Malila Yuwares, Charoenlappanit Sawanya, Phaonakrop Narumon, Srimarut Yanee, Roytrakul Sittiruk
National Center for Genetic Engineering and Biotechnology (BIOTEC), National Science and Technology Development Agency, Pathum Thani, Thailand.
Anim Biosci. 2025 Sep;38(9):2008-2020. doi: 10.5713/ab.24.0892. Epub 2025 Apr 28.
This study aimed to investigate how growth-related myopathies influenced chemical modifications formed on amino acid residues of chicken breast proteins.
Breasts (pectoralis major) of commercial broilers (Gallus gallus) were classified into "normal", White Striping (WS)" and "White Striping + Wooden Breast (WS+WB)" groups (n = 9 per group). The meat was subjected to proteomic analysis using a liquid chromatography-tandem mass spectrometry. Differences in abundance of modified sites, including methylated lysine (Lys) and arginine, acetsylated Lys, and oxidized methionine (Met), due to the growth-related myopathies were identified (false discovery rate [FDR]<0.05). Biological functions of the proteins were analyzed.
Proteomics revealed 185, 105, and 194 modified sites for methylation, Lys acetylation and Met oxidation, respectively. Of 185, 10 sites from seven proteins (TPM1, MYH, MYH1F, DICER1, RCJMB04_5k17, TPI1, and VIM) showed differential abundance in the methylation (FDR<0.05). Seven acetylated Lys sites from five proteins (TPM1, ADHFE1, SPAG9, PCNT, and RCJMB04_5k17) were differentially expressed. The abundance of those sites in normal samples were lower than those of WS samples (FDR<0.05). As for oxidized Met, differential 62 sites were identified (FDR<0.05). The major Met-oxidized protein was MYH. Met oxidation of 40 sites from 22 proteins was increased in WS samples whereas 19 sites of four proteins (MYL11, MYH, MYH1F, and TNNT2) were increased in WS+WB samples. Only four sites from DICER1, LDHA and LDB3 were found in normal samples (FDR<0.05).
The findings shed light on the links between oxidative stress and oxidized Met in the chicken with growth-related myopathies. In addition, methylation and acetylation modifications likely played a role in dynamic cell signaling to maintain cellular activities, particularly metabolism and energy production, against the stress in the affected birds.
本研究旨在探究生长相关性肌病如何影响鸡胸肉蛋白质氨基酸残基上形成的化学修饰。
将商品肉鸡（家鸡）的胸肌（胸大肌）分为“正常”、“白条纹（WS）”和“白条纹+木质胸肌（WS+WB）”组（每组n = 9）。使用液相色谱-串联质谱对肉进行蛋白质组学分析。确定由于生长相关性肌病导致的修饰位点丰度差异，包括甲基化赖氨酸（Lys）和精氨酸、乙酰化Lys以及氧化甲硫氨酸（Met）（错误发现率[FDR]<0.05）。分析蛋白质的生物学功能。
蛋白质组学分别揭示了185个、105个和194个甲基化、Lys乙酰化和Met氧化的修饰位点。在185个甲基化位点中，来自7种蛋白质（TPM1、MYH、MYH1F、DICER1、RCJMB04_5k17、TPI1和VIM）的10个位点在甲基化方面表现出丰度差异（FDR<0.05）。来自5种蛋白质（TPM1、ADHFE1、SPAG9、PCNT和RCJMB04_5k17）的7个乙酰化Lys位点差异表达。正常样品中这些位点的丰度低于WS样品（FDR<0.05）。至于氧化Met，鉴定出62个差异位点（FDR<0.05）。主要的Met氧化蛋白是MYH。WS样品中22种蛋白质的40个位点的Met氧化增加，而WS+WB样品中4种蛋白质（MYL11、MYH、MYH1F和TNNT2）的19个位点增加。正常样品中仅发现来自DICER1、LDHA和LDB3的4个位点（FDR<0.05）。
这些发现揭示了生长相关性肌病鸡中氧化应激与氧化Met之间的联系。此外，甲基化和乙酰化修饰可能在动态细胞信号传导中发挥作用，以维持受影响禽类细胞的活动，特别是代谢和能量产生，以应对应激。
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