| 1. |
- Holm, Lars, et al.
(author)
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An exploration of the methods to determine the protein-specific synthesis and breakdown rates in vivo in humans.
- 2019
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In: Physiological Reports. - : John Wiley & Sons. - 2051-817X. ; 7:17
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Journal article (peer-reviewed)abstract
- The present study explores the methods to determine human in vivo protein-specific myofibrillar and collagenous connective tissue protein fractional synthesis and breakdown rates. We found that in human myofibrillar proteins, the protein-bound tracer disappearance method to determine the protein fractional breakdown rate (FBR) (via 2 H2 O ingestion, endogenous labeling of 2 H-alanine that is incorporated into proteins, and FBR quantified by its disappearance from these proteins) has a comparable intrasubject reproducibility (range: 0.09-53.5%) as the established direct-essential amino acid, here L-ring-13 C6 -phenylalanine, incorporation method to determine the muscle protein fractional synthesis rate (FSR) (range: 2.8-56.2%). Further, the determination of the protein breakdown in a protein structure with complex post-translational processing and maturation, exemplified by human tendon tissue, was not achieved in this experimentation, but more investigation is encouraged to reveal the possibility. Finally, we found that muscle protein FBR measured with an essential amino acid tracer prelabeling is inappropriate presumably because of significant and prolonged intracellular recycling, which also may become a significant limitation for determination of the myofibrillar FSR when repeated infusion trials are completed in the same participants.
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| 2. |
- Moberg, Marcus, et al.
(author)
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Activation of mTORC1 by leucine is potentiated by branched chain amino acids and even more so by essential amino acids following resistance exercise
- 2016
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In: American Journal of Physiology - Cell Physiology. - : American Physiological Society. - 0363-6143 .- 1522-1563. ; 310:11, s. C874-C884
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Journal article (peer-reviewed)abstract
- Protein synthesis is stimulated by resistance exercise and intake of amino acids, in particular leucine. Moreover, activation of mTORC1 signaling by leucine is potentiated by the presence of other essential amino acids (EAA). However, the contribution of the branched-chain amino acids (BCAA) to this effect is yet unknown. Here we compare the stimulatory role of leucine, BCAA and EAA ingestion on anabolic signaling following exercise. Accordingly, eight trained volunteers completed four sessions of resistance exercise during which they ingested either placebo, leucine, BCAA or EAA (including the BCAA) in random order. Muscle biopsies were taken at rest, immediately after exercise and following 90 and 180 min of recovery. Following 90 min of recovery the activity of S6K1 was greater than at rest in all four trials (Placebo37/46 was unaffected by supplementation, while that of Thr46 alone exhibited a pattern similar to that of S6K1, being 18% higher with EAA than BCAA. However, after 180 min of recovery this difference between EAA and BCAA had disappeared, although with both these supplements the increases were still higher than with leucine (40%, P<0.05) and placebo (100%, P<0.05). In summary, EAA ingestion appears to stimulate translation initiation more effectively than the other supplements, although the results also suggest that this effect is primarily attributable to the BCAA.
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