scholarly journals Light‐load resistance exercise increases and prolongs the elevation in myofibrillar protein synthesis rate in human skeletal muscle induced by continuous protein feeding

2011 ◽  
Vol 25 (S1) ◽  
Author(s):  
Lars Holm ◽  
Rasmus Bechshoeft ◽  
Kasper J Dideriksen ◽  
Soeren Reitelseder ◽  
Michael Kjaer
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Human Skeletal Muscle ◽  
Load Resistance ◽  
Myofibrillar Protein ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Light Load ◽  
Protein Feeding ◽  
Myofibrillar Protein Synthesis

Polyadenylated RNA, actin mRNA, and myosin heavy chain mRNA in young and old human skeletal muscle

1996 ◽  
Vol 270 (2) ◽  
pp. E224-E229 ◽  
Author(s):  
S. Welle ◽  
K. Bhatt ◽  
C. Thornton
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Human Skeletal Muscle ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Type I ◽  
Polyadenylated Rna ◽  
Actin Mrna

The myofibrillar protein synthesis rate in old human skeletal muscle is slower than that in young adult muscle. To examine whether this difference in protein synthesis rate is explained by reduced availability of the mRNAs that encode the most abundant myofibrillar proteins, we determined relative hybridization signals from probes for actin mRNA, myosin heavy chain mRNA, and total polyadenylated RNA in vastus lateralis muscle biopsies taken from young (22- to 31-yr-old) and old (61- to 74-yr-old) human subjects. The mean fractional rate of myofibrillar synthesis was 38% slower in the older muscles, as determined by incorporation of a stable isotope tracer. Total actin and myosin heavy chain mRNAs, and polyadenylated RNA, were determined using slot-blot assays. Isoform-specific determinations of alpha-actin mRNA, type I myosin heavy chain mRNA, and type IIa myosin heavy chain mRNA were done with ribonuclease protection assays. Hybridization signals were expressed relative to tissue DNA content. There was no difference between age groups in total polyadenylated RNA or in any of the specific mRNAs. We conclude that the slower myofibrillar synthesis rate in older muscle is not caused by reduced mRNA availability.

scholarly journals Stimulation of skeletal muscle myofibrillar protein synthesis, p70 S6 kinase phosphorylation, and ribosomal protein S6 phosphorylation by inhibition of myostatin in mature mice

2009 ◽  
Vol 296 (3) ◽  
pp. E567-E572 ◽  
Author(s):  
Stephen Welle ◽  
Kerri Burgess ◽  
Sangeeta Mehta
Keyword(s):  
Protein Synthesis ◽  
Ribosomal Protein ◽  
Myofibrillar Protein ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
S6 Kinase ◽  
P70 S6 Kinase ◽  
Ribosomal Protein S6 ◽  
The Mean ◽  
Myofibrillar Protein Synthesis

Knocking out myostatin activity during development increases the rate of muscle protein synthesis. The present study was done to determine whether postdevelopmental loss of myostatin activity stimulates myofibrillar protein synthesis and the phosphorylation of some of the proteins involved in regulation of protein synthesis rate. Myostatin activity was inhibited for 4 days, in 4- to 5-mo-old male mice, with injections of an anti-myostatin antibody (JA16). The mean myofibrillar synthesis rate increased 19% ( P < 0.01) relative to the mean rate in saline-treated mice, as determined by incorporation of deuterium-labeled phenylalanine. JA16 increased phosphorylation of p70 S6 kinase (S6K) and ribosomal protein S6 (rpS6) 1.9-fold ( P < 0.05). It did not affect phosphorylation of eukaryotic initiation factor 4E-binding protein-1 or Akt. Microarrays and real-time PCR analyses indicated that JA16 administration did not selectively enrich levels of mRNAs encoding myofibrillar proteins, ribosomal proteins, or translation initiation and elongation factors. Rapamycin treatment did not affect the rate of myofibrillar protein synthesis whether or not the mice received JA16 injections, although it eliminated the phosphorylation of S6K and rpS6. We conclude that the normal level of myostatin activity in mature muscle is sufficient to inhibit myofibrillar synthesis rate and phosphorylation of S6K and rpS6. Reversal of the inhibition of myofibrillar synthesis with an anti-myostatin antibody is not dependent on mTOR activation.

scholarly journals Essential Amino Acid-Enriched Diet Alleviates Dexamethasone-Induced Loss of Muscle Mass and Function through Stimulation of Myofibrillar Protein Synthesis and Improves Glucose Metabolism in Mice

Metabolites ◽  
2022 ◽  
Vol 12 (1) ◽  
pp. 84
Author(s):  
Yeongmin Kim ◽  
Sanghee Park ◽  
Jinseok Lee ◽  
Jiwoong Jang ◽  
Jiyeon Jung ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Glucose Metabolism ◽  
Muscle Mass ◽  
Muscle Atrophy ◽  
Myofibrillar Protein ◽  
Treadmill Running ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Myofibrillar Protein Synthesis ◽  
Stimulation Of

Dexamethasone (DEX) induces dysregulation of protein turnover, leading to muscle atrophy and impairment of glucose metabolism. Positive protein balance, i.e., rate of protein synthesis exceeding rate of protein degradation, can be induced by dietary essential amino acids (EAAs). In this study, we investigated the roles of an EAA-enriched diet in the regulation of muscle proteostasis and its impact on glucose metabolism in the DEX-induced muscle atrophy model. Mice were fed normal chow or EAA-enriched chow and were given daily injections of DEX over 10 days. We determined muscle mass and functions using treadmill running and ladder climbing exercises, protein kinetics using the D2O labeling method, molecular signaling using immunoblot analysis, and glucose metabolism using a U-13C6 glucose tracer during oral glucose tolerance test (OGTT). The EAA-enriched diet increased muscle mass, strength, and myofibrillar protein synthesis rate, concurrent with improved glucose metabolism (i.e., reduced plasma insulin concentrations and increased insulin sensitivity) during the OGTT. The U-13C6 glucose tracing revealed that the EAA-enriched diet increased glucose uptake and subsequent glycolytic flux. In sum, our results demonstrate a vital role for the EAA-enriched diet in alleviating the DEX-induced muscle atrophy through stimulation of myofibrillar proteins synthesis, which was associated with improved glucose metabolism.

Minor surgery has no immediate effect on protein synthesis rate in human skeletal muscle

1993 ◽  
Vol 12 ◽  
pp. 7
Author(s):  
I. Tjäder ◽  
P. Essén ◽  
A. Thörne ◽  
M.A. McNurlan ◽  
G. Calder ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Human Skeletal Muscle ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Minor Surgery

Protein synthesis rate in human skeletal muscle decreases three days after abdominal surgery

1990 ◽  
Vol 9 ◽  
pp. 54
Author(s):  
P. Essén ◽  
M.A. McNurlan ◽  
J. Wernerman ◽  
E. Vinnars ◽  
P.J. Garlick
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Abdominal Surgery ◽  
Human Skeletal Muscle ◽  
Synthesis Rate ◽  
Protein Synthesis Rate
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