstn+/+:Igf1+, Mstn+/-:Igf1+ and Mstn-/-:Igf1+). Our results demonstrate that a greater than additive effect is observed on the growth of skeletal muscle and in the reduction of body fat when myostatin is absent and IGF1 is in excess. Finally, we show that myostatin and IGF1 regulate skeletal muscle size, myofibre type and gonadal fat through distinct mechanisms that involve increasing the total abundance and phosphorylation status of AKT and rpS6.
Assuntos
Regulação da Expressão Gênica/fisiologia , Fator de Crescimento Insulin-Like I/metabolismo , Músculo Esquelético/fisiologia , Miostatina/metabolismo , Tecido Adiposo/fisiologia , Animais , Genótipo , Fator de Crescimento Insulin-Like I/genética , Masculino , Camundongos , Camundongos Knockout , Camundongos Transgênicos , Miostatina/genética , RNA Mensageiro/genética , RNA Mensageiro/metabolismoRESUMO
Skeletal muscles of myostatin null (Mstn(-/-)) mice are more susceptible to atrophy during hind limb suspension (HS) than are muscles of wild-type mice. Here we sought to elucidate the mechanism for this susceptibility and to determine if Mstn(-/-) mice can regain muscle mass after HS. Male Mstn(-/-) and wild-type mice were subjected to 0, 2 or 7 days of HS or 7 days of HS followed by 1, 3 or 7 days of reloading (nâ=â6 per group). Mstn(-/-) mice lost more mass from muscles expressing the fast type IIb myofibres during HS and muscle mass was recovered in both genotypes after reloading for 7 days. Concentrations of MAFbx and MuRF1 mRNA, crucial ligases regulating the ubiquitin-proteasome system, but not MUSA1, a BMP-regulated ubiquitin ligase, were increased more in muscles of Mstn(-/-) mice, compared with wild-type mice, during HS and concentrations decreased in both genotypes during reloading. Similarly, concentrations of LC3b, Gabarapl1 and Atg4b, key effectors of the autophagy-lysosomal system, were increased further in muscles of Mstn(-/-) mice, compared with wild-type mice, during HS and decreased in both genotypes during reloading. There was a greater abundance of 4E-BP1 and more bound to eIF4E in muscles of Mstn(-/-) compared with wild-type mice (P<0.001). The ratio of phosphorylated to total eIF2α increased during HS and decreased during reloading, while the opposite pattern was observed for rpS6. Concentrations of myogenic regulatory factors (MyoD, Myf5 and myogenin) mRNA were increased during HS in muscles of Mstn(-/-) mice compared with controls (P<0.001). We attribute the susceptibility of skeletal muscles of Mstn(-/-) mice to atrophy during HS to an up- and downregulation, respectively, of the mechanisms regulating atrophy of myofibres and translation of mRNA. These processes are reversed during reloading to aid a faster rate of recovery of muscle mass in Mstn(-/-) mice.
Assuntos
Regulação da Expressão Gênica , Elevação dos Membros Posteriores , Desenvolvimento Muscular/genética , Músculo Esquelético/metabolismo , Atrofia Muscular/genética , Miostatina/deficiência , Biossíntese de Proteínas/genética , Transdução de Sinais/genética , Animais , Western Blotting , Peso Corporal , Masculino , Camundongos Endogâmicos C57BL , Fibras Musculares Esqueléticas/metabolismo , Cadeias Pesadas de Miosina/metabolismo , Miostatina/metabolismo , Tamanho do Órgão , Fosforilação , Ligação Proteica , RNA Mensageiro/genética , RNA Mensageiro/metabolismoRESUMO
Weightlifting is a dynamic strength and power sport in which two, multijoint, whole-body lifts are performed in competition; the snatch and clean and jerk. During the performance of these lifts, weightlifters have achieved some of the highest absolute and relative peak power outputs reported in the literature. The training structure of competitive weightlifters is characterized by the frequent use of high-intensity resistance exercise movements. Varied coaching and training philosophies currently exist around the world and further research is required to substantiate the best type of training programme for male and female weightlifters of various age groups. As competitive weightlifting is contested over eight male and seven female body weight categories, the anthropometric characteristics of the athletes widely ranges. The body compositions of weightlifters are similar to that of athletes of comparable body mass in other strength and power sports. However, the shorter height and limb lengths of weightlifters provide mechanical advantages when lifting heavy loads by reducing the mechanical torque and the vertical distance that the barbell must be displaced. Furthermore, the shorter body dimensions coincide with a greater mean skeletal muscle cross-sectional area that is advantageous to weightlifting performance. Weightlifting training induces a high metabolic cost. Although dietary records demonstrate that weightlifters typically meet their required daily energy intake, weightlifters have been shown to over consume protein and fat at the expense of adequate carbohydrate. The resulting macronutrient imbalance may not yield optimal performance gains. Cross-sectional data suggest that weightlifting training induces type IIX to IIA fibre-type transformation. Furthermore, weightlifters exhibit hypertrophy of type II fibres that is advantageous to weightlifting performance and maximal force production. As such, the isometric peak force and contractile rate of force development of weightlifters is ~15-20% and ~13-16% greater, respectively, than in other strength and power athletes. In addition, weightlifting training has been shown to reduce the typical sex-related difference in the expression of neuromuscular strength and power. However, this apparent sex-related difference appears to be augmented with increasing adult age demonstrating that women undergo a greater age-related decline in muscle shortening velocity and peak power when compared with men. Weightlifting training and competition has been shown to induce significant structural and functional adaptations of the cardiovascular system. The collective evidence shows that these adaptations are physiological as opposed to pathological. Finally, the acute exercise-induced testosterone, cortisol and growth hormone responses of weightlifters have similarities to that of following conventional strength and hypertrophy protocols involving large muscle mass exercises. The routine assessment of the basal testosterone : cortisol ratio may be beneficial when attempting to quantify the adaptive responses to weightlifting training. As competitive weightlifting is becoming increasingly popular around the world, further research addressing the physiological responses and adaptations of female weightlifters and younger (i.e. ≤17 years of age) and older (i.e. ≥35 years of age) weightlifters of both sexes is required.
Assuntos
Desempenho Atlético/fisiologia , Exercício Físico/fisiologia , Força Muscular/fisiologia , Músculo Esquelético/fisiologia , Educação Física e Treinamento , Levantamento de Peso/fisiologia , Composição Corporal , Densidade Óssea , Fenômenos Fisiológicos Cardiovasculares , Feminino , Humanos , Masculino , Testosterona/sangueRESUMO
Peak force (PF), contractile rate of force development (RFD) and contractile impulse (CI) are of great importance to competitive weightlifters (WL). These athletes routinely perform successive bouts of high-intensity resistance exercise (HIRE) within the same day (double-day training) with the aim of improving muscular function and weightlifting performance. The purpose of this investigation was to determine and compare the PF, contractile RFD and CI responses to double-day training between WL and resistance trained (RT) adults (n = 16 per group). Furthermore, we sought to establish whether acute changes in muscle function were associated with acute changes in muscle architecture. Isometric front squat PF, contractile RFD, CI and the pennation angle (θ(p)), anatomical and physiological thickness of the m. vastus lateralis (VL) were determined before and after two equivalent HIRE sessions separated by 4-6 h rest. Each session consisted of ten single repetitions of the dynamic barbell front squat interspersed with 2-min rest, using a load equivalent to 90% of the pre-session PF. Weightlifters demonstrated greater PF at all time points when compared to RT adults and exhibited no significant within or between session changes in PF, contractile RFD or CI. Conversely, RT adults demonstrated within- and between-session decreases in PF and between-session increases in contractile RFD and CI. As no correlations were found between the relative within-session changes in muscle function and the concomitant changes in muscle architecture, other factors must contribute to the divergent responses in PF, contractile RFD and CI between WL and RT adults.
Assuntos
Exercício Físico/fisiologia , Contração Isométrica/fisiologia , Músculo Esquelético/fisiologia , Treinamento Resistido , Levantamento de Peso/fisiologia , Adulto , Feminino , Humanos , Masculino , Força Muscular/fisiologiaRESUMO
The aim of this study was to evaluate the suitability of ultrasonography for the quantification of gastrocnemius muscle architecture in healthy young children. The variation and reliability of measurement of muscle thickness, pennation angle and fibre length of the medial gastrocnemius were determined, using stationary and portable ultrasound machines, in 13 boys and eight girls aged 4-10. Ultrasound images were obtained from each leg, in duplicate, with the ankle at 90 degrees , then at maximal plantar flexion, with the two machines within the same session. The same set of 16 scans was repeated in four children 4-6 weeks later. The mean muscle thickness, pennation angle and fibre length differed between ankle positions and between legs. Measurements obtained using the two machines established similar values with no significant differences in absolute values and coefficients of variation (CV). For duplicate images taken during the same session for the same leg, ankle position and machine, the CV and intraclass correlation coefficients (ICC) ranged, respectively, from 2.1% to 3.1% and 0.94-0.98 for muscle thickness, from 4.1% to 6.0% and 0.85-0.96 for pennation angle and from 4.5% to 6.3% and 0.87-0.96 for fibre length. Corresponding values for variables for the same child measured on two separate occasions were within the same ranges, all being similar to reliability data reported previously for adult muscle. Muscle thickness, pennation angle and fibre length of the medial gastrocnemius can therefore be quantified reliably, using either a stationary or portable ultrasound machine, in healthy young children.
Assuntos
Articulação do Tornozelo/diagnóstico por imagem , Músculo Esquelético/diagnóstico por imagem , Ultrassonografia/métodos , Criança , Pré-Escolar , Feminino , Humanos , Masculino , Reprodutibilidade dos Testes , Sensibilidade e EspecificidadeRESUMO
Intramuscular injections of botulinum toxin A (Btx-A) and exercise are used in the treatment of muscle spasticity in children with cerebral palsy. However, little is known about the biological changes within muscle subsequent to Btx-A-induced paralysis and how the combination of Btx-A and exercise might affect the growing muscle. The wet mass, myosin heavy chain (MHC) composition, and titin content of the juvenile rat gastrocnemius muscle were determined 3 weeks after Btx-A injections and subsequent voluntary wheel-running exercise. Btx-A increased the proportion of type IIa (+121%) and IIx (+65%) MHC while decreasing the proportion of type IIb MHC (-51%) and reducing the titin content (-18%). Exercise did not amplify or reduce the changes induced by Btx-A. Thus, we conclude that although the sarcomeric stability of paralyzed muscle might be impaired, moderate mechanical loading does not seem to affect paralyzed muscle protein composition.
Assuntos
Toxinas Botulínicas Tipo A/toxicidade , Proteínas Musculares/metabolismo , Músculo Esquelético/metabolismo , Cadeias Pesadas de Miosina/metabolismo , Neurotoxinas/toxicidade , Paralisia/induzido quimicamente , Paralisia/metabolismo , Proteínas Quinases/metabolismo , Fatores Etários , Animais , Peso Corporal , Conectina , Masculino , Músculo Esquelético/efeitos dos fármacos , Músculo Esquelético/patologia , Miosina Tipo I/metabolismo , Miosina não Muscular Tipo IIA/metabolismo , Miosina não Muscular Tipo IIB/metabolismo , Tamanho do Órgão , Condicionamento Físico Animal , Isoformas de Proteínas/metabolismo , Ratos , Ratos Sprague-DawleyRESUMO
Myostatin inhibits myogenesis and there is reduced abundance of the mature protein in skeletal muscles of adult male compared with female mice. This reduction probably occurs after translation, which suggests that it is a regulated mechanism to reduce the availability of myostatin in males. Reduced myostatin may, thereby, contribute to the development of sexually dimorphic growth of skeletal muscle. Our first objective was to determine if the decrease in mature myostatin protein occurs before the linear growth phase to aid growth, or afterwards to maintain the mass of adult muscle. Mice were killed from 2 to 32 weeks and the gastrocnemius muscle was excised. Myostatin mRNA increased from 2 to 32 weeks and was higher in males than females (P < 0.001). In contrast, mature protein decreased in males after 6 weeks (P < 0.001). Our second objective was to determine if growth hormone (GH) induces the decrease in mature myostatin protein. GH increased myostatin mRNA and decreased the abundance of mature protein in hypophysectomised mice (P < 0.05). Our final objective was to determine if the decrease in mature protein occurs in skeletal muscles of male Stat5b(-/-) mice (Stat5b mediates the actions of GH). As expected, mature myostatin protein was not reduced in Stat5b(-/-) males compared with females. However, myostatin mRNA remained higher in males than females irrespective of genotype. These data suggest that: (1) the decrease in mature myostatin protein is developmentally regulated, (2) GH acting via Stat5b regulates the abundance of mature myostatin and (3) GH acts via a non-Stat5b pathway to regulate myostatin mRNA.
Assuntos
Regulação para Baixo , Hormônio do Crescimento/metabolismo , Músculo Esquelético , Miostatina/metabolismo , Animais , Peso Corporal , Feminino , Regulação da Expressão Gênica no Desenvolvimento , Masculino , Camundongos , Camundongos Knockout , Desenvolvimento Muscular/fisiologia , Músculo Esquelético/crescimento & desenvolvimento , Músculo Esquelético/metabolismo , Miostatina/genética , Fator de Transcrição STAT5/deficiência , Fator de Transcrição STAT5/genética , Caracteres SexuaisRESUMO
The myogenic regulatory factor MyoD plays an important role in embryonic and adult skeletal muscle growth. Even though it is best known as a marker for activated satellite cells, it is also expressed in myonuclei, and its expression can be induced by a variety of different conditions. Several model systems have been used to study the mechanisms behind MyoD regulation, such as exercise, stretch, disuse, and denervation. Since MyoD reacts in a highly muscle-specific manner, and its expression varies over time and between species, universally valid predictions and explanations for changes in MyoD expression are not possible. This review explores the complex role of MyoD in muscle plasticity by evaluating the induction of MyoD expression in the context of muscle composition and electrical and mechanical stimulation.
Assuntos
Exercício Físico/fisiologia , Denervação Muscular , Músculos/metabolismo , Transtornos Musculares Atróficos/metabolismo , Proteína MyoD/metabolismo , Animais , Regulação da Expressão Gênica/fisiologia , Humanos , Transtornos Musculares Atróficos/patologiaRESUMO
Intramuscular injections of the paralytic botulinum neurotoxin A (Btx) and physical exercise are used in the treatment of chronic spasticity in children with cerebral palsy. We tested whether Btx-induced paralysis and/or exercise training would have differential effects on the expression of mechanosensing and signalling genes implicated in the adaptive remodelling of skeletal muscle. Juvenile (29-day-old) male rats were injected with Btx or saline (NoBtx) into the right gastrocnemius and housed in standard cages (NoEx) or with running wheels (Ex), for 3 weeks (n = 6 per group). The mRNA expression of nine sarcomere-associated genes in the medial gastrocnemius was then determined by quantitative reverse transcriptase-polymerase chain reaction. The Btx-injected muscles weighed 50% less than NoBtx muscles, but Ex had no effect on the wet mass of Btx or NoBtx muscles. Atrogenic MuRF1, sarcomeric Titin and myogenic MyoD were upregulated (2-fold) with the elimination of contractile activity in Btx muscle. Expression of CARP, Ankrd2 and MLP was increased with mechanical stimuli associated with Btx (5- to 10-fold) or Ex (2- to 4-fold). Expression of CARP and Ankrd2 increased synergistically in Btx-Ex muscle (> or = 20-fold), indicating that these genes may be sensitive to passive stretch of the sarcomeric I-band region of titin to which their proteins bind. Tcap, Myopalladin and Atrogin1 were not, or were no longer responsive to the altered mechanical stimuli after 3 weeks of Btx or Ex. The expression of Ankrd2, CARP and MLP may thus be enhanced by passive stretch within the Btx-paralysed and/or exercising gastrocnemius and contribute to adaptations, other than muscle mass, in juvenile rats.
Assuntos
Mecanotransdução Celular , Proteínas Musculares/metabolismo , Músculo Esquelético/metabolismo , Paralisia/metabolismo , Esforço Físico , Adaptação Fisiológica , Animais , Peso Corporal , Toxinas Botulínicas Tipo A/administração & dosagem , Modelos Animais de Doenças , Regulação da Expressão Gênica , Injeções Intramusculares , Masculino , Mecanotransdução Celular/genética , Proteínas Musculares/genética , Músculo Esquelético/patologia , Músculo Esquelético/fisiopatologia , Tamanho do Órgão , Paralisia/induzido quimicamente , Paralisia/genética , Paralisia/fisiopatologia , RNA Mensageiro/metabolismo , Ratos , Ratos Sprague-Dawley , Reação em Cadeia da Polimerase Via Transcriptase Reversa , Sarcômeros/metabolismo , Fatores de TempoRESUMO
The aims of this study were to characterize the pattern of voluntary activity of young rats in response to resistance loading on running wheels and to determine the effects of the activity on the growth of six limb skeletal muscles. Male Sprague-Dawley rats (4 weeks old) were housed individually with a resistance running wheel (R-RUN, n = 7) or a conventional free-spinning running wheel (F-RUN, n = 6) or without a wheel, as non-running control animals (CON, n = 6). The torque required to move the wheel in the R-RUN group was progressively increased, and the activity (velocity, distance and duration of each bout) of the two running wheel groups was recorded continuously for 45 days. The R-RUN group performed many more, shorter and faster bouts of running than the F-RUN group, yet the mean daily distance was not different between the F-RUN (1.3 +/- 0.2 km) and R-RUN group (1.4 +/- 0.6 km). Only the R-RUN resulted in a significantly (P < 0.05) enhanced muscle wet mass, relative to the increase in body mass, of the plantaris (23%) and vastus lateralis muscle (17%), and the plantaris muscle fibre cross-sectional area, compared with CON. Both F-RUN and R-RUN led to a significantly greater wet mass relative to increase in body mass and muscle fibre cross-sectional area in the soleus muscle compared with CON. We conclude that the pattern of voluntary activity on a resistance running wheel differs from that on a free-spinning running wheel and provides a suitable model to induce physiological muscle hypertrophy in rats.
Assuntos
Músculo Esquelético/crescimento & desenvolvimento , Condicionamento Físico Animal/fisiologia , Animais , Peso Corporal/fisiologia , Masculino , Atividade Motora/fisiologia , Fibras Musculares Esqueléticas/fisiologia , Músculo Esquelético/citologia , Músculo Esquelético/fisiologia , Tamanho do Órgão/fisiologia , Esforço Físico/fisiologia , Ratos , Ratos Sprague-Dawley , Corrida/fisiologiaRESUMO
PURPOSE: We determined and compared the magnitude of changes in resting plasma myostatin and IGF-1, muscle strength, and size in response to whole body or local muscle resistance training in healthy men. METHODS: Volunteers performed high-intensity resistance exercise of major muscle groups of the whole body (N = 11), or of the elbow flexors only (N = 6), twice per week for 10 wk. Strength was assessed by elbow flexor one-repetition maximum (1-RM) and repetitions at 80% of 1-RM, muscle cross-sectional area by MRI, and plasma IGF-1 by RIA and myostatin by Western analyses, before and after the training program. RESULTS: In subjects of both groups, elbow flexor 1-RM and cross-sectional area increased (P = 0.05) by 30 +/- 8% (mean +/- SD) and 12 +/- 4%, respectively. Individual changes in myostatin ranged from 5.9 to -56.9%, with a mean decrease of 20 +/- 16%, whereas IGF-1 did not change from pre- to posttraining. There were no significant differences in any of the responses of the subjects between the two training programs. CONCLUSION: Myostatin may play a role in exercise-induced increases in muscle size, its circulating levels decreasing with resistance training in healthy men. Exercise of the whole body versus the elbow flexors alone did not provide a supplementary stimulus in altering resting plasma IGF-1 or myostatin, or in increasing muscle strength or size. Thus, by default, growth factor responses local to the muscle may be more important than circulating factors in contributing to muscle hypertrophy with resistance training.
Assuntos
Fator de Crescimento Insulin-Like I/metabolismo , Músculos/fisiologia , Educação Física e Treinamento/métodos , Fator de Crescimento Transformador beta/sangue , Adolescente , Adulto , Cotovelo/fisiologia , Humanos , Hipertrofia , Estudos Longitudinais , Imageamento por Ressonância Magnética , Masculino , Músculos/anatomia & histologia , Miostatina , Estatísticas não ParamétricasRESUMO
Myostatin inhibits myogenesis. Therefore, we sought to determine if mice lacking the myostatin gene [Mstn(-/-)] would lose less muscle mass than wild-type mice during 7 days of hindlimb suspension (HS). Male Mstn(-/-) and wild-type (C57) mice were subjected to HS or served as ground-based controls (n = 6/group). Wild-type mice lost 8% of body mass and approximately 13% of wet mass from biceps femoris, quadriceps femoris, and soleus, whereas the mass of extensor digitorum longus (EDL) was unchanged after HS. Unexpectedly, Mstn(-/-) mice lost more body (13%, P < 0.05) and quadriceps femoris (17%, P < 0.05) mass than wild-type mice and lost 33% of EDL mass (P < 0.01) after HS. Protein expression of myostatin in biceps femoris and quadriceps femoris was not altered, whereas expression of MyoD, Myf-5, and myogenin increased in wild-type mice and tended to decrease in muscles of Mstn(-/-) mice. These data suggest that HS induced myogenesis in wild-type mice to counter atrophy, whereas myogenesis was not induced in Mstn(-/-) mice, thereby resulting in a greater loss of muscle mass.
Assuntos
Proteínas de Ligação a DNA , Elevação dos Membros Posteriores/fisiologia , Músculo Esquelético/fisiologia , Transativadores , Fator de Crescimento Transformador beta/deficiência , Animais , Atrofia/patologia , Biomarcadores , Western Blotting , Peso Corporal/fisiologia , Camundongos , Camundongos Endogâmicos C57BL , Camundongos Knockout , Proteínas Musculares/metabolismo , Proteína MyoD/metabolismo , Fator Regulador Miogênico 5 , Miogenina/metabolismo , Miostatina , Tamanho do Órgão/fisiologia , Fator de Crescimento Transformador beta/genéticaRESUMO
Botulinum toxin A (Btx) injections and supervised exercise are often used concurrently to treat calf muscle spasticity in children. This study has analyzed the early effects of Btx-induced paralysis and increased activity by voluntary wheel running on cell growth-related processes in juvenile rat gastrocnemius muscle. Btx injection at 29 days of age prevented the normal increases in wet mass (50%) and fiber cross-sectional area (34%) seen by 36 days of age in control rats. Btx-injected vs. contralateral muscles had 22% fewer myonuclei per fiber length but greater than twofold the number of MyoD-positive nuclei at 36 days of age. The accretion of 5-bromo-2'-deoxyuridine-labeled newly produced myonuclei did not differ between limbs. Voluntary exercise during the 7 days increased the mass (18%) and fiber size (23%) of Btx-injected and contralateral muscles but did not affect any other variable. Thus Btx injection and exercise had early effects on muscle and fiber size without consistently associated changes in myonuclear production or number. This suggests the presence of noncontractile activity-dependent, growth-promoting cytoplasmic events in juvenile muscle.