Regulatory mechanisms of skeletal muscle protein turnover during exercise

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Regulatory mechanisms of skeletal muscle protein turnover during exercise. / Rose, Adam John; Richter, Erik A.

I: Journal of Applied Physiology, Bind 106, Nr. 5, 2009, s. 1702-1711.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Rose, AJ & Richter, EA 2009, 'Regulatory mechanisms of skeletal muscle protein turnover during exercise', Journal of Applied Physiology, bind 106, nr. 5, s. 1702-1711. https://doi.org/10.1152/japplphysiol.91375.2008

APA

Rose, A. J., & Richter, E. A. (2009). Regulatory mechanisms of skeletal muscle protein turnover during exercise. Journal of Applied Physiology, 106(5), 1702-1711. https://doi.org/10.1152/japplphysiol.91375.2008

Vancouver

Rose AJ, Richter EA. Regulatory mechanisms of skeletal muscle protein turnover during exercise. Journal of Applied Physiology. 2009;106(5):1702-1711. https://doi.org/10.1152/japplphysiol.91375.2008

Author

Rose, Adam John ; Richter, Erik A. / Regulatory mechanisms of skeletal muscle protein turnover during exercise. I: Journal of Applied Physiology. 2009 ; Bind 106, Nr. 5. s. 1702-1711.

Bibtex

@article{5c01b5a0ed5211ddbf70000ea68e967b,
title = "Regulatory mechanisms of skeletal muscle protein turnover during exercise",
abstract = "Skeletal muscle protein turnover is a relatively slow metabolic process that is altered by various physiological stimuli such as feeding/fasting and exercise. During exercise, catabolism of amino acids contributes very little to ATP turnover in working muscle. With regards to protein turnover, there is now consistent data from tracer studies in rodents and humans showing that global protein synthesis is blunted in working skeletal muscle. Whether there is altered skeletal muscle protein breakdown during exercise remains unclear. The blunting of protein synthesis is believed to be mediated by suppressed mRNA translation initiation and elongation steps involving, but not limited to, changes in eIF4E-binding protein 1 (4EBP1) and eukaryotic elongation factor-2 phosphorylation (eEF2), respectively. Evidence is provided that upstream signaling to translation factors is mediated by signaling downstream of changes in intracellular Ca(2+) and energy turnover. In particular, a signaling cascade involving Ca(2+)-calmodulin-eEF2 kinase-eEF2 is implicated. The possible functional significance of altered protein turnover in working skeletal muscle during exercise is discussed. Further work with available and new techniques will undoubtedly reveal the functional significance and signaling mechanisms behind changes in skeletal muscle protein turnover during exercise. Key words: Exercise, skeletal muscle, protein metabolism, translation.",
author = "Rose, {Adam John} and Richter, {Erik A.}",
note = "CURIS 2009 5200 035",
year = "2009",
doi = "10.1152/japplphysiol.91375.2008",
language = "English",
volume = "106",
pages = "1702--1711",
journal = "Journal of Applied Physiology",
issn = "8750-7587",
publisher = "American Physiological Society",
number = "5",

}

RIS

TY - JOUR

T1 - Regulatory mechanisms of skeletal muscle protein turnover during exercise

AU - Rose, Adam John

AU - Richter, Erik A.

N1 - CURIS 2009 5200 035

PY - 2009

Y1 - 2009

N2 - Skeletal muscle protein turnover is a relatively slow metabolic process that is altered by various physiological stimuli such as feeding/fasting and exercise. During exercise, catabolism of amino acids contributes very little to ATP turnover in working muscle. With regards to protein turnover, there is now consistent data from tracer studies in rodents and humans showing that global protein synthesis is blunted in working skeletal muscle. Whether there is altered skeletal muscle protein breakdown during exercise remains unclear. The blunting of protein synthesis is believed to be mediated by suppressed mRNA translation initiation and elongation steps involving, but not limited to, changes in eIF4E-binding protein 1 (4EBP1) and eukaryotic elongation factor-2 phosphorylation (eEF2), respectively. Evidence is provided that upstream signaling to translation factors is mediated by signaling downstream of changes in intracellular Ca(2+) and energy turnover. In particular, a signaling cascade involving Ca(2+)-calmodulin-eEF2 kinase-eEF2 is implicated. The possible functional significance of altered protein turnover in working skeletal muscle during exercise is discussed. Further work with available and new techniques will undoubtedly reveal the functional significance and signaling mechanisms behind changes in skeletal muscle protein turnover during exercise. Key words: Exercise, skeletal muscle, protein metabolism, translation.

AB - Skeletal muscle protein turnover is a relatively slow metabolic process that is altered by various physiological stimuli such as feeding/fasting and exercise. During exercise, catabolism of amino acids contributes very little to ATP turnover in working muscle. With regards to protein turnover, there is now consistent data from tracer studies in rodents and humans showing that global protein synthesis is blunted in working skeletal muscle. Whether there is altered skeletal muscle protein breakdown during exercise remains unclear. The blunting of protein synthesis is believed to be mediated by suppressed mRNA translation initiation and elongation steps involving, but not limited to, changes in eIF4E-binding protein 1 (4EBP1) and eukaryotic elongation factor-2 phosphorylation (eEF2), respectively. Evidence is provided that upstream signaling to translation factors is mediated by signaling downstream of changes in intracellular Ca(2+) and energy turnover. In particular, a signaling cascade involving Ca(2+)-calmodulin-eEF2 kinase-eEF2 is implicated. The possible functional significance of altered protein turnover in working skeletal muscle during exercise is discussed. Further work with available and new techniques will undoubtedly reveal the functional significance and signaling mechanisms behind changes in skeletal muscle protein turnover during exercise. Key words: Exercise, skeletal muscle, protein metabolism, translation.

U2 - 10.1152/japplphysiol.91375.2008

DO - 10.1152/japplphysiol.91375.2008

M3 - Journal article

C2 - 19074568

VL - 106

SP - 1702

EP - 1711

JO - Journal of Applied Physiology

JF - Journal of Applied Physiology

SN - 8750-7587

IS - 5

ER -

ID: 9974618