Liang Dehuan, Chen Cheng, Huang Song, Liu Sujuan, Fu Li, Niu Yanmei
Department of Rehabilitation, School of Medical Technology, Tianjin Medical University, Tianjin, China.
Department of Anatomy and Histology, School of Basic Medical Science, Tianjin Medical University, Tianjin, China.
Front Aging Neurosci. 2022 May 3;14:859313. doi: 10.3389/fnagi.2022.859313. eCollection 2022.
Regular exercise is a powerful tool that enhances skeletal muscle mass and strength. Lysine acetylation is an important post-translational modification (PTM) involved in a broad array of cellular functions. Skeletal muscle protein contains a considerable number of lysine-acetylated (Kac) sites, so we aimed to investigate the effects of exercise-induced lysine acetylation on skeletal muscle proteins.
We randomly divided 20 male C57BL/6 mice into exercise and control groups. After 6 weeks of treadmill exercise, a lysine acetylation proteomics analysis of the gastrocnemius muscles of mice was performed.
A total of 2,254 lysine acetylation sites in 693 protein groups were identified, among which 1,916 sites in 528 proteins were quantified. The enrichment analysis suggested that protein acetylation could influence both structural and functional muscle protein properties. Moreover, molecular docking revealed that mimicking protein deacetylation primarily influenced the interaction between substrates and enzymes.
Exercise-induced lysine acetylation appears to be a crucial contributor to the alteration of skeletal muscle protein binding free energy, suggesting that its modulation is a potential approach for improving exercise performance.
规律运动是增强骨骼肌质量和力量的有力工具。赖氨酸乙酰化是一种重要的翻译后修饰（PTM），参与广泛的细胞功能。骨骼肌蛋白含有大量赖氨酸乙酰化（Kac）位点，因此我们旨在研究运动诱导的赖氨酸乙酰化对骨骼肌蛋白的影响。
将20只雄性C57BL/6小鼠随机分为运动组和对照组。经过6周的跑步机运动后，对小鼠腓肠肌进行赖氨酸乙酰化蛋白质组学分析。
共鉴定出693个蛋白质组中的2254个赖氨酸乙酰化位点，其中528个蛋白质中的1916个位点被定量。富集分析表明，蛋白质乙酰化可影响肌肉蛋白质的结构和功能特性。此外，分子对接显示，模拟蛋白质去乙酰化主要影响底物与酶之间的相互作用。
运动诱导的赖氨酸乙酰化似乎是骨骼肌蛋白结合自由能改变的关键因素，表明对其进行调节是提高运动表现的潜在途径。
