scholarly journals Myofibrillar protein turnover. Synthesis rates of myofibrillar and sarcoplasmic protein fractions in different muscles and the changes observed during postnatal development and in response to feeding and starvation

1983 ◽  
Vol 214 (2) ◽  
pp. 587-592 ◽  
Author(s):  
P C Bates ◽  
D J Millward
Keyword(s):  
Protein Synthesis ◽  
Steady State ◽  
Postnatal Development ◽  
Turnover Rate ◽  
Myofibrillar Protein ◽  
Protein Fractions ◽  
Myofibrillar Proteins ◽  
Muscle Proteins ◽  
Sarcoplasmic Protein ◽  
Myofibrillar Protein Synthesis

Measurement of rates of synthesis of skeletal-muscle proteins in adult rats shows that the faster overall rate of turnover in diaphragm and soleus muscles compared with several other, more glycolytic, muscles is also exhibited by the myofibrillar proteins, since the ratio of sarcoplasmic to myofibrillar protein synthesis is similar for all muscles. Further, throughout postnatal development, when the overall turnover rate falls with age, parallel changes occur for the myofibrillar proteins, as indicated by a constant ratio of sarcoplasmic to myofibrillar protein synthesis (2.06) in the steady state after overnight starvation. Only in the youngest (4 weeks old) rats is a slightly lower ratio observed (1.72). These results indicate that, when changes in the overall turnover rate of muscle proteins occur, the relative turnover of the two major protein fractions stays constant. However, measurements in the non-steady state during growth and after starvation for 4 days show that the relative synthesis rates of the two fractions change as a result of a disproportionate increase in myofibrillar protein synthesis during growth and decrease during starvation. Thus the synthesis rate of the slower-turning-over myofibrillar protein fraction is more sensitive to nutritional state than is that of the sarcoplasmic protein. It is suggested that such responses may help to maintain constant tissue composition during non-steady-state conditions of growth and atrophy.

scholarly journals Hypoenergetic diet-induced reductions in myofibrillar protein synthesis are restored with resistance training and balanced daily protein ingestion in older men

2015 ◽  
Vol 308 (9) ◽  
pp. E734-E743 ◽  
Author(s):  
Caoileann H. Murphy ◽  
Tyler A. Churchward-Venne ◽  
Cameron J. Mitchell ◽  
Nathan M. Kolar ◽  
Amira Kassis ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Resistance Training ◽  
Older Men ◽  
Myofibrillar Protein ◽  
Energy Restriction ◽  
Protein Distribution ◽  
Protein Meal ◽  
Fed State ◽  
Sarcoplasmic Protein ◽  
Myofibrillar Protein Synthesis

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 sarcoplasmic protein fractional synthetic rates (FSR) were measured during a 13-h primed continuous infusion of l-[ ring-13C6]phenylalanine with BAL and SKEW pattern of protein intake in EB, after 2 wk ER, and after 2 wk ER + RT. Fed-state myofibrillar FSR was lower in ER than EB in both groups ( P < 0.001), but was greater in BAL than SKEW ( P = 0.014). In ER + RT, fed-state myofibrillar FSR increased above ER in both groups and in BAL was not different from EB ( P = 0.903). In SKEW myofibrillar FSR remained lower than EB ( P = 0.002) and lower than BAL ( P = 0.006). Fed-state sarcoplasmic protein FSR was reduced similarly in ER and ER + RT compared with EB ( P < 0.01) in both groups. During ER in overweight/obese older men a BAL consumption of protein stimulated the synthesis of muscle contractile proteins more effectively than traditional, SKEW distribution. Combining RT with a BAL protein distribution “rescued” the lower rates of myofibrillar protein synthesis during moderate ER.

Regulation of myofibrillar protein turnover during maturation in normal and undernourished rat pups

2000 ◽  
Vol 278 (4) ◽  
pp. R845-R854 ◽  
Author(s):  
Marta L. Fiorotto ◽  
Teresa A. Davis ◽  
Peter J. Reeds
Keyword(s):  
Protein Synthesis ◽  
Protein Turnover ◽  
Myofibrillar Protein ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Myofibrillar Proteins ◽  
Sarcoplasmic Proteins ◽  
Rat Pups ◽  
Sarcoplasmic Protein ◽  
Degradation Rates

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.

scholarly journals Development of an UPLC mass spectrometry method for measurement of myofibrillar protein synthesis: application to analysis of murine muscles during cancer cachexia

2013 ◽  
Vol 114 (6) ◽  
pp. 824-828 ◽  
Author(s):  
Maria Lima ◽  
Shuichi Sato ◽  
Reilly T. Enos ◽  
John W. Baynes ◽  
James A. Carson
Keyword(s):  
Mass Spectrometry ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Skeletal Muscles ◽  
Cancer Cachexia ◽  
Myofibrillar Protein ◽  
Amino Acid Pool ◽  
Myofibrillar Proteins ◽  
Acid Pool ◽  
Myofibrillar Protein Synthesis

Cachexia, characterized by skeletal muscle mass loss, is a major contributory factor to patient morbidity and mortality during cancer. However, there are no reports on the rate of myofibrillar protein synthesis (MPS) in skeletal muscles that vary in primary metabolic phenotype during cachexia, in large part because of the small-size muscles and regional differences in larger muscles in the mouse. Here, we describe a sensitive method for measurement of MPS and its application to analysis of MPS in specific muscles of mice with ( Apc Min/+) and without (C57BL/6) cancer cachexia. Mice were injected with a loading dose of deuterated phenylalanine (D5F), and myofibrillar proteins were extracted from skeletal muscles at 30 min. The relative concentrations of D5F and naturally occurring phenylalanine (F) in the myofibrillar proteins and the amino acid pool were quantified by ultra-performance liquid chromatograph (UPLC) mass spectrometry (MS). The rate of MPS was determined from D5F-to-F ratio in the protein fraction compared with the amino acid pool. The rate of MPS, measured in 2–5 mg of muscle protein, was reduced by up to 65% with cachexia in the soleus, plantaris, diaphragm, and oxidative and glycolytic regions of the gastrocnemius. The rate of MPS was significantly higher in the oxidative vs. glycolytic gastrocnemius muscle. A sufficiently sensitive UPLC MS method requiring a very small amount of muscle has been developed to measure the rate of MPS in various mouse muscles. This method should be useful for studies in other animal models for quantifying effects of cancer and anti-cancer therapies on protein synthesis in cachexia, and particularly for analysis of sequential muscle biopsies in a wide range of animal and human studies.

Protein Turnover in Skeletal Muscle. II. The Effect of Starvation and a Protein-Free Diet on the Synthesis and Catabolism of Skeletal Muscle Proteins in Comparison to Liver

1970 ◽  
Vol 39 (5) ◽  
pp. 591-603 ◽  
Author(s):  
D. J. Millward
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Protein Turnover ◽  
Muscle Protein ◽  
Myofibrillar Protein ◽  
Myofibrillar Proteins ◽  
Liver Protein ◽  
Muscle Proteins ◽  
Catabolic Rate ◽  
Protein Free Diet

1. Rates of synthesis and catabolism of liver and muscle sarcoplasmic and myofibrillar protein have been measured in young control, starved and protein (deprived) rats using [14C]Na2CO3 to label protein. 2. Half-lives for synthesis of 1·35, 2·8 and 7·2 days for liver, sarcoplasmic and myofibrillar proteins respectively were obtained, whilst half-lives for catabolism were 1·55, 3·6 and 15·6 days in each case in the control animals. 3. The protein free diet for 3 days caused a small decrease in the rate of synthesis of liver and muscle proteins. The catabolic rate of liver protein was increased by 20% whilst there was a smaller increase in the catabolic rate of myofibrillar proteins. 4. Starvation for 3 days caused a 20% reduction in the rate of liver protein synthesis whilst there were greater reductions in muscle protein synthesis. The catabolic rate of liver protein was only slightly increased whereas there was a 75% increase in the rate of myofibrillar protein breakdown. 5. The total amount of protein synthesis and catabolism in liver and the two muscle protein fractions over the first 3 days of the three regimes were calculated. Muscle protein turnover, in particular myofibrillar, was shown to be very sensitive to dietary protein and/or calorie deficiency. 6. These results are discussed in terms of the mobility and therefore importance of muscle protein metabolism in the economy of the whole animal.

scholarly journals Presleep dietary protein-derived amino acids are incorporated in myofibrillar protein during postexercise overnight recovery

2018 ◽  
Vol 314 (5) ◽  
pp. E457-E467 ◽  
Author(s):  
Jorn Trommelen ◽  
Imre W. K. Kouw ◽  
Andrew M. Holwerda ◽  
Tim Snijders ◽  
Shona L. Halson ◽  
...  
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Dietary Protein ◽  
Myofibrillar Protein ◽  
Whole Body ◽  
Body Protein ◽  
Protein Ingestion ◽  
Casein Protein ◽  
The Impact ◽  
Myofibrillar Protein Synthesis

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 intravenous l-[ ring-2H5]phenylalanine, l-[1-13C]leucine, and l-[ ring-2H2]tyrosine infusions were applied. Blood and muscle tissue samples were collected to assess whole body protein net balance, myofibrillar protein synthesis rates, and overnight incorporation of dietary protein-derived amino acids into myofibrillar protein. Protein ingestion before sleep improved overnight whole body protein net balance ( P < 0.001). Myofibrillar protein synthesis rates did not differ significantly between treatments as assessed by l-[ ring-2H5]phenylalanine (0.057 ± 0.002, 0.055 ± 0.002, and 0.055 ± 0.004%/h for PLA, PRO, and PRO+leu, respectively; means ± SE; P = 0.850) or l-[1-13C]leucine (0.080 ± 0.004, 0.073 ± 0.004, and 0.083 ± 0.006%/h, respectively; P = 0.328). Myofibrillar l-[1-13C]phenylalanine enrichments increased following protein ingestion but did not differ between the PRO and PRO+leu treatments. In conclusion, protein ingestion before sleep improves whole body protein net balance and provides amino acids that are incorporated into myofibrillar protein during sleep. However, the ingestion of 30 g casein protein with or without additional free leucine before sleep does not increase muscle protein synthesis rates during postexercise overnight recovery.

Impact of Short-term Sedentariness on Week-to-Week Myofibrillar Protein Synthesis Rates in Physically Active Young Men

2018 ◽  
Vol 50 (5S) ◽  
pp. 370
Author(s):  
Brandon J. Shad ◽  
Andrew M. Holwerda ◽  
Yasir S. Elhassan ◽  
Luc J.C. van Loon ◽  
Janice L. Thompson ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Young Men ◽  
Myofibrillar Protein ◽  
Short Term ◽  
Physically Active ◽  
Myofibrillar Protein Synthesis

scholarly journals Improved recovery from skeletal muscle damage is largely unexplained by myofibrillar protein synthesis or inflammatory and regenerative gene expression pathways

2020 ◽  
Author(s):  
George Frederick Pavis ◽  
Tom SO Jameson ◽  
Marlou L. Dirks ◽  
Benjamin P. Lee ◽  
Doaa Reda Abdelrahman ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Muscle Damage ◽  
Muscle Function ◽  
Nutritional Intervention ◽  
Myofibrillar Protein ◽  
Skeletal Muscle Damage ◽  
Amino Acid Availability ◽  
Expression Pathways ◽  
Myofibrillar Protein Synthesis

The contribution of myofibrillar protein synthesis (MyoPS) to recovery from skeletal muscle damage in humans is unknown. Recreationally active males and females consumed a daily protein-polyphenol beverage targeted at increasing amino acid availability and reducing inflammation (PPB; n=9), both known to affect MyoPS, or an isocaloric placebo (PLA; n=9) during 168 h of recovery from 300 maximal unilateral eccentric contractions (EE). Muscle function was assessed daily. Muscle biopsies were collected 24, 27, 36, 72 and 168 h for MyoPS measurements using 2H2O and expression of 224 genes using RT-qPCR and pathway analysis. PPB improved recovery of muscle function, which was impaired for five days following EE in PLA (interaction; P<0.05). Acute postprandial MyoPS rates were unaffected by nutritional intervention (24-27 h). EE increased overnight (27-36 h) MyoPS versus control leg (PLA: 33±19%; PPB: 79±25%; leg P<0.01), and PPB tended to increase this further (interaction P=0.06). Daily MyoPS rates were greater with PPB between 72-168 h after EE, albeit after function had recovered. Inflammatory and regenerative signaling pathways were dramatically upregulated and clustered following EE but were unaffected by nutritional intervention. These results suggest that accelerated recovery from EE is not explained by elevated MyoPS or suppression of inflammation.

Characterization of Muscle Sarcoplasmic and Myofibrillar Protein Hydrolysis Caused by Lactobacillus plantarum

1999 ◽  
Vol 65 (8) ◽  
pp. 3540-3546 ◽  
Author(s):  
Silvina Fadda ◽  
Yolanda Sanz ◽  
Graciela Vignolo ◽  
M.-Concepción Aristoy ◽  
Guillermo Oliver ◽  
...  
Keyword(s):  
Lactobacillus Plantarum ◽  
Myofibrillar Protein ◽  
Myofibrillar Proteins ◽  
Muscle Proteins ◽  
Whole Cells ◽  
Sarcoplasmic Proteins ◽  
Cell Extracts ◽  
Hydrophobic Nature ◽  
Hydrolysis Of

ABSTRACT Strains of Lactobacillus plantarum originally isolated from sausages were screened for proteinase and aminopeptidase activities toward synthetic substrates; on the basis of that screening,L. plantarum CRL 681 was selected for further assays on muscle proteins. The activities of whole cells, cell extracts (CE), and a combination of both on sarcoplasmic and myofibrillar protein extracts were determined by protein, peptide, and free-amino-acid analyses. Proteinase from whole cells initiated the hydrolysis of sarcoplasmic proteins. The addition of CE intensified the proteolysis. Whole cells generated hydrophilic peptides from both sarcoplasmic and myofibrillar proteins. Other peptides of a hydrophobic nature resulted from the combination of whole cells and CE. The action of both enzymatic sources on myofibrillar proteins caused maximal increases in lysine, arginine, and leucine, while the action of those on sarcoplasmic proteins mainly released alanine. In general, pronounced hydrolysis of muscle proteins required enzyme activities from whole cells in addition to those supplied by CE.

scholarly journals Blood Flow Restriction Combined With Low-load Resistance-type Exercise Increases Myofibrillar Protein Synthesis Rates

2018 ◽  
Vol 50 (5S) ◽  
pp. 645-646
Author(s):  
Jean Nyakayiru ◽  
Cas J. Fuchs ◽  
Joey S.J. Smeets ◽  
Annemie P. Gijsen ◽  
Joy P.B. Goessens ◽  
...  
Keyword(s):  
Blood Flow ◽  
Protein Synthesis ◽  
Load Resistance ◽  
Myofibrillar Protein ◽  
Blood Flow Restriction ◽  
Flow Restriction ◽  
Low Load ◽  
Myofibrillar Protein Synthesis
Sign in / Sign up

Export Citation Format

Share Document