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An exploration of t...
An exploration of the methods to determine the protein-specific synthesis and breakdown rates in vivo in humans.
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- Holm, Lars (author)
- Institute of Sports Medicine and Department of Orthopedic Surgery M, Bispebjerg Hospital, Copenhagen, Denmark
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- Dideriksen, Kasper (author)
- Institute of Sports Medicine and Department of Orthopedic Surgery M, Bispebjerg Hospital, Copenhagen, Denmark
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- Nielsen, Rie H (author)
- Institute of Sports Medicine and Department of Orthopedic Surgery M, Bispebjerg Hospital, Copenhagen, Denmark
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- Doessing, Simon (author)
- Institute of Sports Medicine and Department of Orthopedic Surgery M, Bispebjerg Hospital, Copenhagen, Denmark
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- Bechshoeft, Rasmus L (author)
- Institute of Sports Medicine and Department of Orthopedic Surgery M, Bispebjerg Hospital, Copenhagen, Denmark
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- Højfeldt, Grith (author)
- Institute of Sports Medicine and Department of Orthopedic Surgery M, Bispebjerg Hospital, Copenhagen, Denmark
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- Moberg, Marcus, 1986- (author)
- Gymnastik- och idrottshögskolan,Eva Blomstrands forskningsgrupp
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- Blomstrand, Eva (author)
- Gymnastik- och idrottshögskolan,Eva Blomstrands forskningsgrupp,Karolinska institutet
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- Reitelseder, Søren (author)
- Institute of Sports Medicine and Department of Orthopedic Surgery M, Bispebjerg Hospital, Copenhagen, Denmark
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- van Hall, Gerrit (author)
- University of Copenhagen, Denmark
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(creator_code:org_t)
- 2019-09-08
- 2019
- English.
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In: Physiological Reports. - : John Wiley & Sons. - 2051-817X. ; 7:17
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Abstract
Subject headings
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- 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.
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Fysiologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Physiology (hsv//eng)
Keyword
- Amino acid recycling
- deuterated alanine
- deuterated water
- fractional breakdown rate
- fractional synthesis rate
- protein turnover
- stable isotope
- Medicin/Teknik
- Medicine/Technology
Publication and Content Type
- ref (subject category)
- art (subject category)
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- By the author/editor
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Holm, Lars
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Dideriksen, Kasp ...
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Nielsen, Rie H
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Doessing, Simon
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Bechshoeft, Rasm ...
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Højfeldt, Grith
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show more...
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Moberg, Marcus, ...
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Blomstrand, Eva
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Reitelseder, Sør ...
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van Hall, Gerrit
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- About the subject
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- MEDICAL AND HEALTH SCIENCES
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MEDICAL AND HEAL ...
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and Basic Medicine
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and Physiology
- Articles in the publication
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Physiological Re ...
- By the university
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The Swedish School of Sport and Health Sciences