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Assessing the Role of Muscle Protein Breakdown in Response to Nutrition and Exercise in Humans

Muscle protein breakdown (MPB) is an important metabolic component of muscle remodeling, adaptation to training, and increasing muscle mass. Degradation of muscle proteins occurs via the integration of three main systems—autophagy and the calpain and ubiquitin-proteasome systems. These systems do no...

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Autores principales: Tipton, Kevin D., Hamilton, D. Lee, Gallagher, Iain J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer International Publishing 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5790854/
https://www.ncbi.nlm.nih.gov/pubmed/29368185
http://dx.doi.org/10.1007/s40279-017-0845-5
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author Tipton, Kevin D.
Hamilton, D. Lee
Gallagher, Iain J.
author_facet Tipton, Kevin D.
Hamilton, D. Lee
Gallagher, Iain J.
author_sort Tipton, Kevin D.
collection PubMed
description Muscle protein breakdown (MPB) is an important metabolic component of muscle remodeling, adaptation to training, and increasing muscle mass. Degradation of muscle proteins occurs via the integration of three main systems—autophagy and the calpain and ubiquitin-proteasome systems. These systems do not operate independently, and the regulation is complex. Complete degradation of a protein requires some combination of the systems. Determination of MPB in humans is technically challenging, leading to a relative dearth of information. Available information on the dynamic response of MPB primarily comes from stable isotopic methods with expression and activity measures providing complementary information. It seems clear that resistance exercise increases MPB, but not as much as the increase in muscle protein synthesis. Both hyperaminoacidemia and hyperinsulinemia inhibit the post-exercise response of MPB. Available data do not allow a comprehensive examination of the mechanisms behind these responses. Practical nutrition recommendations for interventions to suppress MPB following exercise are often made. However, it is likely that some degree of increased MPB following exercise is an important component for optimal remodeling. At this time, it is not possible to determine the impact of nutrition on any individual muscle protein. Thus, until we can develop and employ better methods to elucidate the role of MPB following exercise and the response to nutrition, recommendations to optimize post exercise nutrition should focus on the response of muscle protein synthesis. The aim of this review is to provide a comprehensive examination of the state of knowledge, including methodological considerations, of the response of MPB to exercise and nutrition in humans.
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spelling pubmed-57908542018-02-05 Assessing the Role of Muscle Protein Breakdown in Response to Nutrition and Exercise in Humans Tipton, Kevin D. Hamilton, D. Lee Gallagher, Iain J. Sports Med Review Article Muscle protein breakdown (MPB) is an important metabolic component of muscle remodeling, adaptation to training, and increasing muscle mass. Degradation of muscle proteins occurs via the integration of three main systems—autophagy and the calpain and ubiquitin-proteasome systems. These systems do not operate independently, and the regulation is complex. Complete degradation of a protein requires some combination of the systems. Determination of MPB in humans is technically challenging, leading to a relative dearth of information. Available information on the dynamic response of MPB primarily comes from stable isotopic methods with expression and activity measures providing complementary information. It seems clear that resistance exercise increases MPB, but not as much as the increase in muscle protein synthesis. Both hyperaminoacidemia and hyperinsulinemia inhibit the post-exercise response of MPB. Available data do not allow a comprehensive examination of the mechanisms behind these responses. Practical nutrition recommendations for interventions to suppress MPB following exercise are often made. However, it is likely that some degree of increased MPB following exercise is an important component for optimal remodeling. At this time, it is not possible to determine the impact of nutrition on any individual muscle protein. Thus, until we can develop and employ better methods to elucidate the role of MPB following exercise and the response to nutrition, recommendations to optimize post exercise nutrition should focus on the response of muscle protein synthesis. The aim of this review is to provide a comprehensive examination of the state of knowledge, including methodological considerations, of the response of MPB to exercise and nutrition in humans. Springer International Publishing 2018-01-24 2018 /pmc/articles/PMC5790854/ /pubmed/29368185 http://dx.doi.org/10.1007/s40279-017-0845-5 Text en © The Author(s) 2018 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
spellingShingle Review Article
Tipton, Kevin D.
Hamilton, D. Lee
Gallagher, Iain J.
Assessing the Role of Muscle Protein Breakdown in Response to Nutrition and Exercise in Humans
title Assessing the Role of Muscle Protein Breakdown in Response to Nutrition and Exercise in Humans
title_full Assessing the Role of Muscle Protein Breakdown in Response to Nutrition and Exercise in Humans
title_fullStr Assessing the Role of Muscle Protein Breakdown in Response to Nutrition and Exercise in Humans
title_full_unstemmed Assessing the Role of Muscle Protein Breakdown in Response to Nutrition and Exercise in Humans
title_short Assessing the Role of Muscle Protein Breakdown in Response to Nutrition and Exercise in Humans
title_sort assessing the role of muscle protein breakdown in response to nutrition and exercise in humans
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5790854/
https://www.ncbi.nlm.nih.gov/pubmed/29368185
http://dx.doi.org/10.1007/s40279-017-0845-5
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