Relevant bibliographies by topics / Myofibrillar protein synthesis

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Academic literature on the topic 'Myofibrillar protein synthesis'

Author: Grafiati
Published: 10 January 2023
Last updated: 28 January 2023

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Journal articles on the topic "Myofibrillar protein synthesis"

1

Fiorotto, Marta L., Teresa A. Davis, and Peter J. Reeds. "Regulation of myofibrillar protein turnover during maturation in normal and undernourished rat pups." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 278, no. 4 (April 1, 2000): R845—R854. http://dx.doi.org/10.1152/ajpregu.2000.278.4.r845.

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The study tested the hypothesis that a higher rate of myofibrillar than sarcoplasmic protein synthesis is responsible for the rapid postdifferentiation accumulation of myofibrils and that an inadequate nutrient intake will compromise primarily myofibrillar protein synthesis. Myofibrillar (total and individual) and sarcoplasmic protein synthesis, accretion, and degradation rates were measured in vivo in well-nourished (C) rat pups at 6, 15, and 28 days of age and compared at 6 and 15 days of age with pups undernourished (UN) from birth. In 6-day-old C pups, a higher myofibrillar than sarcoplasmic protein synthesis rate accounted for the greater deposition of myofibrillar than sarcoplasmic proteins. The fractional synthesis rates of both protein compartments decreased with age, but to a greater degree for myofibrillar proteins (−54 vs. −42%). These decreases in synthesis rates were partially offset by reductions in degradation rates, and from 15 days, myofibrillar and sarcoplasmic proteins were deposited in constant proportion to one another. Undernutrition reduced both myofibrillar and sarcoplasmic protein synthesis rates, and the effect was greater at 6 (−25%) than 15 days (−15%). Decreases in their respective degradation rates minimized the effect of undernutrition on sarcoplasmic protein accretion from 4 to 8 days and on myofibrillar proteins from 13 to 17 days. Although these adaptations in protein turnover reduced overall growth of muscle mass, they mitigated the effects of undernutrition on the normal maturational changes in myofibrillar protein concentration.
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2

Welle, S., C. Thornton, R. Jozefowicz, and M. Statt. "Myofibrillar protein synthesis in young and old men." American Journal of Physiology-Endocrinology and Metabolism 264, no. 5 (May 1, 1993): E693—E698. http://dx.doi.org/10.1152/ajpendo.1993.264.5.e693.

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We tested the hypothesis that healthy older men (> 60 yr old) have a slower rate of myofibrillar protein synthesis than young men (< 35 yr old). Myofibrillar protein synthesis was determined by the in vivo incorporation of L-[1-13C]leucine into myofibrillar proteins obtained by muscle biopsy. Subjects were eight young (21-31 yr) and eight older (62-81 yr) men, all healthy and moderately active. There was no significant difference in the mean height and weight of the two age groups, but the older group had 12% less lean body mass (determined by 40K counting) and 21% less muscle mass (estimated by urinary creatinine excretion). Upper leg strength was approximately one-third lower in the older subjects according to isokinetic dynamometry. The fractional rate of myofibrillar protein synthesis was 28% slower in the older group (0.039 +/- 0.009 vs. 0.054 +/- 0.010 %/h, mean +/- SD, P < 0.01). Total myofibrillar protein synthesis, estimated as total myofibrillar mass (from creatinine excretion) times the fractional synthesis rate, was 44% slower in the older group (1.4 vs. 2.5 g/h, P < 0.001). Whole body protein synthesis, assessed as the difference between leucine disappearance rate and leucine oxidation, was marginally slower (8%, P = 0.10) in the older group, but not when the data were adjusted for lean body mass. Myofibrillar protein synthesis was a smaller fraction of whole body protein synthesis in the older group (12 vs. 19%). Reduced myofibrillar protein synthesis may be an important mechanism of the muscle atrophy associated with aging.
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Welle, Stephen, Kerri Burgess, and Sangeeta Mehta. "Stimulation of skeletal muscle myofibrillar protein synthesis, p70 S6 kinase phosphorylation, and ribosomal protein S6 phosphorylation by inhibition of myostatin in mature mice." American Journal of Physiology-Endocrinology and Metabolism 296, no. 3 (March 2009): E567—E572. http://dx.doi.org/10.1152/ajpendo.90862.2008.

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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.
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Welle, S., C. Thornton, M. Statt, and B. McHenry. "Postprandial myofibrillar and whole body protein synthesis in young and old human subjects." American Journal of Physiology-Endocrinology and Metabolism 267, no. 4 (October 1, 1994): E599—E604. http://dx.doi.org/10.1152/ajpendo.1994.267.4.e599.

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Rates of incorporation of leucine (using L-[1-13C]leucine as a tracer) into myofibrillar and whole body proteins were determined in healthy old (> 60 yr old, n = 7) and young (< 30 yr old, n = 9) men and women who were fed small meals (4% of daily energy) every 30 min. There was no difference in whole body incorporation of leucine into proteins in the young (148 +/- 5 mumol.h-1.kg lean body mass-1, means +/- SE) and old groups (150 +/- 3 mumol.h-1.kg lean body mass-1). However, the fractional myofibrillar protein synthesis in the vastus lateralis muscle was 28% slower in the older group (0.063 +/- 0.004 vs. 0.088 +/- 0.003 %/h, P < 0.001). Extrapolation of these results to whole body myofibrillar synthesis (fractional rate x myofibrillar mass estimated by creatinine excretion) indicated that, in the older group, total myofibrillar synthesis was 43% slower (1.8 +/- 0.2 vs. 3.1 +/- 0.2 g/h, P < 0.01) and that their myofibrillar synthesis was a smaller portion of whole body protein synthesis (15 +/- 1 vs. 23 +/- 1%, P < 0.001). Compared with age-matched postabsorptive subjects, whole body protein synthesis was approximately 25% faster, and fractional myofibrillar synthesis was approximately 50% faster in these fed subjects, both young and old. We conclude that myofibrillar synthesis is slower in older subjects during both postabsorptive and postprandial conditions but that aging does not impair the stimulatory effect of feeding on protein synthesis.
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Welle, Stephen, Sangeeta Mehta, and Kerri Burgess. "Effect of postdevelopmental myostatin depletion on myofibrillar protein metabolism." American Journal of Physiology-Endocrinology and Metabolism 300, no. 6 (June 2011): E993—E1001. http://dx.doi.org/10.1152/ajpendo.00509.2010.

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It is unclear whether the muscle hypertrophy induced by loss of myostatin signaling in mature muscles is maintained only by increased protein synthesis or whether reduced proteolysis contributes. To address this issue, we depleted myostatin by activating Cre recombinase for 2 wk in mature mice in which Mstn exon 3 was flanked by loxP sequences. The rate of phenylalanine tracer incorporation into myofibrillar proteins was determined 2, 5, and 24 wk after Cre activation ended. At all of these time points, myostatin-deficient mice had increased gastrocnemius and quadriceps muscle mass (≥27%) and increased myofibrillar synthesis rate per gastrocnemius muscle (≥19%) but normal myofibrillar synthesis rates per myofibrillar mass or RNA mass. Mean fractional myofibrillar degradation rates (estimated from the difference between rate of synthesis and rate of change in myofibrillar mass) and muscle concentrations of free 3-methylhistidine (from actin and myosin degradation) were unaffected by myostatin knockout. Overnight food deprivation reduced myofibrillar synthesis and ribosomal protein S6 phosphorylation and increased concentrations of 3-methylhistidine, muscle RING finger-1 mRNA, and atrogin-1 mRNA. Myostatin depletion did not affect these responses to food deprivation. These data indicate that maintenance of the muscle hypertrophy caused by loss of myostatin is mediated by increased protein synthesis per muscle fiber rather than suppression of proteolysis.
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Welle, Stephen, and Charles A. Thornton. "High-protein meals do not enhance myofibrillar synthesis after resistance exercise in 62- to 75-yr-old men and women." American Journal of Physiology-Endocrinology and Metabolism 274, no. 4 (April 1, 1998): E677—E683. http://dx.doi.org/10.1152/ajpendo.1998.274.4.e677.

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This study tested the hypothesis that increasing the protein content of isocaloric meals increases the rate of myofibrillar synthesis in muscle of healthy subjects over 60 yr old and enhances the stimulation of myofibrillar synthesis induced by resistance exercise. Myofibrillar synthesis of sedentary and exercised quadriceps muscle was determined by incorporation ofl-[1-13C]leucine. During the tracer infusion, subjects consumed meals with a low (7% of energy, n = 6)-, normal (14%, n = 6)-, or high (28%, n = 6)-protein content. In sedentary muscle, the mean (± SE) myofibrillar synthesis was 1.56 ± 0.13%/day in the low-protein group, 1.73 ± 0.11 %/day in the normal-protein group, and 1.76 ± 0.10%/day in the high-protein group ( P = 0.42). Myofibrillar synthesis was faster in exercised muscle (mean 27%, P < 10−6) in all groups (2.10 ± 0.14 %/day in low protein; 2.18 ± 0.10 %/day in normal protein; 2.11 ± 0.09 %/day in high protein; P = 0.84). The stimulation of myofibrillar synthesis by exercise was not significantly different among low-protein [0.54 ± 0.12 %/day (37 ± 9%)], normal-protein [0.46 ± 0.08 %/day (28 ± 5%)], and high-protein groups [0.34 ± 0.04 %/day (20 ± 3%); P = 0.31]. We conclude that high-protein meals do not enhance the stimulation of myofibrillar protein synthesis induced by resistance exercise.
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7

Welle, S., C. Thornton, and M. Statt. "Myofibrillar protein synthesis in young and old human subjects after three months of resistance training." American Journal of Physiology-Endocrinology and Metabolism 268, no. 3 (March 1, 1995): E422—E427. http://dx.doi.org/10.1152/ajpendo.1995.268.3.e422.

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Muscle protein synthesis is slower in healthy older men and women than in young adults, but whether this results from relative disuse rather than aging is unclear. The present study was done to examine rates of myofibrillar protein synthesis before and after a 3-mo progressive resistance exercise program in young and old men and women. Protein synthesis was determined by incorporation of the tracer L-[1-13C]leucine into myofibrillar proteins obtained from the vastus lateralis muscle by needle biopsy. Before exercise, mean fractional myofibrillar synthesis was 33% slower (P < 0.01) in nine older subjects (62-72 yr old, 5 men and 4 women) than in 9 young subjects (22-31 yr old, 5 men and 4 women). Initial strength, as determined by three-repetition-maximum tests, was significantly less in the older group. Strength and training weights increased similarly in young and old groups, when expressed in relation to baseline values. Posttraining myofibrillar synthesis was determined on the day after the final training session. There was not a significant change in fractional myofibrillar synthesis in either the young or the old group after training, and the rate in the older group remained 27% slower (P < 0.05). Whole body protein turnover increased approximately 10% only in the younger group, and 24-h urinary 3-methylhistidine excretion (an index of myofibrillar proteolysis) was not significantly affected by training. These data suggest that the slower myofibrillar synthesis rate in older subjects cannot be explained by disuse.
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8

Wall, Benjamin T., Nicholas A. Burd, Rinske Franssen, Stefan H. M. Gorissen, Tim Snijders, Joan M. Senden, Annemie P. Gijsen, and Luc J. C. van Loon. "Presleep protein ingestion does not compromise the muscle protein synthetic response to protein ingested the following morning." American Journal of Physiology-Endocrinology and Metabolism 311, no. 6 (December 1, 2016): E964—E973. http://dx.doi.org/10.1152/ajpendo.00325.2016.

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Protein ingestion before sleep augments postexercise muscle protein synthesis during overnight recovery. It is unknown whether postexercise and presleep protein consumption modulates postprandial protein handling and myofibrillar protein synthetic responses the following morning. Sixteen healthy young (24 ± 1 yr) men performed unilateral resistance-type exercise (contralateral leg acting as a resting control) at 2000. Participants ingested 20 g of protein immediately after exercise plus 60 g of protein presleep (PRO group; n = 8) or equivalent boluses of carbohydrate (CON; n = 8). The subsequent morning participants received primed, continuous infusions of l-[ ring-2H5]phenylalanine and l-[1-13C]leucine combined with ingestion of 20 g intrinsically l-[1-13C]phenylalanine- and l-[1-13C]leucine-labeled protein to assess postprandial protein handling and myofibrillar protein synthesis in the rested and exercised leg in CON and PRO. Exercise increased postabsorptive myofibrillar protein synthesis rates the subsequent day ( P < 0.001), with no differences between CON and PRO. Protein ingested in the morning increased myofibrillar protein synthesis in both the exercised and rested leg ( P < 0.01), with no differences between treatments. Myofibrillar protein bound l-[1-13C]phenylalanine enrichments were greater in the exercised (0.016 ± 0.002 and 0.015 ± 0.002 MPE in CON and PRO, respectively) vs. rested (0.010 ± 0.002 and 0.009 ± 0.002 MPE in CON and PRO, respectively) leg ( P < 0.05), with no differences between treatments ( P > 0.05). The additive effects of resistance-type exercise and protein ingestion on myofibrillar protein synthesis persist for more than 12 h after exercise and are not modulated by protein consumption during acute postexercise recovery. This work provides evidence of an extended window of opportunity where presleep protein supplementation can be an effective nutrient timing strategy to optimize skeletal muscle reconditioning.
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Preedy, V. R., and P. J. Garlick. "Inhibition of protein synthesis by glucagon in different rat muscles and protein fractions in vivo and in the perfused rat hemicorpus." Biochemical Journal 251, no. 3 (May 1, 1988): 727–32. http://dx.doi.org/10.1042/bj2510727.

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The effect of glucagon on the rate of muscle protein synthesis was examined in vivo and in the isolated perfused rat hemicorpus. An inhibition of protein synthesis in skeletal muscles from overnight-fasted rats at various plasma concentrations of glucagon was demonstrated in vivo. The plantaris muscle (Type II, fibre-rich) was more sensitive than the soleus (Type I, fibre-rich). Myofibrillar and sarcoplasmic proteins were equally sensitive in vivo. However, protein synthesis in mixed protein and in sarcoplasmic and myofibrillar fractions of the heart was unresponsive to glucagon in vivo. In isolated perfused muscle preparations from fed animals, the addition of glucagon also decreased the synthesis of mixed muscle proteins in gastrocnemius (Type I and II fibres) and plantaris, but not in the soleus. The sarcoplasmic and myofibrillar fractions of the plantaris were also equally affected in vitro. Similar results were observed in vitro with 1-day-starved rats, but the changes were less marked.
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Welle, Stephen, Kirti Bhatt, and Carl A. Pinkert. "Myofibrillar protein synthesis in myostatin-deficient mice." American Journal of Physiology-Endocrinology and Metabolism 290, no. 3 (March 2006): E409—E415. http://dx.doi.org/10.1152/ajpendo.00433.2005.

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Either increased protein synthesis or prolonged protein half-life is necessary to support the excessive muscle growth and maintenance of enlarged muscles in myostatin-deficient mice. This issue was addressed by determining in vivo rates of myofibrillar protein synthesis in mice with constitutive myostatin deficiency (MstnΔE3/ΔE3) or normal myostatin expression (Mstn+/+) by measuring tracer incorporation after a systemic flooding dose of l-[ ring-2H5]phenylalanine. At 5–6 wk of age, MstnΔE3/ΔE3 mice had increased muscle mass (40%), fractional rates of myofibrillar synthesis (14%), and protein synthesis per whole muscle (60%) relative to Mstn+/+ mice. With maturation, fractional rates of synthesis declined >50% in parallel with decreased DNA and RNA [total, 28S rRNA, and poly(A) RNA] concentrations in muscle. At 6 mo of age, MstnΔE3/ΔE3 mice had even greater increases in muscle mass (90%) and myofibrillar synthesis per muscle (85%) relative to Mstn+/+ mice, but the fractional rate of synthesis was normal. Estimated myofibrillar protein half-life was not affected by myostatin deficiency. Muscle DNA concentrations were reduced in both young and mature MstnΔE3/ΔE3 mice, whereas RNA concentrations were normal, so the ratio of RNA to DNA was ∼30% greater than normal in MstnΔE3/ΔE3 mice. Thus the increased protein synthesis and RNA content per muscle in myostatin-deficient mice cannot be explained entirely by an increased number of myonuclei.
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Dissertations / Theses on the topic "Myofibrillar protein synthesis"

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Kumar, Vinod. "Effects of resistance exercise (intensity and volume) with or without leucine enriched protein supplementation on human myofibrillar protein synthesis and cell anabolic signalling." Thesis, University of Nottingham, 2010. http://eprints.nottingham.ac.uk/11571/.

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Sarcopenia or the involuntary age associated muscle wasting starts in the fourth decade of life and accelerates markedly from the fifth decade. This gradual loss of muscle mass eventually results in an inability of older people to carry out simple daily tasks, instability, is associated with an increased risk of falls and fractures, loss of independence, and reduced quality of life. As the number of older people is growing steadily in our society, this in turn places an increasing burden on health care resources, making the topic of sarcopenia and its consequences an important area for research. Resistance exercise and protein enriched feeding are potent stimulators of MPS and act synergistically to increase the MPS; however, the muscle protein synthetic responses to amino acids are blunted in the elderly in the resting state. Leucine has been shown to be the most potent branched-chain amino acid acting as a signal for accelerating MPS in the resting state. How intensity and duration of resistance exercise can affect MPS and anabolic signalling in the elderly is less well understood. Can leucine enriched protein supplementation coupled with resistance exercise rejuvenate the MPS responses in the elderly? We aimed to answer these questions. The results revealed a sigmoidal dose-response relationship between exercise intensity and the stimulation of MPS in the post absorptive state, with little increase from 20-40% 1RM, then a bigger rise at 60 % of 1 RM with no significant further increase up to 90% 1RM in both the young and the elderly. Both groups showed quantitatively similar increases in phosphorylation of both p70s6K and 4E-BP1, which were maximal for exercise at 60-90% 1 RM at 1 h post exercise, i.e. just before the maximal increase in MPS. However, older men demonstrated a blunted rise in MPS and anabolic signalling activity after exercise, suggesting a general pattern of a reduced protein synthetic response to exercise in the elderly. This may explain, in part the mechanisms through which muscle is lost gradually with ageing. Increasing exercise volume from 3 to 6 sets at 40% and 75% 1RM produced no additional MPS responses in post absorptive young men; however, in older men, it resulted in enhanced MPS and p70S6K responses at both intensities, suggesting that the muscle of older men requires a greater volume of exercise to activate the protein synthetic machinery sufficiently to achieve synthetic responses comparable to those seen in younger men. Exercise, irrespective of intensity and volume caused only short term stimulation in MPS (returned to basal level at 4h post exercise) in the post absorptive state. Leucine supplementation to protein feeding after resistance exercise appeared to overcome age-related anabolic blunting of responses of myofibrillar protein synthesis and p70S6K phosphorylation in skeletal muscle of older men by rejuvenating their synthetic responses. In summary, the results gave a clear indication as to the likely optimal exercise intensity and volume of acute resistance exercise (6 sets of 8-10 reps at 75% 1RM) coupled with optimal amino acid supplementation (leucine supplemented drink containing about 20 g of protein) required to effectively stimulate MPS and anabolic signalling in the elderly for maintenance of muscle mass. This work helps shed light on the pathophysiology of sarcopenia and suggests strategies that could be used to develop effective countermeasures to counteract sarcopenia.
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Langer, Henning Tim [Verfasser]. "The effect of chronic constriction injury to the sciatic nerve on myofibrillar protein synthesis in rat tibialis anterior / Henning Tim Langer." Berlin : Medizinische Fakultät Charité - Universitätsmedizin Berlin, 2021. http://d-nb.info/1228861099/34.

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3

Saner, Nicholas. "Can exercise mitigate the negative metabolic effects associated with sleep loss?" Thesis, 2019. https://vuir.vu.edu.au/40011/.

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The increased time-demands imposed on modern society means that many people don’t meet nightly sleep recommendations. However, despite the obvious importance of sleep for the maintenance of good health, the effects of sleep loss are remarkably understudied. The consequences of sleep loss on aspects of metabolic health are becoming more apparent, with detrimental changes to glucose tolerance, insulin sensitivity, and an increased risk of numerous metabolic conditions being reported. Comparatively, the underlying mechanisms that lead to these changes are not well characterised, but may include circadian misalignment, changes in mitochondrial function, and inhibition of the molecular signalling pathways that govern protein synthesis. Due to the emergence of these detrimental metabolic changes, interventions that are capable of mitigating these effects (which remain following bouts of ‘recovery sleep’) should be investigated. Exercise improves glucose tolerance, improves mitochondrial function and is also thought to be able to shift circadian rhythms, making it an ideal candidate to mitigate some of the detrimental effects of sleep loss. Accordingly, the overall aim of this thesis was to investigate the metabolic consequences of sleep loss, and the underlying cellular mechanisms, and to determine the effectiveness of exercise on aspects of metabolic health during a period of sleep loss.
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Books on the topic "Myofibrillar protein synthesis"

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K, Linderman Jon, and United States. National Aeronautics and Space Administration., eds. Stimulation of myofibrillar protein synthesis in hindlimb suspended rats by resistance exercise and growth hormone. [Washington, DC: National Aeronautics and Space Administration, 1995.

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Book chapters on the topic "Myofibrillar protein synthesis"

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Yang, Yifan, Tyler A. Churchward-Venne, Nicholas A. Burd, Leigh Breen, Mark A. Tarnopolsky, and Stuart M. Phillips. "Myofibrillar Protein Synthesis Following Ingestion of Soy Protein Isolate at Rest and After Resistance Exercise in Elderly Men." In Clinical Nutrition and Aging, 105–26. Toronto; New Jersey : Apple Academic Press, 2015.: Apple Academic Press, 2017. http://dx.doi.org/10.1201/9781315364971-8.

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Yang, Yifan, Tyler Churchward-Venne, Nicholas Burd, Leigh Breen, and Stuart Phillips. "Myofibrillar Protein Synthesis Following Ingestion of Soy Protein Isolate at Rest and After Resistance Exercise in Elderly Men." In Clinical Nutrition and Aging, 105–26. Apple Academic Press, 2016. http://dx.doi.org/10.1201/b19985-9.

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