Comparative phosphoproteomics provides insights into the differences of porcine longissimus thoracis, semimembranosus, psoas major and semitendinosus muscles
Different pork cuts vary in muscle fiber characteristics and meat quality, significantly affecting processing properties and consumer preference. However, the role of protein phosphorylation in meat quality variation in pork cuts remains unclear. Using a 4D label-free platform, we performed quantita...
Saved in:
| Main Authors: | , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2025-12-01
|
| Series: | Food Chemistry: Molecular Sciences |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2666566225000474 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1849226846166581248 |
|---|---|
| author | Li Zhang Wen Luo Linlin Zhao Longyun Li Yizhong Huang |
| author_facet | Li Zhang Wen Luo Linlin Zhao Longyun Li Yizhong Huang |
| author_sort | Li Zhang |
| collection | DOAJ |
| description | Different pork cuts vary in muscle fiber characteristics and meat quality, significantly affecting processing properties and consumer preference. However, the role of protein phosphorylation in meat quality variation in pork cuts remains unclear. Using a 4D label-free platform, we performed quantitative phosphoproteomic analysis on longissimus thoracis (LT), semimembranosus (SMM), psoas major muscle (PS) and semitendinosus (SMT), identifying 13,232 phosphopeptides from 3137 phosphoproteins, and over 1000 differentially accumulated phosphopeptides (DAPPs) in each of six comparison groups. Enrichment analysis showed that these phosphoproteins were enriched in sarcomere organization and muscle cytoskeleton pathways. A total of 184, 53, 75, and 691 unique DAPPs were identified in LT, SMM, PS, and SMT, respectively. Protein-protein interaction networks revealed that phosphoproteins regulated meat quality differences. Several key phosphoproteins, including ATP5F1A, ATP5F1C, FLNC, MDH2, BAG3, and AKT1, demonstrated significant associations with meat quality traits. These findings provide valuable insights for phosphoproteins that regulate meat quality in pigs. |
| format | Article |
| id | doaj-art-2040b6be56be445eb19ff34603aa362a |
| institution | Kabale University |
| issn | 2666-5662 |
| language | English |
| publishDate | 2025-12-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Food Chemistry: Molecular Sciences |
| spelling | doaj-art-2040b6be56be445eb19ff34603aa362a2025-08-24T05:14:50ZengElsevierFood Chemistry: Molecular Sciences2666-56622025-12-011110028610.1016/j.fochms.2025.100286Comparative phosphoproteomics provides insights into the differences of porcine longissimus thoracis, semimembranosus, psoas major and semitendinosus musclesLi Zhang0Wen Luo1Linlin Zhao2Longyun Li3Yizhong Huang4College of Life Science, Nanchang Normal University, Nanchang 330032, China; College of Forestry, Jiangxi Agricultural University, Nanchang 330045, ChinaCollege of Life Science, Nanchang Normal University, Nanchang 330032, ChinaCollege of Life Science, Nanchang Normal University, Nanchang 330032, ChinaCollege of Life Science, Nanchang Normal University, Nanchang 330032, China; Corresponding authors.College of Life Science, Nanchang Normal University, Nanchang 330032, China; Corresponding authors.Different pork cuts vary in muscle fiber characteristics and meat quality, significantly affecting processing properties and consumer preference. However, the role of protein phosphorylation in meat quality variation in pork cuts remains unclear. Using a 4D label-free platform, we performed quantitative phosphoproteomic analysis on longissimus thoracis (LT), semimembranosus (SMM), psoas major muscle (PS) and semitendinosus (SMT), identifying 13,232 phosphopeptides from 3137 phosphoproteins, and over 1000 differentially accumulated phosphopeptides (DAPPs) in each of six comparison groups. Enrichment analysis showed that these phosphoproteins were enriched in sarcomere organization and muscle cytoskeleton pathways. A total of 184, 53, 75, and 691 unique DAPPs were identified in LT, SMM, PS, and SMT, respectively. Protein-protein interaction networks revealed that phosphoproteins regulated meat quality differences. Several key phosphoproteins, including ATP5F1A, ATP5F1C, FLNC, MDH2, BAG3, and AKT1, demonstrated significant associations with meat quality traits. These findings provide valuable insights for phosphoproteins that regulate meat quality in pigs.http://www.sciencedirect.com/science/article/pii/S2666566225000474Pork cutsMeat qualityPhosphoproteomeDifferentially accumulated phosphopeptidesCut-specific phosphoproteins |
| spellingShingle | Li Zhang Wen Luo Linlin Zhao Longyun Li Yizhong Huang Comparative phosphoproteomics provides insights into the differences of porcine longissimus thoracis, semimembranosus, psoas major and semitendinosus muscles Food Chemistry: Molecular Sciences Pork cuts Meat quality Phosphoproteome Differentially accumulated phosphopeptides Cut-specific phosphoproteins |
| title | Comparative phosphoproteomics provides insights into the differences of porcine longissimus thoracis, semimembranosus, psoas major and semitendinosus muscles |
| title_full | Comparative phosphoproteomics provides insights into the differences of porcine longissimus thoracis, semimembranosus, psoas major and semitendinosus muscles |
| title_fullStr | Comparative phosphoproteomics provides insights into the differences of porcine longissimus thoracis, semimembranosus, psoas major and semitendinosus muscles |
| title_full_unstemmed | Comparative phosphoproteomics provides insights into the differences of porcine longissimus thoracis, semimembranosus, psoas major and semitendinosus muscles |
| title_short | Comparative phosphoproteomics provides insights into the differences of porcine longissimus thoracis, semimembranosus, psoas major and semitendinosus muscles |
| title_sort | comparative phosphoproteomics provides insights into the differences of porcine longissimus thoracis semimembranosus psoas major and semitendinosus muscles |
| topic | Pork cuts Meat quality Phosphoproteome Differentially accumulated phosphopeptides Cut-specific phosphoproteins |
| url | http://www.sciencedirect.com/science/article/pii/S2666566225000474 |
| work_keys_str_mv | AT lizhang comparativephosphoproteomicsprovidesinsightsintothedifferencesofporcinelongissimusthoracissemimembranosuspsoasmajorandsemitendinosusmuscles AT wenluo comparativephosphoproteomicsprovidesinsightsintothedifferencesofporcinelongissimusthoracissemimembranosuspsoasmajorandsemitendinosusmuscles AT linlinzhao comparativephosphoproteomicsprovidesinsightsintothedifferencesofporcinelongissimusthoracissemimembranosuspsoasmajorandsemitendinosusmuscles AT longyunli comparativephosphoproteomicsprovidesinsightsintothedifferencesofporcinelongissimusthoracissemimembranosuspsoasmajorandsemitendinosusmuscles AT yizhonghuang comparativephosphoproteomicsprovidesinsightsintothedifferencesofporcinelongissimusthoracissemimembranosuspsoasmajorandsemitendinosusmuscles |