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

Yu He; Xiaofan Tan; Hongqiang Li; Zhiwei Yan; Jing Chen; Ruixue Zhao; David M Irwin; Wangjun Wu; Shuyi Zhang; Bojiang Li

doi:10.3389/fnut.2022.1006739

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

Front Nutr. 2022 Dec 22:9:1006739. doi: 10.3389/fnut.2022.1006739. eCollection 2022.

Authors

Yu He¹, Xiaofan Tan¹, Hongqiang Li², Zhiwei Yan¹, Jing Chen¹, Ruixue Zhao¹, David M Irwin³, Wangjun Wu⁴, Shuyi Zhang¹, Bojiang Li¹

Affiliations

¹ Department of Animal Genetics, Breeding and Reproduction, College of Animal Science and Veterinary Medicine, Shenyang Agricultural University, Shenyang, China.
² Hebei Key Laboratory of Specialty Animal Germplasm Resources Exploration and Innovation, College of Animal Science and Technology, Hebei Normal University of Science and Technology, Qinhuangdao, China.
³ Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, ON, Canada.
⁴ Department of Animal Genetics, Breeding and Reproduction, College of Animal Science and Technology, Nanjing Agricultural University, Nanjing, China.

Abstract

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.

Keywords: differentially expressed phosphorylation sites; meat quality; muscle fiber types; phosphoproteomic; pigs.