Diurnal Differences in Human Muscle Isometric Force In Vivo Are Associated with Differential Phosphorylation of Sarcomeric M-Band Proteins
We investigated whether diurnal differences in muscle force output are associated with the post-translational state of muscle proteins. Ten physically active men (mean ± SD; age 26.7 ± 3.7 y) performed experimental sessions in the morning (08:00 h) and evening (17:00 h), which were counterbalanced i...
| Main Authors: | , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-08-01
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| Series: | Proteomes |
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| Online Access: | https://www.mdpi.com/2227-7382/8/3/22 |
| _version_ | 1797555469096583168 |
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| author | Zulezwan Ab Malik Kelly A. Bowden Davies Elliott C. R. Hall Jennifer Barrett Samuel A. Pullinger Robert M. Erskine Sam O. Shepherd Zafar Iqbal Ben J. Edwards Jatin G. Burniston |
| author_facet | Zulezwan Ab Malik Kelly A. Bowden Davies Elliott C. R. Hall Jennifer Barrett Samuel A. Pullinger Robert M. Erskine Sam O. Shepherd Zafar Iqbal Ben J. Edwards Jatin G. Burniston |
| author_sort | Zulezwan Ab Malik |
| collection | DOAJ |
| description | We investigated whether diurnal differences in muscle force output are associated with the post-translational state of muscle proteins. Ten physically active men (mean ± SD; age 26.7 ± 3.7 y) performed experimental sessions in the morning (08:00 h) and evening (17:00 h), which were counterbalanced in order of administration and separated by at least 72 h. Knee extensor maximal voluntary isometric contraction (MVIC) force and peak rate of force development (RFD) were measured, and samples of vastus lateralis were collected immediately after exercise. MVIC force was greater in the evening (mean difference of 67 N, 10.2%; <i>p</i> < 0.05). Two-dimensional (2D) gel analysis encompassed 122 proteoforms and discovered 6 significant (<i>p</i> < 0.05; false discovery rate [FDR] = 10%) diurnal differences. Phosphopeptide analysis identified 1693 phosphopeptides and detected 140 phosphopeptides from 104 proteins that were more (<i>p</i> < 0.05, FDR = 22%) phosphorylated in the morning. Myomesin 2, muscle creatine kinase, and the C-terminus of titin exhibited the most robust (FDR < 10%) diurnal differences. Exercise in the morning, compared to the evening, coincided with a greater phosphorylation of M-band-associated proteins in human muscle. These protein modifications may alter the M-band structure and disrupt force transmission, thus potentially explaining the lower force output in the morning. |
| first_indexed | 2024-03-10T16:47:57Z |
| format | Article |
| id | doaj.art-876199ae7ec84eb18099b794307ae447 |
| institution | Directory Open Access Journal |
| issn | 2227-7382 |
| language | English |
| last_indexed | 2024-03-10T16:47:57Z |
| publishDate | 2020-08-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Proteomes |
| spelling | doaj.art-876199ae7ec84eb18099b794307ae4472023-11-20T11:27:10ZengMDPI AGProteomes2227-73822020-08-01832210.3390/proteomes8030022Diurnal Differences in Human Muscle Isometric Force In Vivo Are Associated with Differential Phosphorylation of Sarcomeric M-Band ProteinsZulezwan Ab Malik0Kelly A. Bowden Davies1Elliott C. R. Hall2Jennifer Barrett3Samuel A. Pullinger4Robert M. Erskine5Sam O. Shepherd6Zafar Iqbal7Ben J. Edwards8Jatin G. Burniston9Research Institute for Sport & Exercise Sciences, Liverpool John Moores University, Liverpool L3 3AF, UKResearch Institute for Sport & Exercise Sciences, Liverpool John Moores University, Liverpool L3 3AF, UKResearch Institute for Sport & Exercise Sciences, Liverpool John Moores University, Liverpool L3 3AF, UKResearch Institute for Sport & Exercise Sciences, Liverpool John Moores University, Liverpool L3 3AF, UKResearch Institute for Sport & Exercise Sciences, Liverpool John Moores University, Liverpool L3 3AF, UKResearch Institute for Sport & Exercise Sciences, Liverpool John Moores University, Liverpool L3 3AF, UKResearch Institute for Sport & Exercise Sciences, Liverpool John Moores University, Liverpool L3 3AF, UKCrystal Palace Football Club, London SE25 6PU, UKResearch Institute for Sport & Exercise Sciences, Liverpool John Moores University, Liverpool L3 3AF, UKResearch Institute for Sport & Exercise Sciences, Liverpool John Moores University, Liverpool L3 3AF, UKWe investigated whether diurnal differences in muscle force output are associated with the post-translational state of muscle proteins. Ten physically active men (mean ± SD; age 26.7 ± 3.7 y) performed experimental sessions in the morning (08:00 h) and evening (17:00 h), which were counterbalanced in order of administration and separated by at least 72 h. Knee extensor maximal voluntary isometric contraction (MVIC) force and peak rate of force development (RFD) were measured, and samples of vastus lateralis were collected immediately after exercise. MVIC force was greater in the evening (mean difference of 67 N, 10.2%; <i>p</i> < 0.05). Two-dimensional (2D) gel analysis encompassed 122 proteoforms and discovered 6 significant (<i>p</i> < 0.05; false discovery rate [FDR] = 10%) diurnal differences. Phosphopeptide analysis identified 1693 phosphopeptides and detected 140 phosphopeptides from 104 proteins that were more (<i>p</i> < 0.05, FDR = 22%) phosphorylated in the morning. Myomesin 2, muscle creatine kinase, and the C-terminus of titin exhibited the most robust (FDR < 10%) diurnal differences. Exercise in the morning, compared to the evening, coincided with a greater phosphorylation of M-band-associated proteins in human muscle. These protein modifications may alter the M-band structure and disrupt force transmission, thus potentially explaining the lower force output in the morning.https://www.mdpi.com/2227-7382/8/3/22maximum voluntary isometric contractionmuscle contractionphosphopeptidephosphoproteomicprotein processingpost-translational |
| spellingShingle | Zulezwan Ab Malik Kelly A. Bowden Davies Elliott C. R. Hall Jennifer Barrett Samuel A. Pullinger Robert M. Erskine Sam O. Shepherd Zafar Iqbal Ben J. Edwards Jatin G. Burniston Diurnal Differences in Human Muscle Isometric Force In Vivo Are Associated with Differential Phosphorylation of Sarcomeric M-Band Proteins Proteomes maximum voluntary isometric contraction muscle contraction phosphopeptide phosphoproteomic protein processing post-translational |
| title | Diurnal Differences in Human Muscle Isometric Force In Vivo Are Associated with Differential Phosphorylation of Sarcomeric M-Band Proteins |
| title_full | Diurnal Differences in Human Muscle Isometric Force In Vivo Are Associated with Differential Phosphorylation of Sarcomeric M-Band Proteins |
| title_fullStr | Diurnal Differences in Human Muscle Isometric Force In Vivo Are Associated with Differential Phosphorylation of Sarcomeric M-Band Proteins |
| title_full_unstemmed | Diurnal Differences in Human Muscle Isometric Force In Vivo Are Associated with Differential Phosphorylation of Sarcomeric M-Band Proteins |
| title_short | Diurnal Differences in Human Muscle Isometric Force In Vivo Are Associated with Differential Phosphorylation of Sarcomeric M-Band Proteins |
| title_sort | diurnal differences in human muscle isometric force in vivo are associated with differential phosphorylation of sarcomeric m band proteins |
| topic | maximum voluntary isometric contraction muscle contraction phosphopeptide phosphoproteomic protein processing post-translational |
| url | https://www.mdpi.com/2227-7382/8/3/22 |
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