Aerobic capacity and muscle proteome: Insights from a mouse model
Abstract We explored the association between aerobic capacity (AC) and the skeletal muscle proteome of McArdle (n = 10) and wild‐type (n = 8) mice, as models of intrinsically ‘low’ and ‘normal’ AC, respectively. AC was determined as total distance achieved in treadmill running until exhaustion. The...
Saved in:
| Main Authors: | , , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Wiley
2025-02-01
|
| Series: | Experimental Physiology |
| Subjects: | |
| Online Access: | https://doi.org/10.1113/EP092308 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1832576341855174656 |
|---|---|
| author | Abel Plaza‐Florido Alejandro Santos‐Lozano Susana López‐Ortiz Beatriz G. Gálvez Joaquín Arenas Miguel A. Martín Pedro L. Valenzuela Tomàs Pinós Alejandro Lucia Carmen Fiuza‐Luces |
| author_facet | Abel Plaza‐Florido Alejandro Santos‐Lozano Susana López‐Ortiz Beatriz G. Gálvez Joaquín Arenas Miguel A. Martín Pedro L. Valenzuela Tomàs Pinós Alejandro Lucia Carmen Fiuza‐Luces |
| author_sort | Abel Plaza‐Florido |
| collection | DOAJ |
| description | Abstract We explored the association between aerobic capacity (AC) and the skeletal muscle proteome of McArdle (n = 10) and wild‐type (n = 8) mice, as models of intrinsically ‘low’ and ‘normal’ AC, respectively. AC was determined as total distance achieved in treadmill running until exhaustion. The quadriceps muscle proteome was studied using liquid chromatography with tandem mass spectrometry, with the Search Tool for the Retrieval of Interacting Genes/Proteins database used to generate protein–protein interaction (PPI) networks and enrichment analyses. AC was significantly associated (P‐values ranging from 0.0002 to 0.049) with 73 (McArdle) and 61 (wild‐type) proteins (r‐values from −0.90 to 0.94). These proteins were connected in PPI networks that enriched biological processes involved in skeletal muscle structure/function in both groups (false discovery rate <0.05). In McArdle mice, the proteins associated with AC were involved in skeletal muscle fibre differentiation/development, lipid oxidation, mitochondrial function and calcium homeostasis, whereas in wild‐type animals AC‐associated proteins were related to cytoskeleton structure (intermediate filaments), cell cycle regulation and endocytic trafficking. Two proteins (WEE2, THYG) were associated with AC (negatively and positively, respectively) in both groups. Only 14 of the 132 proteins (∼11%) associated with AC in McArdle or wild‐type mice were also associated with those previously reported to be modified by aerobic training in these mice, providing preliminary evidence for a large divergence in the muscle proteome signature linked to aerobic training or AC, irrespective of AC (intrinsically low or normal) levels. Our findings might help to gain insight into the molecular mechanisms underlying AC at the muscle tissue level. |
| format | Article |
| id | doaj-art-67e29359c60c4224899d3cf643f8b927 |
| institution | Kabale University |
| issn | 0958-0670 1469-445X |
| language | English |
| publishDate | 2025-02-01 |
| publisher | Wiley |
| record_format | Article |
| series | Experimental Physiology |
| spelling | doaj-art-67e29359c60c4224899d3cf643f8b9272025-01-31T06:19:51ZengWileyExperimental Physiology0958-06701469-445X2025-02-01110229330610.1113/EP092308Aerobic capacity and muscle proteome: Insights from a mouse modelAbel Plaza‐Florido0Alejandro Santos‐Lozano1Susana López‐Ortiz2Beatriz G. Gálvez3Joaquín Arenas4Miguel A. Martín5Pedro L. Valenzuela6Tomàs Pinós7Alejandro Lucia8Carmen Fiuza‐Luces9Pediatric Exercise and Genomics Research Center, Department of Pediatrics, School of MedicineUniversity of California IrvineIrvineCaliforniaUSAi+HeALTHEuropean University Miguel de CervantesValladolidSpaini+HeALTHEuropean University Miguel de CervantesValladolidSpainDepartment of Biochemistry and Molecular Biology, Faculty of PharmacyUniversidad Complutense de MadridMadridSpainPhysical Activity and HEalth Reseach Group (PAHERG)Research Institute of the Hospital 12 de Octubre (‘imas12’)Madrid SpainPhysical Activity and HEalth Reseach Group (PAHERG)Research Institute of the Hospital 12 de Octubre (‘imas12’)Madrid SpainPhysical Activity and HEalth Reseach Group (PAHERG)Research Institute of the Hospital 12 de Octubre (‘imas12’)Madrid SpainUnit 701Spanish Network for Biomedical Research in Rare Diseases (CIBERER)Madrid SpainFaculty of Sport SciencesUniversidad Europea de MadridMadridSpainPhysical Activity and HEalth Reseach Group (PAHERG)Research Institute of the Hospital 12 de Octubre (‘imas12’)Madrid SpainAbstract We explored the association between aerobic capacity (AC) and the skeletal muscle proteome of McArdle (n = 10) and wild‐type (n = 8) mice, as models of intrinsically ‘low’ and ‘normal’ AC, respectively. AC was determined as total distance achieved in treadmill running until exhaustion. The quadriceps muscle proteome was studied using liquid chromatography with tandem mass spectrometry, with the Search Tool for the Retrieval of Interacting Genes/Proteins database used to generate protein–protein interaction (PPI) networks and enrichment analyses. AC was significantly associated (P‐values ranging from 0.0002 to 0.049) with 73 (McArdle) and 61 (wild‐type) proteins (r‐values from −0.90 to 0.94). These proteins were connected in PPI networks that enriched biological processes involved in skeletal muscle structure/function in both groups (false discovery rate <0.05). In McArdle mice, the proteins associated with AC were involved in skeletal muscle fibre differentiation/development, lipid oxidation, mitochondrial function and calcium homeostasis, whereas in wild‐type animals AC‐associated proteins were related to cytoskeleton structure (intermediate filaments), cell cycle regulation and endocytic trafficking. Two proteins (WEE2, THYG) were associated with AC (negatively and positively, respectively) in both groups. Only 14 of the 132 proteins (∼11%) associated with AC in McArdle or wild‐type mice were also associated with those previously reported to be modified by aerobic training in these mice, providing preliminary evidence for a large divergence in the muscle proteome signature linked to aerobic training or AC, irrespective of AC (intrinsically low or normal) levels. Our findings might help to gain insight into the molecular mechanisms underlying AC at the muscle tissue level.https://doi.org/10.1113/EP092308cardiorespiratory fitnessenduranceexerciseglycogenosis type Vomicsproteome |
| spellingShingle | Abel Plaza‐Florido Alejandro Santos‐Lozano Susana López‐Ortiz Beatriz G. Gálvez Joaquín Arenas Miguel A. Martín Pedro L. Valenzuela Tomàs Pinós Alejandro Lucia Carmen Fiuza‐Luces Aerobic capacity and muscle proteome: Insights from a mouse model Experimental Physiology cardiorespiratory fitness endurance exercise glycogenosis type V omics proteome |
| title | Aerobic capacity and muscle proteome: Insights from a mouse model |
| title_full | Aerobic capacity and muscle proteome: Insights from a mouse model |
| title_fullStr | Aerobic capacity and muscle proteome: Insights from a mouse model |
| title_full_unstemmed | Aerobic capacity and muscle proteome: Insights from a mouse model |
| title_short | Aerobic capacity and muscle proteome: Insights from a mouse model |
| title_sort | aerobic capacity and muscle proteome insights from a mouse model |
| topic | cardiorespiratory fitness endurance exercise glycogenosis type V omics proteome |
| url | https://doi.org/10.1113/EP092308 |
| work_keys_str_mv | AT abelplazaflorido aerobiccapacityandmuscleproteomeinsightsfromamousemodel AT alejandrosantoslozano aerobiccapacityandmuscleproteomeinsightsfromamousemodel AT susanalopezortiz aerobiccapacityandmuscleproteomeinsightsfromamousemodel AT beatrizggalvez aerobiccapacityandmuscleproteomeinsightsfromamousemodel AT joaquinarenas aerobiccapacityandmuscleproteomeinsightsfromamousemodel AT miguelamartin aerobiccapacityandmuscleproteomeinsightsfromamousemodel AT pedrolvalenzuela aerobiccapacityandmuscleproteomeinsightsfromamousemodel AT tomaspinos aerobiccapacityandmuscleproteomeinsightsfromamousemodel AT alejandrolucia aerobiccapacityandmuscleproteomeinsightsfromamousemodel AT carmenfiuzaluces aerobiccapacityandmuscleproteomeinsightsfromamousemodel |