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Comparative Proteomic Analysis of Glycolytic and Oxidative Muscle in Pigs

The quality of meat is highly correlated with muscle fiber type. However, the mechanisms via which proteins regulate muscle fiber types in pigs are not entirely understood. In the current study, we have performed proteomic profiling of fast/glycolytic biceps femoris (BF) and slow/oxidative soleus (S...

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Autores principales: Tan, Xiaofan, He, Yu, He, Yuqiao, Yan, Zhiwei, Chen, Jing, Zhao, Ruixue, Sui, Xin, Zhang, Lei, Du, Xuehai, Irwin, David M., Zhang, Shuyi, Li, Bojiang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9957308/
https://www.ncbi.nlm.nih.gov/pubmed/36833290
http://dx.doi.org/10.3390/genes14020361
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author Tan, Xiaofan
He, Yu
He, Yuqiao
Yan, Zhiwei
Chen, Jing
Zhao, Ruixue
Sui, Xin
Zhang, Lei
Du, Xuehai
Irwin, David M.
Zhang, Shuyi
Li, Bojiang
author_facet Tan, Xiaofan
He, Yu
He, Yuqiao
Yan, Zhiwei
Chen, Jing
Zhao, Ruixue
Sui, Xin
Zhang, Lei
Du, Xuehai
Irwin, David M.
Zhang, Shuyi
Li, Bojiang
author_sort Tan, Xiaofan
collection PubMed
description The quality of meat is highly correlated with muscle fiber type. However, the mechanisms via which proteins regulate muscle fiber types in pigs are not entirely understood. In the current study, we have performed proteomic profiling of fast/glycolytic biceps femoris (BF) and slow/oxidative soleus (SOL) muscles and identified several candidate differential proteins among these. We performed proteomic analyses based on tandem mass tags (TMTs) and identified a total of 26,228 peptides corresponding to 2667 proteins among the BF and SOL muscle samples. Among these, we found 204 differentially expressed proteins (DEPs) between BF and SOL muscle, with 56 up-regulated and 148 down-regulated DEPs in SOL muscle samples. KEGG and GO enrichment analyses of the DEPs revealed that the DEPs are involved in some GO terms (e.g., actin cytoskeleton, myosin complex, and cytoskeletal parts) and signaling pathways (PI3K-Akt and NF-kappa B signaling pathways) that influence muscle fiber type. A regulatory network of protein–protein interaction (PPI) between these DEPs that regulates muscle fiber types was constructed, which demonstrates how three down-regulated DEPs, including PFKM, GAPDH, and PKM, interact with other proteins to potentially control the glycolytic process. This study offers a new understanding of the molecular mechanisms in glycolytic and oxidative muscles as well as a novel approach for enhancing meat quality by transforming the type of muscle fibers in pigs.
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spelling pubmed-99573082023-02-25 Comparative Proteomic Analysis of Glycolytic and Oxidative Muscle in Pigs Tan, Xiaofan He, Yu He, Yuqiao Yan, Zhiwei Chen, Jing Zhao, Ruixue Sui, Xin Zhang, Lei Du, Xuehai Irwin, David M. Zhang, Shuyi Li, Bojiang Genes (Basel) Article The quality of meat is highly correlated with muscle fiber type. However, the mechanisms via which proteins regulate muscle fiber types in pigs are not entirely understood. In the current study, we have performed proteomic profiling of fast/glycolytic biceps femoris (BF) and slow/oxidative soleus (SOL) muscles and identified several candidate differential proteins among these. We performed proteomic analyses based on tandem mass tags (TMTs) and identified a total of 26,228 peptides corresponding to 2667 proteins among the BF and SOL muscle samples. Among these, we found 204 differentially expressed proteins (DEPs) between BF and SOL muscle, with 56 up-regulated and 148 down-regulated DEPs in SOL muscle samples. KEGG and GO enrichment analyses of the DEPs revealed that the DEPs are involved in some GO terms (e.g., actin cytoskeleton, myosin complex, and cytoskeletal parts) and signaling pathways (PI3K-Akt and NF-kappa B signaling pathways) that influence muscle fiber type. A regulatory network of protein–protein interaction (PPI) between these DEPs that regulates muscle fiber types was constructed, which demonstrates how three down-regulated DEPs, including PFKM, GAPDH, and PKM, interact with other proteins to potentially control the glycolytic process. This study offers a new understanding of the molecular mechanisms in glycolytic and oxidative muscles as well as a novel approach for enhancing meat quality by transforming the type of muscle fibers in pigs. MDPI 2023-01-30 /pmc/articles/PMC9957308/ /pubmed/36833290 http://dx.doi.org/10.3390/genes14020361 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Tan, Xiaofan
He, Yu
He, Yuqiao
Yan, Zhiwei
Chen, Jing
Zhao, Ruixue
Sui, Xin
Zhang, Lei
Du, Xuehai
Irwin, David M.
Zhang, Shuyi
Li, Bojiang
Comparative Proteomic Analysis of Glycolytic and Oxidative Muscle in Pigs
title Comparative Proteomic Analysis of Glycolytic and Oxidative Muscle in Pigs
title_full Comparative Proteomic Analysis of Glycolytic and Oxidative Muscle in Pigs
title_fullStr Comparative Proteomic Analysis of Glycolytic and Oxidative Muscle in Pigs
title_full_unstemmed Comparative Proteomic Analysis of Glycolytic and Oxidative Muscle in Pigs
title_short Comparative Proteomic Analysis of Glycolytic and Oxidative Muscle in Pigs
title_sort comparative proteomic analysis of glycolytic and oxidative muscle in pigs
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9957308/
https://www.ncbi.nlm.nih.gov/pubmed/36833290
http://dx.doi.org/10.3390/genes14020361
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