Proteomics unveils chemical modifications on protein side chains in raw breast meat of broilers (Gallus gallus) affected with growth-related myopathies.

IF 2.4 2区 农林科学 Q1 AGRICULTURE, DAIRY & ANIMAL SCIENCE
Yuwares Malila, Sawanya Charoenlappanit, Narumon Phaonakrop, Yanee Srimarut, Sittiruk Roytrakul
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引用次数: 0

Abstract

Objective: This study aimed to investigate how growth-related myopathies influenced chemical modifications formed on amino acid residues of chicken breast proteins.

Methods: 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 (Arg), 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.

Results: 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).

Conclusion: 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.

蛋白质组学揭示了受生长相关肌病影响的肉鸡(Gallus Gallus)生胸肉中蛋白质侧链的化学修饰。
目的:研究生长相关肌病如何影响鸡胸肉蛋白氨基酸残基的化学修饰。方法:将商品肉鸡(Gallus Gallus)的乳房(胸大肌)分为“正常”组、“白色条纹”组和“白色条纹+木胸”组(WS+WB),每组9只。用液相色谱-串联质谱法对肉进行蛋白质组学分析。由于生长相关的肌病,修饰位点(包括甲基化赖氨酸(Lys)和精氨酸(Arg)、乙酰化赖氨酸和氧化蛋氨酸(Met))的丰度存在差异(错误发现率,FDR < 0.05)。分析了蛋白质的生物学功能。结果:蛋白质组学分别发现185、105和194个甲基化、赖氨酸乙酰化和Met氧化修饰位点。在185个位点中,来自7个蛋白(TPM1、MYH、MYH1F、DICER1、RCJMB04_5k17、TPI1和VIM)的10个位点的甲基化丰度存在差异(FDR < 0.05)。来自5个蛋白(TPM1、ADHFE1、SPAG9、PCNT和RCJMB04_5k17)的7个乙酰化赖氨酸位点差异表达。正常样本中这些位点的丰度低于WS样本(FDR < 0.05)。对于氧化Met,鉴定出62个差异位点(FDR < 0.05)。主要的met氧化蛋白为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个位点的Met氧化增加。正常标本中DICER1、LDHA和LDB3位点仅出现4个位点(FDR < 0.05)。结论:研究结果揭示了生长相关肌病鸡氧化应激与氧化蛋氨酸之间的联系。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,以维持细胞活动,特别是代谢和能量产生,以对抗受影响鸟类的压力。
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来源期刊
Animal Bioscience
Animal Bioscience AGRICULTURE, DAIRY & ANIMAL SCIENCE-
CiteScore
5.00
自引率
0.00%
发文量
223
审稿时长
3 months
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