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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Frontiers Media S.A.
2022-12-01
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| Series: | Frontiers in Nutrition |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fnut.2022.1006739/full |
| _version_ | 1797979221094563840 |
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| author | Yu He Xiaofan Tan Hongqiang Li Zhiwei Yan Jing Chen Ruixue Zhao David M. Irwin Wangjun Wu Shuyi Zhang Bojiang Li |
| author_facet | Yu He Xiaofan Tan Hongqiang Li Zhiwei Yan Jing Chen Ruixue Zhao David M. Irwin Wangjun Wu Shuyi Zhang Bojiang Li |
| author_sort | Yu He |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-04-11T05:35:27Z |
| format | Article |
| id | doaj.art-1b51b8d364dc4d428db3ddbb765708b3 |
| institution | Directory Open Access Journal |
| issn | 2296-861X |
| language | English |
| last_indexed | 2024-04-11T05:35:27Z |
| publishDate | 2022-12-01 |
| publisher | Frontiers Media S.A. |
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| series | Frontiers in Nutrition |
| spelling | doaj.art-1b51b8d364dc4d428db3ddbb765708b32022-12-22T12:38:19ZengFrontiers Media S.A.Frontiers in Nutrition2296-861X2022-12-01910.3389/fnut.2022.10067391006739Phosphoproteomic analysis identifies differentially expressed phosphorylation sites that affect muscle fiber type in pigsYu He0Xiaofan Tan1Hongqiang Li2Zhiwei Yan3Jing Chen4Ruixue Zhao5David M. Irwin6Wangjun Wu7Shuyi Zhang8Bojiang Li9Department of Animal Genetics, Breeding and Reproduction, College of Animal Science and Veterinary Medicine, Shenyang Agricultural University, Shenyang, ChinaDepartment of Animal Genetics, Breeding and Reproduction, College of Animal Science and Veterinary Medicine, Shenyang Agricultural University, Shenyang, ChinaHebei Key Laboratory of Specialty Animal Germplasm Resources Exploration and Innovation, College of Animal Science and Technology, Hebei Normal University of Science and Technology, Qinhuangdao, ChinaDepartment of Animal Genetics, Breeding and Reproduction, College of Animal Science and Veterinary Medicine, Shenyang Agricultural University, Shenyang, ChinaDepartment of Animal Genetics, Breeding and Reproduction, College of Animal Science and Veterinary Medicine, Shenyang Agricultural University, Shenyang, ChinaDepartment of Animal Genetics, Breeding and Reproduction, College of Animal Science and Veterinary Medicine, Shenyang Agricultural University, Shenyang, ChinaDepartment of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, ON, CanadaDepartment of Animal Genetics, Breeding and Reproduction, College of Animal Science and Technology, Nanjing Agricultural University, Nanjing, ChinaDepartment of Animal Genetics, Breeding and Reproduction, College of Animal Science and Veterinary Medicine, Shenyang Agricultural University, Shenyang, ChinaDepartment of Animal Genetics, Breeding and Reproduction, College of Animal Science and Veterinary Medicine, Shenyang Agricultural University, Shenyang, ChinaSkeletal 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.https://www.frontiersin.org/articles/10.3389/fnut.2022.1006739/fullpigsphosphoproteomicdifferentially expressed phosphorylation sitesmuscle fiber typesmeat quality |
| spellingShingle | Yu He Xiaofan Tan Hongqiang Li Zhiwei Yan Jing Chen Ruixue Zhao David M. Irwin Wangjun Wu Shuyi Zhang Bojiang Li Phosphoproteomic analysis identifies differentially expressed phosphorylation sites that affect muscle fiber type in pigs Frontiers in Nutrition pigs phosphoproteomic differentially expressed phosphorylation sites muscle fiber types meat quality |
| 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 | pigs phosphoproteomic differentially expressed phosphorylation sites muscle fiber types meat quality |
| url | https://www.frontiersin.org/articles/10.3389/fnut.2022.1006739/full |
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