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Phosphoproteomic analysis identifies differentially expressed phosphorylation sites that affect muscle fiber type in pigs

Skeletal muscle of livestock is composed of both fast- and slow-twitch muscle fibers, which are key factors in their meat quality. However, the role of protein phosphorylation in muscle fiber type is not completely understood. Here, a fast-twitch (biceps femoris, BF) and slow-twitch (soleus, SOL) mu...

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Autores principales: He, Yu, Tan, Xiaofan, Li, Hongqiang, Yan, Zhiwei, Chen, Jing, Zhao, Ruixue, Irwin, David M., Wu, Wangjun, Zhang, Shuyi, Li, Bojiang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9815177/
https://www.ncbi.nlm.nih.gov/pubmed/36618708
http://dx.doi.org/10.3389/fnut.2022.1006739
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author He, Yu
Tan, Xiaofan
Li, Hongqiang
Yan, Zhiwei
Chen, Jing
Zhao, Ruixue
Irwin, David M.
Wu, Wangjun
Zhang, Shuyi
Li, Bojiang
author_facet He, Yu
Tan, Xiaofan
Li, Hongqiang
Yan, Zhiwei
Chen, Jing
Zhao, Ruixue
Irwin, David M.
Wu, Wangjun
Zhang, Shuyi
Li, Bojiang
author_sort He, Yu
collection PubMed
description Skeletal muscle of livestock is composed of both fast- and slow-twitch muscle fibers, which are key factors in their meat quality. However, the role of protein phosphorylation in muscle fiber type is not completely understood. Here, a fast-twitch (biceps femoris, BF) and slow-twitch (soleus, SOL) muscle tissue sample was collected from three male offspring of Duroc and Meishan pigs. We demonstrate that the meat quality of SOL muscle is significantly better than that of BF muscle. We further used phosphoproteomic profiling of BF and SOL muscles to identify differences between these muscle types. A total of 2,327 phosphorylation sites from 770 phosphoproteins were identified. Among these sites, 287 differentially expressed phosphorylation sites (DEPSs) were identified between BF and SOL. GO and KEGG enrichment analysis of proteins containing DEPSs showed that these phosphorylated proteins were enriched in the glycolytic process GO term and the AMPK signaling pathway. A protein-protein interaction (PPI) analysis reveals that these phosphorylated proteins interact with each other to regulate the transformation of muscle fiber type. These analyses reveal that protein phosphorylation modifications are involved in porcine skeletal muscle fiber type transformation. This study provides new insights into the molecular mechanisms by which protein phosphorylation regulates muscle fiber type transformation and meat quality in pigs.
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spelling pubmed-98151772023-01-06 Phosphoproteomic analysis identifies differentially expressed phosphorylation sites that affect muscle fiber type in pigs He, Yu Tan, Xiaofan Li, Hongqiang Yan, Zhiwei Chen, Jing Zhao, Ruixue Irwin, David M. Wu, Wangjun Zhang, Shuyi Li, Bojiang Front Nutr Nutrition Skeletal muscle of livestock is composed of both fast- and slow-twitch muscle fibers, which are key factors in their meat quality. However, the role of protein phosphorylation in muscle fiber type is not completely understood. Here, a fast-twitch (biceps femoris, BF) and slow-twitch (soleus, SOL) muscle tissue sample was collected from three male offspring of Duroc and Meishan pigs. We demonstrate that the meat quality of SOL muscle is significantly better than that of BF muscle. We further used phosphoproteomic profiling of BF and SOL muscles to identify differences between these muscle types. A total of 2,327 phosphorylation sites from 770 phosphoproteins were identified. Among these sites, 287 differentially expressed phosphorylation sites (DEPSs) were identified between BF and SOL. GO and KEGG enrichment analysis of proteins containing DEPSs showed that these phosphorylated proteins were enriched in the glycolytic process GO term and the AMPK signaling pathway. A protein-protein interaction (PPI) analysis reveals that these phosphorylated proteins interact with each other to regulate the transformation of muscle fiber type. These analyses reveal that protein phosphorylation modifications are involved in porcine skeletal muscle fiber type transformation. This study provides new insights into the molecular mechanisms by which protein phosphorylation regulates muscle fiber type transformation and meat quality in pigs. Frontiers Media S.A. 2022-12-22 /pmc/articles/PMC9815177/ /pubmed/36618708 http://dx.doi.org/10.3389/fnut.2022.1006739 Text en Copyright © 2022 He, Tan, Li, Yan, Chen, Zhao, Irwin, Wu, Zhang and Li. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Nutrition
He, Yu
Tan, Xiaofan
Li, Hongqiang
Yan, Zhiwei
Chen, Jing
Zhao, Ruixue
Irwin, David M.
Wu, Wangjun
Zhang, Shuyi
Li, Bojiang
Phosphoproteomic analysis identifies differentially expressed phosphorylation sites that affect muscle fiber type in pigs
title Phosphoproteomic analysis identifies differentially expressed phosphorylation sites that affect muscle fiber type in pigs
title_full Phosphoproteomic analysis identifies differentially expressed phosphorylation sites that affect muscle fiber type in pigs
title_fullStr Phosphoproteomic analysis identifies differentially expressed phosphorylation sites that affect muscle fiber type in pigs
title_full_unstemmed Phosphoproteomic analysis identifies differentially expressed phosphorylation sites that affect muscle fiber type in pigs
title_short Phosphoproteomic analysis identifies differentially expressed phosphorylation sites that affect muscle fiber type in pigs
title_sort phosphoproteomic analysis identifies differentially expressed phosphorylation sites that affect muscle fiber type in pigs
topic Nutrition
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9815177/
https://www.ncbi.nlm.nih.gov/pubmed/36618708
http://dx.doi.org/10.3389/fnut.2022.1006739
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