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Journal articles on the topic 'Myofibrillar protein synthesis'

Author: Grafiati

Published: 10 January 2023

Last updated: 28 January 2023

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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 (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 sarcoplasm

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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 (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 (esti

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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 (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 incorpo

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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 (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

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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 (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

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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 (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 1.5

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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 (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 o

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8

Wall, Benjamin T., Nicholas A. Burd, Rinske Franssen, et al. "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 (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 subseque

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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 (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 is

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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 (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 s

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Meidell, R. S., A. Sen, S. A. Henderson, M. F. Slahetka, and K. R. Chien. "Alpha 1-adrenergic stimulation of rat myocardial cells increases protein synthesis." American Journal of Physiology-Heart and Circulatory Physiology 251, no. 5 (1986): H1076—H1084. http://dx.doi.org/10.1152/ajpheart.1986.251.5.h1076.

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The effects of adrenergic stimulation on the rates of protein synthesis, degradation, and accumulation were examined in primary cultures of neonatal rat heart cells. Treatment of myocardial cells with norepinephrine increased total cellular protein content and the rate of incorporation of radiolabeled tyrosine into trichloroacetic acid insoluble protein. alpha 1-Adrenergic, but not alpha 2- or beta-adrenergic blockade, inhibited these norepinephrine induced increases. The rate of protein synthesis estimated from the kinetics of equilibrium labeling and from combined equilibrium and pulse label

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Wall, Benjamin T., Marlou L. Dirks, Tim Snijders, et al. "Short-term muscle disuse lowers myofibrillar protein synthesis rates and induces anabolic resistance to protein ingestion." American Journal of Physiology-Endocrinology and Metabolism 310, no. 2 (2016): E137—E147. http://dx.doi.org/10.1152/ajpendo.00227.2015.

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Disuse leads to rapid loss of skeletal muscle mass and function. It has been hypothesized that short successive periods of muscle disuse throughout the lifespan play an important role in the development of sarcopenia. The physiological mechanisms underlying short-term muscle disuse atrophy remain to be elucidated. We assessed the impact of 5 days of muscle disuse on postabsorptive and postprandial myofibrillar protein synthesis rates in humans. Twelve healthy young (22 ± 1 yr) men underwent a 5-day period of one-legged knee immobilization (full leg cast). Quadriceps cross-sectional area (CSA)

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Preedy, V. R., and P. H. Sugden. "The effects of fasting or hypoxia on rates of protein synthesis in vivo in subcellular fractions of rat heart and gastrocnemius muscle." Biochemical Journal 257, no. 2 (1989): 519–27. http://dx.doi.org/10.1042/bj2570519.

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We measured rates of protein synthesis in vivo in subcellular fractions (soluble, myofibrillar and stromal fractions) of the heart and the gastrocnemius from rats after fasting or under hypoxic conditions (i.e. atmospheres containing 5% or 10% O2). Such interventions are known to inhibit protein synthesis under some circumstances. The recovery of tissue protein after fractionation was 80-100%. The proportions of protein present in the soluble and stromal fractions were different in the two muscles. The rates of protein synthesis in the myofibrillar and stromal fractions were less than those fo

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Trommelen, Jorn, Imre W. K. Kouw, Andrew M. Holwerda, et al. "Presleep dietary protein-derived amino acids are incorporated in myofibrillar protein during postexercise overnight recovery." American Journal of Physiology-Endocrinology and Metabolism 314, no. 5 (2018): E457—E467. http://dx.doi.org/10.1152/ajpendo.00273.2016.

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The purpose of this study was to determine the impact of ingesting 30 g casein protein with and without 2 g free leucine before sleep on myofibrillar protein synthesis rates during postexercise overnight recovery. Thirty-six healthy young men performed a single bout of resistance-type exercise in the evening (1945) after a full day of dietary standardization. Thirty minutes before sleep (2330), subjects ingested 30 g intrinsically l-[1-13C]phenylalanine-labeled protein with (PRO+leu, n = 12) or without (PRO, n = 12) 2 g free leucine, or a noncaloric placebo (PLA, n = 12). Continuous intravenou

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Shad, Brandon J., Janice L. Thompson, James Mckendry, et al. "Daily Myofibrillar Protein Synthesis Rates in Response to Low- and High-Frequency Resistance Exercise Training in Healthy, Young Men." International Journal of Sport Nutrition and Exercise Metabolism 31, no. 3 (2021): 209–16. http://dx.doi.org/10.1123/ijsnem.2020-0274.

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The impact of resistance exercise frequency on muscle protein synthesis rates remains unknown. The aim of this study was to compare daily myofibrillar protein synthesis rates over a 7-day period of low-frequency (LF) versus high-frequency (HF) resistance exercise training. Nine young men (21 ± 2 years) completed a 7-day period of habitual physical activity (BASAL). This was followed by a 7-day exercise period of volume-matched, LF (10 × 10 repetitions at 70% one-repetition maximum, once per week) or HF (2 × 10 repetitions at ∼70% one-repetition maximum, five times per week) resistance exercise

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Murphy, Caoileann H., Tyler A. Churchward-Venne, Cameron J. Mitchell, et al. "Hypoenergetic diet-induced reductions in myofibrillar protein synthesis are restored with resistance training and balanced daily protein ingestion in older men." American Journal of Physiology-Endocrinology and Metabolism 308, no. 9 (2015): E734—E743. http://dx.doi.org/10.1152/ajpendo.00550.2014.

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Strategies to enhance weight loss with a high fat-to-lean ratio in overweight/obese older adults are important since lean loss could exacerbate sarcopenia. We examined how dietary protein distribution affected muscle protein synthesis during energy balance (EB), energy restriction (ER), and energy restriction plus resistance training (ER + RT). A 4-wk ER diet was provided to overweight/obese older men (66 ± 4 yr, 31 ± 5 kg/m2) who were randomized to either a balanced (BAL: 25% daily protein/meal × 4) or skewed (SKEW: 7:17:72:4% daily protein/meal; n = 10/group) pattern. Myofibrillar and sarcop

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Preedy, V. R., and T. J. Peters. "The effect of chronic ethanol ingestion on synthesis and degradation of soluble, contractile and stromal protein fractions of skeletal muscles from immature and mature rats." Biochemical Journal 259, no. 1 (1989): 261–66. http://dx.doi.org/10.1042/bj2590261.

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1. An investigation was carried out into the response of soluble, myofibrillar and stromal protein fractions of skeletal muscle to chronic ethanol feeding. Groups of male Wistar rats, of approx. 85 or 280 g body wt., were pair-fed on a nutritionally complete liquid diet containing glucose or a diet in which 36% of the total energy was provided by ethanol. After 6 weeks, rates of protein synthesis were measured with a flooding dose of L-[4-3H]phenylalanine. 2. The protein contents of soluble, myofibrillar and stromal fractions in gastrocnemius muscle from small and large rats were decreased by

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Miller, Benjamin F., Mette Hansen, Jens L. Olesen, et al. "No effect of menstrual cycle on myofibrillar and connective tissue protein synthesis in contracting skeletal muscle." American Journal of Physiology-Endocrinology and Metabolism 290, no. 1 (2006): E163—E168. http://dx.doi.org/10.1152/ajpendo.00300.2005.

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We tested the hypothesis that acute exercise would stimulate synthesis of myofibrillar protein and intramuscular collagen in women and that the phase of the menstrual cycle at which the exercise took place would influence the extent of the change. Fifteen young, healthy female subjects were studied in the follicular (FP, n = 8) or the luteal phase (LP, n = 7, n = 1 out of phase) 24 h after an acute bout of one-legged exercise (60 min of kicking at 67% Wmax), samples being taken from the vastus lateralis in both the exercised and resting legs. Rates of synthesis of myofibrillar and muscle colla

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Holwerda, Andrew M., Freek G. Bouwman, Miranda Nabben, et al. "Endurance-Type Exercise Increases Bulk and Individual Mitochondrial Protein Synthesis Rates in Rats." International Journal of Sport Nutrition and Exercise Metabolism 30, no. 2 (2020): 153–64. http://dx.doi.org/10.1123/ijsnem.2019-0281.

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Physical activity increases muscle protein synthesis rates. However, the impact of exercise on the coordinated up- and/or downregulation of individual protein synthesis rates in skeletal muscle tissue remains unclear. The authors assessed the impact of exercise on mixed muscle, myofibrillar, and mitochondrial protein synthesis rates as well as individual protein synthesis rates in vivo in rats. Adult Lewis rats either remained sedentary (n = 3) or had access to a running wheel (n = 3) for the last 2 weeks of a 3-week experimental period. Deuterated water was injected and subsequently administe

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Kilroe, Sean P., Jonathan Fulford, Andrew M. Holwerda, et al. "Short-term muscle disuse induces a rapid and sustained decline in daily myofibrillar protein synthesis rates." American Journal of Physiology-Endocrinology and Metabolism 318, no. 2 (2020): E117—E130. http://dx.doi.org/10.1152/ajpendo.00360.2019.

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Short-term muscle disuse has been reported to lower both postabsorptive and postprandial myofibrillar protein synthesis rates. This study assessed the impact of disuse on daily myofibrillar protein synthesis rates following short-term (2 and 7 days) muscle disuse under free living conditions. Thirteen healthy young men (age: 20 ± 1 yr; BMI: 23 ± 1 kg/m−2) underwent 7 days of unilateral leg immobilization via a knee brace, with the nonimmobilized leg acting as a control. Four days before immobilization participants ingested 400 mL of 70% deuterated water, with 50-mL doses consumed daily thereaf

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Simpson, D. G., W. W. Sharp, T. K. Borg, R. L. Price, L. Terracio, and A. M. Samarel. "Mechanical regulation of cardiac myocyte protein turnover and myofibrillar structure." American Journal of Physiology-Cell Physiology 270, no. 4 (1996): C1075—C1087. http://dx.doi.org/10.1152/ajpcell.1996.270.4.c1075.

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Mechanical forces play an essential role in regulating the synthesis and assembly of contractile proteins into the sarcomeres of cardiac myocytes. To examine if physical forces might also regulate the turnover of contractile proteins at a posttranslational site of control, beating and nonbeating neonatal cardiac myocytes (NCM) were subjected to a 5% static stretch. The L-type calcium channel blocker nifedipine (12 microM) was used to inhibit contraction. Pulse-chase biosynthetic labeling experiments demonstrated that contractile arrest accelerated the loss of isotopic tracer from the total myo

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van Vliet, Stephan, Alan Fappi, Dominic N. Reeds, and Bettina Mittendorfer. "No independent or combined effects of vitamin D and conjugated linoleic acids on muscle protein synthesis in older adults: a randomized, double-blind, placebo-controlled clinical trial." American Journal of Clinical Nutrition 112, no. 5 (2020): 1382–89. http://dx.doi.org/10.1093/ajcn/nqaa240.

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ABSTRACT Background Aging is associated with skeletal muscle anabolic resistance (i.e., reduced muscle protein synthesis during anabolic conditions such as hyperaminoacidemia). The results from studies conducted in cell culture systems and animals suggest that both vitamin D and conjugated linoleic acids (CLAs) stimulate muscle protein synthesis. Objectives To conduct a randomized, double-blind, placebo-controlled clinical trial to determine the independent and combined effects of dietary vitamin D and CLA supplementation on myofibrillar protein synthesis rates in sedentary older adults. Metho

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CAMERA, DONNY M., DANIEL W. D. WEST, STUART M. PHILLIPS, et al. "Protein Ingestion Increases Myofibrillar Protein Synthesis after Concurrent Exercise." Medicine & Science in Sports & Exercise 47, no. 1 (2015): 82–91. http://dx.doi.org/10.1249/mss.0000000000000390.

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Welle, S., K. Bhatt, and C. Thornton. "Polyadenylated RNA, actin mRNA, and myosin heavy chain mRNA in young and old human skeletal muscle." American Journal of Physiology-Endocrinology and Metabolism 270, no. 2 (1996): E224—E229. http://dx.doi.org/10.1152/ajpendo.1996.270.2.e224.

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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 mus

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Fuchs, Cas J., Joey S. J. Smeets, Joan M. Senden, et al. "Hot-water immersion does not increase postprandial muscle protein synthesis rates during recovery from resistance-type exercise in healthy, young males." Journal of Applied Physiology 128, no. 4 (2020): 1012–22. http://dx.doi.org/10.1152/japplphysiol.00836.2019.

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The purpose of this study was to assess the impact of postexercise hot-water immersion on postprandial myofibrillar protein synthesis rates during recovery from a single bout of resistance-type exercise in healthy, young men. Twelve healthy, adult men (age: 23 ± 1 y) performed a single bout of resistance-type exercise followed by 20 min of water immersion of both legs. One leg was immersed in hot water [46°C: hot-water immersion (HWI)], while the other leg was immersed in thermoneutral water (30°C: CON). After water immersion, a beverage was ingested containing 20 g intrinsically L-[1-13C]-phe

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Fuchs, Cas J., Wesley J. H. Hermans, Andrew M. Holwerda, et al. "Branched-chain amino acid and branched-chain ketoacid ingestion increases muscle protein synthesis rates in vivo in older adults: a double-blind, randomized trial." American Journal of Clinical Nutrition 110, no. 4 (2019): 862–72. http://dx.doi.org/10.1093/ajcn/nqz120.

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ABSTRACTBackgroundProtein ingestion increases muscle protein synthesis rates. However, limited data are currently available on the effects of branched-chain amino acid (BCAA) and branched-chain ketoacid (BCKA) ingestion on postprandial muscle protein synthesis rates.ObjectiveThe aim of this study was to compare the impact of ingesting 6 g BCAA, 6 g BCKA, and 30 g milk protein (MILK) on the postprandial rise in circulating amino acid concentrations and subsequent myofibrillar protein synthesis rates in older males.MethodsIn a parallel design, 45 older males (age: 71 ± 1 y; BMI: 25.4 ± 0.8 kg/m2

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Davis, Teresa A., Marta L. Fiorotto, Philip R. Beckett, et al. "Differential effects of insulin on peripheral and visceral tissue protein synthesis in neonatal pigs." American Journal of Physiology-Endocrinology and Metabolism 280, no. 5 (2001): E770—E779. http://dx.doi.org/10.1152/ajpendo.2001.280.5.e770.

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We recently demonstrated in neonatal pigs that, with amino acids and glucose maintained at fasting levels, the stimulation of protein synthesis in longissimus dorsi muscle with feeding can be reproduced by a physiological rise in insulin alone. In the current report, we determine whether the response of protein synthesis to insulin in the neonatal pig is 1) present in muscles of different fiber types, 2) proportional in myofibrillar and sarcoplasmic proteins, 3) associated with increased translational efficiency and ribosome number, and 4) present in other peripheral tissues and in viscera. Hy

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Holwerda, Andrew M., Kevin J. M. Paulussen, Maarten Overkamp, et al. "Dose-Dependent Increases in Whole-Body Net Protein Balance and Dietary Protein-Derived Amino Acid Incorporation into Myofibrillar Protein During Recovery from Resistance Exercise in Older Men." Journal of Nutrition 149, no. 2 (2019): 221–30. http://dx.doi.org/10.1093/jn/nxy263.

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ABSTRACT Background Age-related decline in skeletal muscle mass is at least partly attributed to anabolic resistance to food intake. Resistance exercise sensitizes skeletal muscle tissue to the anabolic properties of amino acids. Objective The present study assessed protein digestion and amino acid absorption kinetics, whole-body protein balance, and the myofibrillar protein synthetic response to ingestion of different amounts of protein during recovery from resistance exercise in older men. Methods Forty-eight healthy older men [mean ± SEM age: 66 ± 1 y; body mass index (kg/m2): 25.4 ± 0.3] w

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Pinckaers, Philippe J. M., Michelle E. G. Weijzen, Lisanne H. P. Houben, et al. "The Muscle Protein Synthetic Response Following Ingestion of Corn Protein, Milk Protein and Their Protein Blend in Young Males." Current Developments in Nutrition 4, Supplement_2 (2020): 651. http://dx.doi.org/10.1093/cdn/nzaa049_044.

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Abstract Objectives The muscle protein synthetic response to the ingestion of animal based proteins has been reported to be superior to the ingestion of plant based proteins. The lesser anabolic properties of plant based compared with animal based proteins has been attributed to differences in essential amino acid (EAA) contents and amino acid composition. This study compares post-prandial muscle protein synthesis rates following the ingestion of 30 g milk protein with the ingestion of 30 g corn protein or a blend of 30 g corn and milk protein in vivo, in young males. Methods In a randomized,

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Mitchell, Cameron J., Randall F. D’Souza, Sarah M. Mitchell, et al. "Impact of dairy protein during limb immobilization and recovery on muscle size and protein synthesis; a randomized controlled trial." Journal of Applied Physiology 124, no. 3 (2018): 717–28. http://dx.doi.org/10.1152/japplphysiol.00803.2017.

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Muscle disuse results in the loss of muscular strength and size, due to an imbalance between protein synthesis (MPS) and breakdown (MPB). Protein ingestion stimulates MPS, although it is not established if protein is able to attenuate muscle loss with immobilization (IM) or influence the recovery consisting of ambulatory movement followed by resistance training (RT). Thirty men (49.9 ± 0.6 yr) underwent 14 days of unilateral leg IM, 14 days of ambulatory recovery (AR), and a further six RT sessions over 14 days. Participants were randomized to consume an additional 20 g of dairy protein or pla

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Gasier, Heath G., James D. Fluckey, Stephen F. Previs, Michael P. Wiggs, and Steven E. Riechman. "Acute resistance exercise augments integrative myofibrillar protein synthesis." Metabolism 61, no. 2 (2012): 153–56. http://dx.doi.org/10.1016/j.metabol.2011.07.001.

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Silver, G., and J. D. Etlinger. "Regulation of myofibrillar accumulation in chick muscle cultures: evidence for the involvement of calcium and lysosomes in non-uniform turnover of contractile proteins." Journal of Cell Biology 101, no. 6 (1985): 2383–91. http://dx.doi.org/10.1083/jcb.101.6.2383.

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The effect of calcium on myofibrillar turnover in primary chick leg skeletal muscle cultures was examined. Addition of the calcium ionophore A23187 at subcontraction threshold levels (0.38 microM) increased significantly rates of efflux of preloaded 45Ca+2 but had no effect on total protein accumulation. However, A23187 as well as ionomycin caused decreased accumulation of the myofibrillar proteins, myosin heavy chain (MHC), myosin light chain 1f (LC1f), 2f (LC2f), alpha-actin (Ac), and tropomyosin (TM). A23187 increased the degradation rate of LC1f, LC2f, and TM after 24 h. In contrast, the c

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Robinson, Matthew M., Christopher Bell, Frederick F. Peelor та Benjamin F. Miller. "β-Adrenergic receptor blockade blunts postexercise skeletal muscle mitochondrial protein synthesis rates in humans". American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 301, № 2 (2011): R327—R334. http://dx.doi.org/10.1152/ajpregu.00160.2011.

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β-Adrenergic receptor (AR) signaling is a regulator of skeletal muscle protein synthesis and mitochondrial biogenesis in mice. We hypothesized that β-AR blockade blunts postexercise skeletal muscle mitochondrial protein synthesis rates in adult humans. Six healthy men (mean ± SD: 26 ± 6 yr old, 39.9 ± 4.9 ml·kg−1·min−1 peak O2 uptake, 26.7 ± 2.0 kg/m2 body mass index) performed 1 h of stationary cycle ergometer exercise (60% peak O2 uptake) during 1) β-AR blockade (intravenous propranolol) and 2) administration of saline (control). Skeletal muscle mitochondrial, myofibrillar, and sarcoplasmic

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Young, R. B., D. M. Moriarity, C. E. McGee, W. R. Farrar, and H. E. Richter. "Protein metabolism in chicken muscle cell cultures treated with cimaterol." Journal of Animal Science 68, no. 4 (1990): 1158–69. http://dx.doi.org/10.2527/1990.6841158x.

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Abstract Primary muscle cell cultures were prepared from the leg muscle of 12-d broiler chicken embryos. The partitioning agent cimaterol (10−6 to 10−10M) was added on d 1 and each day thereafter, and cells were studied after 7 d in culture. Cimaterol had no effect at any level either on the percentage of nuclei within multinucleated myotubes or on the total number of nuclei within myotubes. At 10−7M cimaterol, the quantity of the myofibrillar protein fraction was increased by 25.1 ± 8.0% (P <.05) and the quantity of myosin heavy chain was increased by 30.9 ± 4.5% (P < .05). To understan

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Robinson, Meghann J., Nicholas A. Burd, Leigh Breen, et al. "Dose-dependent responses of myofibrillar protein synthesis with beef ingestion are enhanced with resistance exercise in middle-aged men." Applied Physiology, Nutrition, and Metabolism 38, no. 2 (2013): 120–25. http://dx.doi.org/10.1139/apnm-2012-0092.

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Aging impairs the sensitivity of skeletal muscle to anabolic stimuli, such as amino acids and resistance exercise. Beef is a nutrient-rich source of dietary protein capable of stimulating muscle protein synthesis (MPS) rates in older men at rest. To date, the dose–response of myofibrillar protein synthesis to graded ingestion of protein-rich foods, such as beef, has not been determined. We aimed to determine the dose–response of MPS with and without resistance exercise to graded doses of beef ingestion. Thirty-five middle-aged men (59 ± 2 years) ingested 0 g, 57 g (2 oz; 12 g protein), 113 g (

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Simpson, D. G., M. L. Decker, W. A. Clark, and R. S. Decker. "Contractile activity and cell-cell contact regulate myofibrillar organization in cultured cardiac myocytes." Journal of Cell Biology 123, no. 2 (1993): 323–36. http://dx.doi.org/10.1083/jcb.123.2.323.

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Adult feline ventricular myocytes cultured on a laminin-coated substratum reestablish intercellular junctions, yet disassemble their myofibrils. Immunofluorescence microscopy reveals that these non-beating heart cells lack vinculin-positive focal adhesions; moreover, intercellular junctions are also devoid of vinculin. When these quiescent myocytes are stimulated to contract with the beta-adrenergic agonist, isoproterenol, extensive vinculin-positive focal adhesions and intercellular junctions emerge. If solitary myocytes are stimulated to beat, an elaborate series of vinculin-positive focal a

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Sundaram, Priyanka, Zhiyu Pang, Miao Miao, Lu Yu, and Simon S. Wing. "USP19-deubiquitinating enzyme regulates levels of major myofibrillar proteins in L6 muscle cells." American Journal of Physiology-Endocrinology and Metabolism 297, no. 6 (2009): E1283—E1290. http://dx.doi.org/10.1152/ajpendo.00409.2009.

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The ubiquitin-proteasome system plays an important role in the degradation of myofibrillar proteins that occurs in muscle wasting. Many studies have demonstrated the importance of enzymes mediating conjugation of ubiquitin. However, little is known about the role of deubiquitinating enzymes. We previously showed that the USP19-deubiquitinating enzyme is induced in atrophying skeletal muscle (Combaret L, Adegoke OA, Bedard N, Baracos V, Attaix D, Wing SS. Am J Physiol Endocrinol Metab 288: E693–E700, 2005). To further explore the role of USP19, we used small interfering RNA (siRNA) in L6 muscle

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Phillips, Stuart M. "Short-Term Training: When Do Repeated Bouts of Resistance Exercise Become Training?" Canadian Journal of Applied Physiology 25, no. 3 (2000): 185–93. http://dx.doi.org/10.1139/h00-014.

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Chronic resistance training induces increases in muscle fibre cross-sectional area (CSA), otherwise known as hypertrophy. This is due to an increased volume percentage of myofibrillar proteins within a given fibre. The exact time-course for muscle fibre hypertrophy is not well-documented but appears to require at least 6-7 weeks of regular resistive training at reasonably high intensity before increases in fibre CSA are deemed significant. Proposed training-induced changes in neural drive are hypothesized to increase strength due to increased synchrony of motor unit firing, reduced antagonist

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Hobler, Scott C., Arthur B. Williams, Josef E. Fischer, and Per-Olof Hasselgren. "IGF-I stimulates protein synthesis but does not inhibit protein breakdown in muscle from septic rats." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 274, no. 2 (1998): R571—R576. http://dx.doi.org/10.1152/ajpregu.1998.274.2.r571.

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Sepsis is associated with reduced protein synthesis and increased protein degradation in skeletal muscle. We examined the effects of insulin-like growth factor I (IGF-I) on protein synthesis and breakdown in muscles from nonseptic and septic rats. Sepsis was induced by cecal ligation and puncture; control rats were sham operated. Extensor digitorum longus muscles were incubated in the absence or presence of IGF-I at concentrations ranging from 100 ng/ml to 10 μg/ml. Total and myofibrillar protein breakdown rates were measured as net release of tyrosine and 3-methylhistidine, respectively. Prot

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Hall-Angeras, M., U. Angeras, P. O. Hasselgren, and J. E. Fischer. "Effects of elevated temperature on protein breakdown in muscles from septic rats." American Journal of Physiology-Cell Physiology 258, no. 4 (1990): C589—C592. http://dx.doi.org/10.1152/ajpcell.1990.258.4.c589.

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Elevated temperature has been proposed to contribute to accelerated muscle protein degradation during fever and sepsis. The present study examined the effect of increased temperature in vitro on protein turnover in skeletal muscles from septic and control rats. Sepsis was induced by cecal ligation and puncture (CLP); control rats were sham operated. After 16 h, the extensor digitorum longus (EDL) and soleus (SOL) muscles were incubated at 37 or 40 degrees C. Protein synthesis was determined by measuring incorporation of [14C]phenylalanine into protein. Total and myofibrillar protein breakdown

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Welle, Stephen, Kirti Bhatt, and Charles A. Thornton. "Stimulation of myofibrillar synthesis by exercise is mediated by more efficient translation of mRNA." Journal of Applied Physiology 86, no. 4 (1999): 1220–25. http://dx.doi.org/10.1152/jappl.1999.86.4.1220.

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Resistance exercises stimulate protein synthesis in human muscle, but the roles of changes in mRNA concentrations and changes in the efficiency of mRNA translation have not been defined. The present study was done to determine whether resistance exercise affects concentrations of total RNA, total mRNA, actin mRNA, or myosin heavy-chain mRNA (total and isoform specific). Eight subjects, 62–75 yr old, performed unilateral knee extensions at 80% of their one-repetition-maximum capacity on days 1, 3, and 6 of the study. On day 7, biopsies of exercised and nonexercised vastus lateralis muscles were

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Davis, Teresa A., Marta L. Fiorotto, Douglas G. Burrin, et al. "Stimulation of protein synthesis by both insulin and amino acids is unique to skeletal muscle in neonatal pigs." American Journal of Physiology-Endocrinology and Metabolism 282, no. 4 (2002): E880—E890. http://dx.doi.org/10.1152/ajpendo.00517.2001.

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In neonatal pigs, the feeding-induced stimulation of protein synthesis in skeletal muscle, but not liver, can be reproduced by insulin infusion when essential amino acids and glucose are maintained at fasting levels. In the present study, 7- and 26-day-old pigs were studied during 1) fasting, 2) hyperinsulinemic-euglycemic-euaminoacidemic clamps, 3) euinsulinemic-euglycemic-hyperaminoacidemic clamps, and 4) hyperinsulinemic-euglycemic-hyperaminoacidemic clamps. Amino acids were clamped using a new amino acid mixture enriched in nonessential amino acids. Tissue protein synthesis was measured us

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Svanberg, E., H. Zachrisson, C. Ohlsson, B. M. Iresjo, and K. G. Lundholm. "Role of insulin and IGF-I in activation of muscle protein synthesis after oral feeding." American Journal of Physiology-Endocrinology and Metabolism 270, no. 4 (1996): E614—E620. http://dx.doi.org/10.1152/ajpendo.1996.270.4.e614.

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The aim was to evaluate the role of insulin and insulin-like growth factor I (IGF-I) in activation of muscle protein synthesis after oral feeding. Synthesis rate of globular and myofibrillar proteins in muscle tissue was quantified by a flooding dose of radioactive phenylalanine. Muscle tissue expression of IGF-I mRNA was measured. Normal (C57 Bl) and diabetic mice (type I and type II) were subjected to an overnight fast (18 h) with subsequent refeeding procedures for 3 h with either oral chow intake or provision of insulin, IGF-I, glucose, and amino acids. Anti-insulin and anti-IGF-I were pro

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Varanoske, Alyssa, Stephen Hennigar, Lee Margolis, et al. "Effects of Prolonged Energy Restriction and Dietary Protein on Muscle Protein Synthesis and Proteome Dynamics in Obese Zucker Rats." Current Developments in Nutrition 4, Supplement_2 (2020): 670. http://dx.doi.org/10.1093/cdn/nzaa049_063.

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Abstract Objectives High protein (HP) diets during short-term energy restriction (ER) attenuate energy-mediated reductions in muscle protein synthesis (MPS). MPS-adaptive responses to HP diets during prolonged ER are not well described. This study examined the effects of prolonged ER and HP on MPS and the synthesis rates of numerous individual muscle proteins. Methods Female 6-wk-old obese Zucker (leprfa+/fa+, n = 48) rats were randomized to one of four diet groups for 10 weeks: ad libitum-standard protein (AL-SP; 14% protein), AL-HP (35% protein), ER-SP, and ER-HP (both fed 60% of intake of A

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Kouw, Imre W. K., Naomi M. Cermak, Nicholas A. Burd, et al. "Sodium nitrate co-ingestion with protein does not augment postprandial muscle protein synthesis rates in older, type 2 diabetes patients." American Journal of Physiology-Endocrinology and Metabolism 311, no. 2 (2016): E325—E334. http://dx.doi.org/10.1152/ajpendo.00122.2016.

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The age-related anabolic resistance to protein ingestion is suggested to be associated with impairments in insulin-mediated capillary recruitment and postprandial muscle tissue perfusion. The present study investigated whether dietary nitrate co-ingestion with protein improves muscle protein synthesis in older, type 2 diabetes patients. Twenty-four men with type 2 diabetes (72 ± 1 yr, 26.7 ± 1.4 m/kg2 body mass index, 7.3 ± 0.4% HbA1C) received a primed continuous infusion of l-[ring-2H5]phenylalanine and l-[1-13C]leucine and ingested 20 g of intrinsically l-[1-13C]phenylalanine- and l-[1-13C]

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Hasselgren, P. O., O. Zamir, J. H. James, and J. E. Fischer. "Prostaglandin E2 does not regulate total or myofibrillar protein breakdown in incubated skeletal muscle from normal or septic rats." Biochemical Journal 270, no. 1 (1990): 45–50. http://dx.doi.org/10.1042/bj2700045.

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The role of prostaglandins in the regulation of muscle protein breakdown is controversial. We examined the influence of arachidonic acid (5 microM), prostaglandin E2 (PGE2) (2.8 microM) and the prostaglandin-synthesis inhibitor indomethacin (3 microM) on total and myofibrillar protein breakdown in rat extensor digitorum longus and soleus muscles incubated under different conditions in vitro. In other experiments, the effects of indomethacin, administered in vivo to septic rats (3 mg/kg, injected subcutaneously twice after induction of sepsis by caecal ligation and puncture) on plasma levels an

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Davies, Robert W., Joseph J. Bass, Brian P. Carson, et al. "The Effect of Whey Protein Supplementation on Myofibrillar Protein Synthesis and Performance Recovery in Resistance-Trained Men." Nutrients 12, no. 3 (2020): 845. http://dx.doi.org/10.3390/nu12030845.

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Background: The aim of this study was to investigate the effect of whey protein supplementation on myofibrillar protein synthesis (myoPS) and muscle recovery over a 7-d period of intensified resistance training (RT). Methods: In a double-blind randomised parallel group design, 16 resistance-trained men aged 18 to 35 years completed a 7-d RT protocol, consisting of three lower-body RT sessions on non-consecutive days. Participants consumed a controlled diet (146 kJ·kg−1·d−1, 1.7 g·kg−1·d−1 protein) with either a whey protein supplement or an isonitrogenous control (0.33 g·kg−1·d−1 protein). To

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Kim, Yeongmin, Sanghee Park, Jinseok Lee, et al. "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 12, no. 1 (2022): 84. http://dx.doi.org/10.3390/metabo12010084.

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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 functi

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Kumar, Vinod, Philip Atherton, Kenneth Smith, and Michael J. Rennie. "Human muscle protein synthesis and breakdown during and after exercise." Journal of Applied Physiology 106, no. 6 (2009): 2026–39. http://dx.doi.org/10.1152/japplphysiol.91481.2008.

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Skeletal muscle demonstrates extraordinary mutability in its responses to exercise of different modes, intensity, and duration, which must involve alterations of muscle protein turnover, both acutely and chronically. Here, we bring together information on the alterations in the rates of synthesis and degradation of human muscle protein by different types of exercise and the influences of nutrition, age, and sexual dimorphism. Where possible, we summarize the likely changes in activity of signaling proteins associated with control of protein turnover. Exercise of both the resistance and nonresi

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Özerman Edis, Bilge, Muhammet Bektaş, and Rüstem Nurten. "Myofibrillar degeneration with diphtheria toxin." Turkish Journal of Biochemistry 45, no. 4 (2020): 351–57. http://dx.doi.org/10.1515/tjb-2019-0109.

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AbstractObjectivesCardiac damage in patient with diphtheritic myocarditis is reported as the leading cause of mortality. Diphtheria toxin (DTx) is a well-known bacterial toxin inducing various cytotoxic effects. Mainly, catalytic fragment inhibits protein synthesis, induces cytotoxicity, and depolymerizes actin filaments. In this study, we aimed to demonstrate the extent of myofibrillar damage under DTx treatment to porcine cardiac tissue samples.MethodsTissue samples were incubated with DTx for 1–3 h in culture conditions. To analyze whole toxin (both fragments) distribution, conjugation of D

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