scholarly journals Growth hormone stimulates the collagen synthesis in human tendon and skeletal muscle without affecting myofibrillar protein synthesis

2010 ◽  
Vol 588 (2) ◽  
pp. 341-351 ◽  
Author(s):  
Simon Doessing ◽  
Katja M. Heinemeier ◽  
Lars Holm ◽  
Abigail L. Mackey ◽  
Peter Schjerling ◽  
...  
Author(s):  
George Frederick Pavis ◽  
Tom SO Jameson ◽  
Marlou L. Dirks ◽  
Benjamin P. Lee ◽  
Doaa Reda Abdelrahman ◽  
...  

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.


2017 ◽  
Vol 28 (1) ◽  
pp. 116-125 ◽  
Author(s):  
A. Pérez-López ◽  
J. McKendry ◽  
M. Martin-Rincon ◽  
D. Morales-Alamo ◽  
B. Pérez-Köhler ◽  
...  

Life Sciences ◽  
1995 ◽  
Vol 57 (8) ◽  
pp. 755-762 ◽  
Author(s):  
Jon K. Linderman ◽  
Justen B. Whittall ◽  
Kristin L. Gosselink ◽  
Tommy J. Wang ◽  
Venkat R. Mukku ◽  
...  

2006 ◽  
Vol 290 (1) ◽  
pp. E163-E168 ◽  
Author(s):  
Benjamin F. Miller ◽  
Mette Hansen ◽  
Jens L. Olesen ◽  
Allan Flyvbjerg ◽  
Peter Schwarz ◽  
...  

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 collagen proteins were measured by incorporation of [13C]leucine. Myofibrillar protein synthesis (means ± SD; rest FP: 0.053 ± 0.009%/h, LP: 0.055 ± 0.013%/h) was increased at 24-h postexercise (FP: 0.131 ± 0.018%/h, P < 0.05, LP: 0.134 ± 0.018%/h, P < 0.05) with no differences between phases. Similarly, muscle collagen synthesis (rest FP: 0.024 ± 0.017%/h, LP: 0.021 ± 0.006%/h) was elevated at 24-h postexercise (FP: 0.073 ± 0.016%/h, P < 0.05, LP: 0.072 ± 0.015%/h, P < 0.05), but the responses did not differ between menstrual phases. Therefore, there is no effect of menstrual cycle phase, at rest or in response to an acute bout of exercise, on myofibrillar protein synthesis and muscle collagen synthesis in women.


2020 ◽  
Vol 129 (1) ◽  
pp. 133-143 ◽  
Author(s):  
Sarkis J. Hannaian ◽  
Nathan Hodson ◽  
Sidney Abou Sawan ◽  
Michael Mazzulla ◽  
Hiroyuki Kato ◽  
...  

This is the first study to investigate whether postexercise leucine-enriched amino acid (LEAA) ingestion elevates mTORC1 translocation and protein-protein interactions in human skeletal muscle. Here, we observed that although LEAA ingestion did not further elevate postexercise MyoPS or mTORC1 signaling compared with placebo, mTORC1 peripheral location and interaction with Rheb were maintained. This may serve to “prime” mTORC1 for subsequent anabolic stimuli.


2014 ◽  
Vol 307 (1) ◽  
pp. E71-E83 ◽  
Author(s):  
Tyler A. Churchward-Venne ◽  
Lisa M. Cotie ◽  
Maureen J. MacDonald ◽  
Cameron J. Mitchell ◽  
Todd Prior ◽  
...  

Aging is associated with anabolic resistance, a reduced sensitivity of myofibrillar protein synthesis (MPS) to postprandial hyperaminoacidemia, particularly with low protein doses. Impairments in postprandial skeletal muscle blood flow and/or microvascular perfusion with hyperaminoacidemia and hyperinsulinemia may contribute to anabolic resistance. We examined whether providing citrulline, a precursor for arginine and nitric oxide synthesis, would increase arterial blood flow, skeletal muscle microvascular perfusion, MPS, and signaling through mTORC1. Twenty-one elderly males (65–80 yr) completed acute unilateral resistance exercise prior to being assigned to ingest a high dose (45 g) of whey protein (WHEY) or a low dose (15 g) of whey protein with 10 g of citrulline (WHEY + CIT) or with 10 g of nonessential amino acids (WHEY + NEAA). A primed, continuous infusion of l-[ ring-13C6] phenylalanine with serial muscle biopsies was used to measure MPS and protein phosphorylation, whereas ultrasound was used to measure microvascular circulation under basal and postprandial conditions in both a rested (FED) and exercised (EX-FED) leg. Argininemia was greater in WHEY + CIT vs. WHEY and WHEY + NEAA from 30 to 300 min postexercise ( P < 0.001), but there were no treatment differences in blood flow or microvascular perfusion (all P > 0.05). Phosphorylation of p70S6K-Thr389was greater in WHEY vs. WHEY + NEAA ( P = 0.02). Postprandial MPS was greater in WHEY vs. WHEY + CIT and WHEY + NEAA under both FED (WHEY: ∼128%; WHEY + CIT: ∼56%; WHEY + NEAA: ∼38%) and EX-FED (WHEY: ∼251%; WHEY + CIT: ∼124%; WHEY + NEAA: ∼108%) conditions ( P = 0.003). Citrulline coingestion with a low quantity of protein was ineffective in augmenting the anabolic properties of protein compared with nonessential amino acids.


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