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Open AccessFeature PaperArticle

Diurnal Differences in Human Muscle Isometric Force In Vivo Are Associated with Differential Phosphorylation of Sarcomeric M-Band Proteins

1
Research Institute for Sport & Exercise Sciences, Liverpool John Moores University, Liverpool L3 3AF, UK
2
Institute of Sport, Exercise and Health, University College London, London WC1E 6BT, UK
3
Crystal Palace Football Club, London SE25 6PU, UK
4
Liverpool Centre for Cardiovascular Science, Liverpool John Moores University, Liverpool L3 3AF, UK
*
Author to whom correspondence should be addressed.
Current address: Faculty of Sports Science and Coaching, Universiti Pendidikan Sultan Idris, Perak Darul Ridzuan 35900, Malaysia.
Current address: Department of Sport & Exercise Science, Manchester Metropolitan University, Manchester M15 6BH, UK.
§
Current address: Aspire Academy, Al Henaizibia Street, Al Waab, Doha P.O. Box 22287, Qatar.
Proteomes 2020, 8(3), 22; https://doi.org/10.3390/proteomes8030022
Received: 29 June 2020 / Revised: 6 August 2020 / Accepted: 25 August 2020 / Published: 26 August 2020
(This article belongs to the Special Issue Striated Muscle Proteomics II)
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%; p < 0.05). Two-dimensional (2D) gel analysis encompassed 122 proteoforms and discovered 6 significant (p < 0.05; false discovery rate [FDR] = 10%) diurnal differences. Phosphopeptide analysis identified 1693 phosphopeptides and detected 140 phosphopeptides from 104 proteins that were more (p < 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. View Full-Text
Keywords: maximum voluntary isometric contraction; muscle contraction; phosphopeptide; phosphoproteomic; protein processing; post-translational; proteomics; rate-of-force development; sarcomere; time of day maximum voluntary isometric contraction; muscle contraction; phosphopeptide; phosphoproteomic; protein processing; post-translational; proteomics; rate-of-force development; sarcomere; time of day
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MDPI and ACS Style

Ab Malik, Z.; Bowden Davies, K.A.; Hall, E.C.R.; Barrett, J.; Pullinger, S.A.; Erskine, R.M.; Shepherd, S.O.; Iqbal, Z.; Edwards, B.J.; Burniston, J.G. Diurnal Differences in Human Muscle Isometric Force In Vivo Are Associated with Differential Phosphorylation of Sarcomeric M-Band Proteins. Proteomes 2020, 8, 22. https://doi.org/10.3390/proteomes8030022

AMA Style

Ab Malik Z, Bowden Davies KA, Hall ECR, Barrett J, Pullinger SA, Erskine RM, Shepherd SO, Iqbal Z, Edwards BJ, Burniston JG. Diurnal Differences in Human Muscle Isometric Force In Vivo Are Associated with Differential Phosphorylation of Sarcomeric M-Band Proteins. Proteomes. 2020; 8(3):22. https://doi.org/10.3390/proteomes8030022

Chicago/Turabian Style

Ab Malik, Zulezwan; Bowden Davies, Kelly A.; Hall, Elliott C.R.; Barrett, Jennifer; Pullinger, Samuel A.; Erskine, Robert M.; Shepherd, Sam O.; Iqbal, Zafar; Edwards, Ben J.; Burniston, Jatin G. 2020. "Diurnal Differences in Human Muscle Isometric Force In Vivo Are Associated with Differential Phosphorylation of Sarcomeric M-Band Proteins" Proteomes 8, no. 3: 22. https://doi.org/10.3390/proteomes8030022

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