Revealing the Mechanism of Protein Degradation in Postmortem Meat: The Role of Phosphorylation and Ubiquitination
The aim of this study was to investigate the possible effects of phosphorylation and ubiquitination on the degradation of myofibrillar proteins in mutton with different tenderness. The <i>longissimus thoracis lumborum</i> muscles were chosen and divided into tender and tough groups (<...
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2025-01-01
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| author | Xinran Zhao Saisai Wu Chi Ren Yuqiang Bai Chengli Hou Xin Li Zhenyu Wang Dequan Zhang |
| author_facet | Xinran Zhao Saisai Wu Chi Ren Yuqiang Bai Chengli Hou Xin Li Zhenyu Wang Dequan Zhang |
| author_sort | Xinran Zhao |
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| description | The aim of this study was to investigate the possible effects of phosphorylation and ubiquitination on the degradation of myofibrillar proteins in mutton with different tenderness. The <i>longissimus thoracis lumborum</i> muscles were chosen and divided into tender and tough groups (<i>n</i> = 9), and then stored at 4 °C for 1 h, 12 h, 1 d, 3 d, and 5 d postmortem. Shear force, pH, myofibril fragmentation index, AMPK activity, E3 ubiquitin ligase abundance, protein phosphorylation, and the ubiquitination levels of muscle samples were measured. The results demonstrated that the meat of samples in the tender group had a higher degradation of desmin and a lower phosphorylation level of desmin at 1 d compared with the tough group. The ubiquitination level of desmin, AMPK activity, and E3 ubiquitin ligase abundance in the tender group were noticeably higher than those in the tough group at 12 h. There was a negative correlation between the shear force and desmin degradation. The desmin degradation was negatively correlated with desmin phosphorylation and ubiquitination levels. The phosphorylation level of desmin was positively correlated with its ubiquitination. In summary, this study suggests that AMPK and E3 ubiquitin ligase concurrently play significant roles in regulating meat tenderness by regulating phosphorylation and ubiquitination in meat postmortem. |
| format | Article |
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| institution | Kabale University |
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| language | English |
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| series | Foods |
| spelling | doaj-art-bf0ebc1c0936480da25b655a6ded34cc2025-01-24T13:32:47ZengMDPI AGFoods2304-81582025-01-0114218410.3390/foods14020184Revealing the Mechanism of Protein Degradation in Postmortem Meat: The Role of Phosphorylation and UbiquitinationXinran Zhao0Saisai Wu1Chi Ren2Yuqiang Bai3Chengli Hou4Xin Li5Zhenyu Wang6Dequan Zhang7Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products Quality & Safety in Harvest, Storage, Transportation, Management and Control, Ministry of Agriculture and Rural Affairs, Beijing 100193, ChinaInstitute of Food Science and Technology, Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products Quality & Safety in Harvest, Storage, Transportation, Management and Control, Ministry of Agriculture and Rural Affairs, Beijing 100193, ChinaInstitute of Food Science and Technology, Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products Quality & Safety in Harvest, Storage, Transportation, Management and Control, Ministry of Agriculture and Rural Affairs, Beijing 100193, ChinaInstitute of Food Science and Technology, Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products Quality & Safety in Harvest, Storage, Transportation, Management and Control, Ministry of Agriculture and Rural Affairs, Beijing 100193, ChinaInstitute of Food Science and Technology, Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products Quality & Safety in Harvest, Storage, Transportation, Management and Control, Ministry of Agriculture and Rural Affairs, Beijing 100193, ChinaInstitute of Food Science and Technology, Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products Quality & Safety in Harvest, Storage, Transportation, Management and Control, Ministry of Agriculture and Rural Affairs, Beijing 100193, ChinaInstitute of Food Science and Technology, Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products Quality & Safety in Harvest, Storage, Transportation, Management and Control, Ministry of Agriculture and Rural Affairs, Beijing 100193, ChinaInstitute of Food Science and Technology, Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products Quality & Safety in Harvest, Storage, Transportation, Management and Control, Ministry of Agriculture and Rural Affairs, Beijing 100193, ChinaThe aim of this study was to investigate the possible effects of phosphorylation and ubiquitination on the degradation of myofibrillar proteins in mutton with different tenderness. The <i>longissimus thoracis lumborum</i> muscles were chosen and divided into tender and tough groups (<i>n</i> = 9), and then stored at 4 °C for 1 h, 12 h, 1 d, 3 d, and 5 d postmortem. Shear force, pH, myofibril fragmentation index, AMPK activity, E3 ubiquitin ligase abundance, protein phosphorylation, and the ubiquitination levels of muscle samples were measured. The results demonstrated that the meat of samples in the tender group had a higher degradation of desmin and a lower phosphorylation level of desmin at 1 d compared with the tough group. The ubiquitination level of desmin, AMPK activity, and E3 ubiquitin ligase abundance in the tender group were noticeably higher than those in the tough group at 12 h. There was a negative correlation between the shear force and desmin degradation. The desmin degradation was negatively correlated with desmin phosphorylation and ubiquitination levels. The phosphorylation level of desmin was positively correlated with its ubiquitination. In summary, this study suggests that AMPK and E3 ubiquitin ligase concurrently play significant roles in regulating meat tenderness by regulating phosphorylation and ubiquitination in meat postmortem.https://www.mdpi.com/2304-8158/14/2/184meat tendernessprotein posttranslational modificationsAMPKE3 ubiquitin ligase |
| spellingShingle | Xinran Zhao Saisai Wu Chi Ren Yuqiang Bai Chengli Hou Xin Li Zhenyu Wang Dequan Zhang Revealing the Mechanism of Protein Degradation in Postmortem Meat: The Role of Phosphorylation and Ubiquitination Foods meat tenderness protein posttranslational modifications AMPK E3 ubiquitin ligase |
| title | Revealing the Mechanism of Protein Degradation in Postmortem Meat: The Role of Phosphorylation and Ubiquitination |
| title_full | Revealing the Mechanism of Protein Degradation in Postmortem Meat: The Role of Phosphorylation and Ubiquitination |
| title_fullStr | Revealing the Mechanism of Protein Degradation in Postmortem Meat: The Role of Phosphorylation and Ubiquitination |
| title_full_unstemmed | Revealing the Mechanism of Protein Degradation in Postmortem Meat: The Role of Phosphorylation and Ubiquitination |
| title_short | Revealing the Mechanism of Protein Degradation in Postmortem Meat: The Role of Phosphorylation and Ubiquitination |
| title_sort | revealing the mechanism of protein degradation in postmortem meat the role of phosphorylation and ubiquitination |
| topic | meat tenderness protein posttranslational modifications AMPK E3 ubiquitin ligase |
| url | https://www.mdpi.com/2304-8158/14/2/184 |
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