Changes in myosin heavy chain mRNA and protein expression in human skeletal muscle with age and endurance exercise training

2005 ◽  
Vol 99 (1) ◽  
pp. 95-102 ◽  
Author(s):  
Kevin R. Short ◽  
Janet L. Vittone ◽  
Maureen L. Bigelow ◽  
David N. Proctor ◽  
Jill M. Coenen-Schimke ◽  
...  
Keyword(s):  
Exercise Training ◽  
Protein Expression ◽  
Myosin Heavy Chain ◽  
Endurance Exercise ◽  
Heavy Chain ◽  
Contractile Function ◽  
Mhc I ◽  
Altered Expression ◽  
Endurance Exercise Training ◽  
Mhc Iia

Aging is associated with reduced muscle strength and atrophy of type II muscle fibers. Muscle fiber type and contractile function are primarily determined by myosin heavy chain (MHC) isoforms. There are few data available on the effects of aging on MHC isoform expression in humans. In the present study, we tested the hypothesis that MHC isoform protein composition and mRNA abundance would favor a fast-to-slow isoform shift with aging and in response to endurance exercise training. Muscle biopsies were obtained from previously sedentary, healthy men and women, aged 21–87 yr before ( n = 77) and after ( n = 65) 16 wk of bicycle training (up to 45 min at 80% peak heart rate, 3–4 days/wk). At baseline, MHC I mRNA was unchanged with age, whereas IIa and IIx declined by 14 and 10% per decade, respectively ( P < 0.001). MHC IIa and IIx protein declined by 3 and 1% per decade with a reciprocal increase in MHC I ( P < 0.05). After training, MHC I and IIa mRNA increased by 61 and 99%, respectively, and IIx decreased by 50% (all P < 0.001). The increase in MHC I mRNA was positively associated with age, whereas the changes in MHC IIa and IIx mRNA were similar across age. MHC I protein increased by 6% and was positively related to age, whereas IIx decreased by 5% and was inversely related to age. These results suggest that the altered expression of MHC isoforms with aging is transcriptionally regulated. In response to endurance exercise, regulation of MHC isoform transcripts remains robust in older muscle, but this did not result in corresponding changes in MHC protein expression.

scholarly journals Endurance Exercise Training Up-Regulates Lipolytic Proteins and Reduces Triglyceride Content in Skeletal Muscle of Obese Subjects

2013 ◽  
Vol 98 (12) ◽  
pp. 4863-4871 ◽  
Author(s):  
Katie Louche ◽  
Pierre-Marie Badin ◽  
Emilie Montastier ◽  
Claire Laurens ◽  
Virginie Bourlier ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Exercise Training ◽  
Protein Expression ◽  
Endurance Exercise ◽  
Oxidative Capacity ◽  
Metabolic Effects ◽  
Gene Identification ◽  
Mrna Levels ◽  
Endurance Exercise Training ◽  
Obese Subjects

Context: Skeletal muscle lipase and intramyocellular triglyceride (IMTG) play a role in obesity-related metabolic disorders. Objectives: The aim of the present study was to investigate the impact of 8 weeks of endurance exercise training on IMTG content and lipolytic proteins in obese male subjects. Design and Volunteers: Ten obese subjects completed an 8-week supervised endurance exercise training intervention in which vastus lateralis muscle biopsy samples were collected before and after training. Main Outcome Measures: Clinical characteristics and ex vivo substrate oxidation rates were measured pre- and posttraining. Skeletal muscle lipid content and lipolytic protein expression were also investigated. Results: Our data show that exercise training reduced IMTG content by 42% (P &lt; .01) and increased skeletal muscle oxidative capacity, whereas no change in total diacylglycerol content and glucose oxidation was found. Exercise training up-regulated adipose triglyceride lipase, perilipin (PLIN) 3 protein, and PLIN5 protein contents in skeletal muscle despite no change in mRNA levels. Training also increased hormone sensitive–lipase Ser660 phosphorylation. No significant changes in comparative gene identification 58, G0/G1 switch gene 2, and PLIN2 protein and mRNA levels were observed in response to training. Interestingly, we noted a strong relationship between skeletal muscle comparative gene identification 58 and mitochondrial respiratory chain complex I protein contents at baseline (r = 0.87, P &lt; .0001). Conclusions: Endurance exercise training coordinately up-regulates fat oxidative capacity and lipolytic protein expression in skeletal muscle of obese subjects. This physiological adaptation probably favors fat oxidation and may alleviate the lipotoxic lipid pressure in skeletal muscle. Enhancement of IMTG turnover may be required for the beneficial metabolic effects of exercise in obesity.

Histamine stimulates proliferation of airway smooth muscle and induces c-fos expression

1990 ◽  
Vol 259 (6) ◽  
pp. L365-L371 ◽  
Author(s):  
R. A. Panettieri ◽  
P. A. Yadvish ◽  
A. M. Kelly ◽  
N. A. Rubinstein ◽  
M. I. Kotlikoff
Keyword(s):  
Cell Proliferation ◽  
Smooth Muscle ◽  
Protein Expression ◽  
Myosin Heavy Chain ◽  
Airway Smooth Muscle ◽  
Heavy Chain ◽  
Thymidine Incorporation ◽  
Dependent Manner ◽  
Altered Expression ◽  
Mrna Induction

Although chronic severe asthma is characterized by increased smooth muscle mass in the airways, the physiological stimuli that promote airway smooth muscle (ASM) proliferation (hyperplasia) or increase ASM protein expression (hypertrophy) are unknown. We examined the effects of histamine, an autocoid associated with airway hyperresponsiveness, on protein synthesis, myosin heavy chain expression, and cell proliferation in cultured canine ASM cells. In confluent ASM cells, histamine significantly increased incorporation of [35S]-methionine in protein. Maintenance of the proportion of smooth muscle-specific myosin heavy chain to total myosin heavy chain suggested a nonspecific increase in contractile protein expression. DNA synthesis, as measured by [3H]thymidine incorporation, was significantly increased by histamine in a concentration-dependent manner. Cell proliferation paralleled [3H]thymidine incorporation; histamine significantly increased cell numbers at 24 and 48 h of stimulation. Because growth of mesenchymal-derived cells is associated with transcription of c-fos mRNA, we examined whether histamine altered expression of this proto-oncogene. Histamine-treated cells showed marked increases in expressions of steady-state c-fos mRNA, with a time course of mRNA induction similar to cells exposed to platelet-derived growth factor or serum, known smooth muscle and fibroblast cell mitogens. Therefore, histamine is an ASM mitogen with an action similar to other mesenchymal cell growth factors and may play a role in the hyperplasia of ASM in asthma.

scholarly journals Enhanced Fatty Acid Oxidation and FATP4 Protein Expression after Endurance Exercise Training in Human Skeletal Muscle

PLoS ONE ◽  
2012 ◽  
Vol 7 (1) ◽  
pp. e29391 ◽  
Author(s):  
Jacob Jeppesen ◽  
Andreas B. Jordy ◽  
Kim A. Sjøberg ◽  
Joachim Füllekrug ◽  
Andreas Stahl ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Fatty Acid ◽  
Exercise Training ◽  
Protein Expression ◽  
Fatty Acid Oxidation ◽  
Endurance Exercise ◽  
Human Skeletal Muscle ◽  
Acid Oxidation ◽  
Endurance Exercise Training

scholarly journals Dossier : Caractérisation des différents types de fibres musculaires dans plusieurs espèces : production et utilisation d’anticorps monoclonaux dirigés contre les chaînes lourdes de myosine rapide IIa et IIb

1998 ◽  
Vol 11 (2) ◽  
pp. 145-163 ◽  
Author(s):  
B. PICARD ◽  
L. LEFAUCHEUR ◽  
B. FAUCONNEAU ◽  
H. REMIGNON ◽  
Y. CHEREL ◽  
...  
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
De Novo ◽  
Mhc I ◽  
Muscle Squelettique ◽  
Anticorps Monoclonaux ◽  
Mhc Iia

Des anticorps monoclonaux dirigés contre les chaînes lourdes de myosine (MHC : myosin heavy chain) de différentes espèces d’animaux : bovin, porc, poisson, poulet, dinde, cheval ont été produits. Ils ont été testés par immunohistologie sur des coupes de muscle squelettique chez le bovin, le porc, le poisson, le poulet et la dinde et par ELISA chez le cheval. Les différents anticorps retenus dans ce projet permettent de nouvelles applications pour l’étude du muscle squelettique. En particulier deux anticorps monoclonaux peuvent être utilisés pour classer par immunohistologie les fibres IIA et IIB : l’un reconnaissant les MHC I et IIb chez le bovin et le cheval et les MHC I, IIb et IIx chez le porc, l’autre reconnaissant les MHC IIa et IIx chez le porc. D’autres anticorps ont permis de révéler une hétérogénéité dans la composition en myosine des fibres des muscles blanc et rouge de poisson, mais également dans la composition en myosine rapide des muscles de poulet et de dinde, sans toutefois permettre dans ces deux espèces une distinction précise des fibres IIA et IIB. De plus, chez la truite arc-en-ciel, un anticorps réagit plus spécifiquement contre les myosines des petites fibres témoins d’une myogénèse de novo dans le muscle blanc. Cependant il n’a pas été possible d’obtenir des anticorps spécifiques des fibres IIA et IIB utilisables en particulier en dosage ELISA ; cette obtention demeure un objectif important pour la poursuite des travaux.

Myosin heavy chain composition in young and old rat skeletal muscle: effects of endurance exercise

1995 ◽  
Vol 78 (6) ◽  
pp. 2115-2120 ◽  
Author(s):  
V. K. Sullivan ◽  
S. K. Powers ◽  
D. S. Criswell ◽  
N. Tumer ◽  
J. S. Larochelle ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Exercise Training ◽  
Myosin Heavy Chain ◽  
Succinate Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Endurance Exercise ◽  
Heavy Chain ◽  
Medial Gastrocnemius ◽  
Type I ◽  
Succinate Dehydrogenase Activity

The objective of this study was to determine the effects of age and exercise on the myosin heavy chain (MHC) composition of skeletal muscle. Young (3 mo) and old (22 mo) female specific pathogen-free barrier-reared Fischer 344 rats were randomly assigned to young untrained or young trained and old untrained or old trained groups, respectively. Young trained and old trained animals performed endurance exercise training on a motorized treadmill for 8 wk. Succinate dehydrogenase activity and MHC isoforms were measured in the plantaris (Plan), lateral and medial gastrocnemius (Gast), and soleus (Sol) muscles. In sedentary animals, aging resulted in a decrease (P < 0.05) in type IIb MHC and an increase (P < 0.05) in type IIa MHC in both the Gast and Plan muscles. Also, aging resulted in a small but significant increase (approximately 4%; P < 0.05) in type I MHC in the Sol. Exercise training resulted in significant (P < 0.05) increases in Gast, Plan, and Sol succinate dehydrogenase activity in both young and old animals. Furthermore, exercise training resulted in a decrease (P < 0.05) in the percentage of type IIb MHC and an increase (P < 0.05) in the percentage of type IIa MHC in the Plan in both young and old animals. These data suggest that there is an age-related shift in locomotor muscle MHC isoforms from a faster to a slower isoform.

Low-intensity exercise training during doxorubicin treatment protects against cardiotoxicity

2006 ◽  
Vol 100 (2) ◽  
pp. 519-527 ◽  
Author(s):  
Adam J. Chicco ◽  
David S. Hydock ◽  
Carole M. Schneider ◽  
Reid Hayward
Keyword(s):  
Lipid Peroxidation ◽  
Heat Shock ◽  
Exercise Training ◽  
Protein Expression ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Caspase 3 ◽  
Lv Function ◽  
Low Intensity ◽  
Low Intensity Exercise

Doxorubicin (Dox) is a highly effective antineoplastic antibiotic associated with a dose-limiting cardiotoxicity that may result in irreversible cardiomyopathy and heart failure. The purpose of this study was to examine the effects of low-intensity exercise training (LIET) during the course of Dox treatment on cardiac function, myosin heavy chain expression, oxidative stress, and apoptosis activation following treatment. Male Sprague-Dawley rats either remained sedentary or were exercise trained on a motorized treadmill at 15 m/min, 20 min/day, 5 days/wk (Monday through Friday) for 2 wk. During the same 2-wk period, Dox (2.5 mg/kg) or saline was administered intraperitoneally to sedentary and exercised rats 3 days/wk (Monday, Wednesday, Friday) 1–2 h following the exercise training sessions (cumulative Dox dose: 15 mg/kg). Five days following the final injections, hearts were isolated for determination of left ventricular (LV) function, lipid peroxidation, antioxidant enzyme protein expression, 72-kDa heat shock protein expression, caspase-3 activity, and myosin heavy chain isoform expression. Dox treatment significantly impaired LV function and increased caspase-3 activity in sedentary animals ( P < 0.05). LIET attenuated the LV dysfunction and apoptotic signal activation induced by Dox treatment and increased glutathione peroxidase expression, but it had no significant effect on lipid peroxidation, protein expression of myosin heavy chain isoforms, 72-kDa heat shock protein, or superoxide dismutase isoforms. In conclusion, our data suggest that LIET applied during chronic Dox treatment protects against cardiac dysfunction following treatment, possibly by enhancing antioxidant defenses and inhibiting apoptosis.

scholarly journals Role of intrinsic aerobic capacity and ventilator-induced diaphragm dysfunction

2015 ◽  
Vol 118 (7) ◽  
pp. 849-857 ◽  
Author(s):  
Kurt J. Sollanek ◽  
Ashley J. Smuder ◽  
Michael P. Wiggs ◽  
Aaron B. Morton ◽  
Lauren G. Koch ◽  
...  
Keyword(s):  
Exercise Training ◽  
Endurance Exercise ◽  
Aerobic Capacity ◽  
Citrate Synthase ◽  
Contractile Function ◽  
Prolonged Mechanical Ventilation ◽  
Diaphragm Muscle ◽  
Oxidative Enzymes ◽  
Diaphragm Dysfunction ◽  
Endurance Exercise Training

Prolonged mechanical ventilation (MV) leads to rapid diaphragmatic atrophy and contractile dysfunction, which is collectively termed “ventilator-induced diaphragm dysfunction” (VIDD). Interestingly, endurance exercise training prior to MV has been shown to protect against VIDD. Further, recent evidence reveals that sedentary animals selectively bred to possess a high aerobic capacity possess a similar skeletal muscle phenotype to muscles from endurance trained animals. Therefore, we tested the hypothesis that animals with a high intrinsic aerobic capacity would naturally be afforded protection against VIDD. To this end, animals were selectively bred over 33 generations to create two divergent strains, differing in aerobic capacity: high-capacity runners (HCR) and low-capacity runners (LCR). Both groups of animals were subjected to 12 h of MV and compared with nonventilated control animals within the same strains. As expected, contrasted to LCR animals, the diaphragm muscle from the HCR animals contained higher levels of oxidative enzymes (e.g., citrate synthase) and antioxidant enzymes (e.g., superoxide dismutase and catalase). Nonetheless, compared with nonventilated controls, prolonged MV resulted in significant diaphragmatic atrophy and impaired diaphragm contractile function in both the HCR and LCR animals, and the magnitude of VIDD did not differ between strains. In conclusion, these data demonstrate that possession of a high intrinsic aerobic capacity alone does not afford protection against VIDD. Importantly, these results suggest that endurance exercise training differentially alters the diaphragm phenotype to resist VIDD. Interestingly, levels of heat shock protein 72 did not differ between strains, thus potentially representing an important area of difference between animals with intrinsically high aerobic capacity and exercise-trained animals.

scholarly journals Effect of 6 months of GH treatment on myosin heavy chain composition in GH-deficient patients

1999 ◽  
pp. 342-349 ◽  
Author(s):  
◽  
M Bramnert ◽  
P Manhem ◽  
T Endre ◽  
LC Groop ◽  
...  
Keyword(s):  
Body Composition ◽  
Physical Fitness ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
The Body ◽  
Vastus Lateralis Muscle ◽  
Mhc I ◽  
Significant Difference ◽  
Igf I ◽  
Mhc Iia

OBJECTIVE: To investigate the effect of GH on myosin heavy chain (MHC) isoform composition, physical fitness and body composition in GH-deficient (GHD) patients. DESIGN: Twenty-two GHD patients were randomized in a double blind manner and half were treated with recombinant human GH (rhGH) and half were treated with placebo for 6 months. Twelve age-matched controls were also included in the study. METHODS: MHC isoform composition in biopsies obtained from the vastus lateralis muscle was determined using SDS-PAGE. Physical fitness was determined on a bicycle ergometer and body composition was determined using bioelectrical impedance analysis. RESULTS: More MHC IIX (28.9 +/- 4.1% and 10.0 +/- 3.1% in GHD and controls respectively (means +/- S.E.M.)) and less MHC I (36.2 +/- 2.4% and 51.7 +/- 3.9% in GHD and controls respectively (means +/- S.E.M.)) were present in the GHD patients compared with the controls. No significant difference in the amount of MHC IIA was detected. Linear regression was used to determine the relationship between variables. There were no significant relationships between the concentration of insulin-like growth factor-I (IGF-I) or the body composition and the MHC composition. Maximal oxygen uptake (VO(2)max) per kg body weight (BW) (litres/min per kg) correlated significantly with the amount of MHC I (r=0.60) and MHC IIX (r=-0.72) but not with the amount of MHC IIA (r=0.35). Treatment of GHD patients with rhGH for 6 months increased the concentration of IGF-I, lean body mass and decreased fat mass but had no effect on MHC composition and physical fitness. CONCLUSIONS: We conclude that a major part of the differences in MHC composition between GHD patients and age-matched controls can be explained by variation in physical fitness. The severity of the GHD and the body composition does not seem to be important for the MHC composition. Furthermore, treatment with GH for 6 months does not affect MHC composition in GHD patients.

scholarly journals A screen for genetic loci required for body-wall muscle development during embryogenesis in Caenorhabditis elegans.

Genetics ◽  
1994 ◽  
Vol 137 (2) ◽  
pp. 483-498
Author(s):  
J Ahnn ◽  
A Fire
Keyword(s):  
Caenorhabditis Elegans ◽  
Myosin Heavy Chain ◽  
Muscle Cell ◽  
Heavy Chain ◽  
Body Wall ◽  
Muscle Development ◽  
Contractile Function ◽  
The Body ◽  
Body Wall Muscle ◽  
Genetic Loci

Abstract We have used available chromosomal deficiencies to screen for genetic loci whose zygotic expression is required for formation of body-wall muscle cells during embryogenesis in Caenorhabditis elegans. To test for muscle cell differentiation we have assayed for both contractile function and the expression of muscle-specific structural proteins. Monoclonal antibodies directed against two myosin heavy chain isoforms, the products of the unc-54 and myo-3 genes, were used to detect body-wall muscle differentiation. We have screened 77 deficiencies, covering approximately 72% of the genome. Deficiency homozygotes in most cases stain with antibodies to the body-wall muscle myosins and in many cases muscle contractile function is observed. We have identified two regions showing distinct defects in myosin heavy chain gene expression. Embryos homozygous for deficiencies removing the left tip of chromosome V fail to accumulate the myo-3 and unc-54 products, but express antigens characteristic of hypodermal, pharyngeal and neural development. Embryos lacking a large region on chromosome III accumulate the unc-54 product but not the myo-3 product. We conclude that there exist only a small number of loci whose zygotic expression is uniquely required for adoption of a muscle cell fate.

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