Table_7_Proteomic Exploration of Porcine Oocytes During Meiotic Maturation in vitro Using an Accurate TMT-Based Quantitative Approach.xlsx

The dynamic changes in protein expression are well known to be required for oocyte meiotic maturation. Although proteomic analysis has been performed in porcine oocytes during in vitro maturation, there is still no full data because of the technical limitations at that time. Here, a novel tandem mass tag (TMT)-based quantitative approach was used to compare the proteomic profiles of porcine immature and in vitro mature oocytes. The results of our study showed that there were 763 proteins considered with significant difference−450 over-expressed and 313 under-expressed proteins. The GO and KEGG analyses revealed multiple regulatory mechanisms of oocyte nuclear and cytoplasmic maturation such as spindle and chromosome configurations, cytoskeletal reconstruction, epigenetic modifications, energy metabolism, signal transduction and others. In addition, 12 proteins identified with high-confidence peptide and related to oocyte maturation were quantified by a parallel reaction monitoring technique to validate the reliability of TMT results. In conclusion, we provided a detailed proteomics dataset to enrich the understanding of molecular characteristics underlying porcine oocyte maturation in vitro.

蛋白质表达水平的动态变化对于卵母细胞的减数成熟至关重要。尽管在体外成熟过程中对猪卵母细胞进行了蛋白质组学分析，但由于当时的技术限制，仍缺乏完整的数据。在本研究中，我们采用了基于串联质量标签（TMT）的定量方法，以比较猪未成熟和体外成熟卵母细胞的蛋白质组学特征。我们的研究结果表明，有763种蛋白质被认为存在显著差异，其中450种蛋白表达上调，313种蛋白表达下调。GO和KEGG分析揭示了卵母细胞核和细胞质成熟的多重调控机制，如纺锤体和染色体配置、细胞骨架重建、表观遗传修饰、能量代谢、信号转导等。此外，通过平行反应监测技术对12种具有高置信度的肽段及其与卵母细胞成熟相关的蛋白进行了量化，以验证TMT结果的可靠性。总之，我们提供了一套详细的蛋白质组学数据集，以丰富对猪卵母细胞体外成熟分子特征的认知。