Effect of endurance exercise on myosin heavy chain gene regulation in human skeletal muscle

1999 ◽  
Vol 276 (2) ◽  
pp. R414-R419 ◽  
Author(s):  
D. Sean O’Neill ◽  
Donghai Zheng ◽  
Wade K. Anderson ◽  
G. Lynis Dohm ◽  
Joseph A. Houmard
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Human Skeletal Muscle ◽  
Contractile Activity ◽  
Maximal Oxygen Consumption ◽  
Exercise Bout ◽  
Cycle Ergometer ◽  
Chain Gene ◽  
Exercise Period

The purpose of this study was to determine the effect of endurance-oriented exercise on myosin heavy chain (MHC) isoform regulation in human skeletal muscle. Exercise consisted of 1 h of cycle ergometer work per day at 75% maximal oxygen consumption for seven consecutive days. Muscle was obtained before the first bout of exercise, 3 h after the first bout of exercise, and before and 3 h after the final exercise bout on day 7( n = 9 subjects). No changes in MHC mRNA (I, IIa, IIx) were evident after the first exercise period. There was, however, a significant ( P < 0.05) decline (−30%) in MHC IIx mRNA 3 h after the final training bout. An interesting finding was that a higher pretraining level of MHC IIx mRNA was associated with a greater decline in the transcript before ( r = 0.68, P < 0.05) and 3 h after ( r = 0.82, P < 0.05) the final exercise bout. These findings suggest that MHC IIx mRNA is downregulated during the early phase of endurance-oriented exercise training in human skeletal muscle but only after repeated contractile activity. Pretraining MHC IIx mRNA content may influence the magnitude of this response.

Impact of hyperinsulinemia on myosin heavy chain gene regulation

1999 ◽  
Vol 86 (6) ◽  
pp. 1828-1832 ◽  
Author(s):  
Joseph A. Houmard ◽  
D. Sean O’Neill ◽  
Donghai Zheng ◽  
Matthew S. Hickey ◽  
G. Lynis Dohm
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Human Skeletal Muscle ◽  
Vastus Lateralis ◽  
Chain Gene ◽  
Type I ◽  
Myosin Heavy Chain Gene ◽  
Mrna Concentration ◽  
Before And After

The purpose of this study was to determine whether hyperinsulinemia alters myosin heavy chain (MHC) gene expression in human skeletal muscle. A biopsy from the vastus lateralis was obtained in young, lean [age 24.6 ± 1.0 (SE) yr, body fat 11.9 ± 1.9%, body mass index 26.1 ± 1.1 kg/m2; n = 10] men before and after 3 h of hyperinsulinemia (hyperinsulinemic-euglycemic clamp). Muscle was analyzed for mRNA of type I, IIa, and IIx MHC isoforms. Hyperinsulinemia (mean of 1,065.7 ± 9.8 pmol/l during minutes 20 to 180) did not change ( P > 0.05) the mRNA concentration of either the type I MHC or type IIA MHC isoforms. In contrast, type IIX MHC mRNA increased ( P < 0.05) with hyperinsulinemia compared with the fasted condition. These data indicate that hyperinsulinemia rapidly increases type IIx MHC mRNA in human skeletal muscle.

Differential patterns of transcript accumulation during human myogenesis

1987 ◽  
Vol 7 (11) ◽  
pp. 4100-4114
Author(s):  
P Gunning ◽  
E Hardeman ◽  
R Wade ◽  
P Ponte ◽  
W Bains ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Carbonic Anhydrase ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Time Course ◽  
Human Skeletal Muscle ◽  
Transcript Accumulation ◽  
Mrna Accumulation ◽  
Adult Human ◽  
Alpha Actin

We evaluated the extent to which muscle-specific genes display identical patterns of mRNA accumulation during human myogenesis. Cloned satellite cells isolated from adult human skeletal muscle were expanded in culture, and RNA was isolated from low- and high-confluence cells and from fusing cultures over a 15-day time course. The accumulation of over 20 different transcripts was compared in these samples with that in fetal and adult human skeletal muscle. The expression of carbonic anhydrase 3, myoglobin, HSP83, and mRNAs encoding eight unknown proteins were examined in human myogenic cultures. In general, the expression of most of the mRNAs was induced after fusion to form myotubes. However, several exceptions, including carbonic anhydrase and myoglobin, showed no detectable expression in early myotubes. Comparison of all transcripts demonstrated little, if any, identity of mRNA accumulation patterns. Similar variability was also seen for mRNAs which were also expressed in nonmuscle cells. Accumulation of mRNAs encoding alpha-skeletal, alpha-cardiac, beta- and gamma-actin, total myosin heavy chain, and alpha- and beta-tubulin also displayed discordant regulation, which has important implications for sarcomere assembly. Cardiac actin was the only muscle-specific transcript that was detected in low-confluency cells and was the major alpha-actin mRNA at all times in fusing cultures. Skeletal actin was transiently induced in fusing cultures and then reduced by an order of magnitude. Total myosin heavy-chain mRNA accumulation lagged behind that of alpha-actin. Whereas beta- and gamma-actin displayed a sharp decrease after initiation of fusion and thereafter did not change, alpha- and beta-tubulin were transiently induced to a high level during the time course in culture. We conclude that each gene may have its own unique determinants of transcript accumulation and that the phenotype of a muscle may not be determined so much by which genes are active or silent but rather by the extent to which their transcript levels are modulated. Finally, we observed that patterns of transcript accumulation established within the myotube cultures were consistent with the hypothesis that myoblasts isolated from adult tissue recapitulate a myogenic developmental program. However, we also detected a transient appearance of adult skeletal muscle-specific transcripts in high-confluence myoblast cultures. This indicates that the initial differentiation of these myoblasts may reflect a more complex process than simple recapitulation of development.

scholarly journals Mutation of the IIB myosin heavy chain gene results in muscle fiber loss and compensatory hypertrophy

2001 ◽  
Vol 280 (3) ◽  
pp. C637-C645 ◽  
Author(s):  
David L. Allen ◽  
Brooke C. Harrison ◽  
Carol Sartorius ◽  
William C. Byrnes ◽  
Leslie A. Leinwand
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Body Mass ◽  
Heavy Chain ◽  
Compensatory Hypertrophy ◽  
Muscle Disease ◽  
Chain Gene ◽  
Fiber Types ◽  
Mouse Skeletal Muscle ◽  
Ultrastructural Studies

The fast skeletal IIb gene is the source of most myosin heavy chain (MyHC) in adult mouse skeletal muscle. We have examined the effects of a null mutation in the IIb MyHC gene on the growth and morphology of mouse skeletal muscle. Loss in muscle mass of several head and hindlimb muscles correlated with amounts of IIb MyHC expressed in that muscle in wild types. Decreased mass was accompanied by decreases in mean fiber number, and immunological and ultrastructural studies revealed fiber pathology. However, mean cross-sectional area was increased in all fiber types, suggesting compensatory hypertrophy. Loss of muscle and body mass was not attributable to impaired chewing, and decreased food intake as a softer diet did not prevent the decrease in body mass. Thus loss of the major MyHC isoform produces fiber loss and fiber pathology reminiscent of muscle disease.

Improving human skeletal muscle myosin heavy chain fiber typing efficiency

2016 ◽  
Vol 37 (1-2) ◽  
pp. 1-5 ◽  
Author(s):  
Kevin A. Murach ◽  
James R. Bagley ◽  
Kathryn A. McLeland ◽  
Jose A. Arevalo ◽  
Anthony B. Ciccone ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Human Skeletal Muscle ◽  
Skeletal Muscle Myosin ◽  
Muscle Myosin

scholarly journals Isolation of human skeletal muscle myosin heavy chain and actin for measurement of fractional synthesis rates

1998 ◽  
Vol 275 (6) ◽  
pp. E1092-E1099 ◽  
Author(s):  
D. L. Hasten ◽  
G. S. Morris ◽  
S. Ramanadham ◽  
K. E. Yarasheski
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Human Skeletal Muscle ◽  
Sodium Dodecyl ◽  
Synthesis Rate ◽  
Simple Method ◽  
Skeletal Muscle Myosin ◽  
Fractional Synthesis

Using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), we have developed a simple method to isolate myosin heavy chain (MHC) and actin from small (60–80 mg) human skeletal muscle samples for the determination of their fractional synthesis rates. The amounts of MHC and actin isolated are adequate for the quantification of [13C]leucine abundance by gas chromatography-combustion-isotope ratio mass spectrometry (GC-C-IRMS). Fractional synthesis rates of mixed muscle protein (MMP), MHC, and actin were determined in six healthy young subjects (27 ± 1 yr) after they received a 14-h intravenous infusion (prime = 7.58 μmol/kg body wt, constant infusion = 7.58 μmol ⋅ kg body wt−1 ⋅ h−1) of [1-13C]leucine. The fractional synthesis rates of MMP, MHC, and actin were found to be 0.0468 ± 0.0048, 0.0376 ± 0.0033, and 0.0754 ± 0.0078%/h, respectively. Overall, the synthesis rate of MHC was 20% lower ( P = 0.012), and the synthesis rate of actin was 61% higher ( P = 0.060, not significant) than the MMP synthesis rate. The isolation of these proteins for isotope abundance analysis by GC-C-IRMS provides important information about the synthesis rates of these specific contractile proteins, as opposed to the more general information provided by the determination of MMP synthesis rates.

Relationships between maximal strength, muscle size, and myosin heavy chain isoform composition and postactivation potentiation

2016 ◽  
Vol 41 (5) ◽  
pp. 491-497 ◽  
Author(s):  
Laurent B. Seitz ◽  
Gabriel S. Trajano ◽  
G. Gregory Haff ◽  
Charles C.L.S. Dumke ◽  
James J. Tufano ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Human Skeletal Muscle ◽  
Knee Extensor ◽  
Type Ii ◽  
Postactivation Potentiation ◽  
Test Protocol ◽  
Extensor Torque ◽  
Type Ii Myosin

The purpose of this study was to examine the relationships between maximal voluntary postactivation potentiation (PAP) and maximal knee extensor torque, quadriceps cross-sectional area (CSA) and volume, and type II myosin heavy chain (MHC) isoform percentage in human skeletal muscle. Thirteen resistance-trained men completed a test protocol consisting of 2 isokinetic knee extensions at 180°·s–1 performed before and 1, 4, 7, and 10 min after the completion of 4 maximal knee extensions at 60°·s–1 (i.e., a conditioning activity (CA)). Magnetic resonance imaging and muscle microbiopsy procedures were completed on separate days to assess quadriceps CSA and volume and MHC isoform content. Maximal voluntary PAP response was assessed as the ratio of the highest knee extensor torques measured before and after the CA. There were large to very large correlations between maximal voluntary PAP response and maximal knee extensor torque (r = 0.62) and quadriceps CSA (r = 0.68) and volume (r = 0.63). Nonetheless, these correlations were not statistically significant after adjusting for the influence of type II MHC percentage using partial correlation analysis. By contrast, the strongest correlation was observed for type II MHC percentage (r = 0.77), and this correlation remained significant after adjusting for the other variables. Maximal voluntary PAP response is strongly correlated with maximal knee extensor torque and quadriceps CSA and volume, but is mostly clearly associated with the type II myosin isoform percentage in human skeletal muscle.

Sign in / Sign up

Export Citation Format

Share Document