QOPNA & LAQV-REQUIMTE, Departamento de Química, Universidade de Aveiro, Aveiro, Portugal.
iBiMED, Department of Medical Sciences, University of Aveiro, Aveiro, Portugal.
J Proteome Res. 2021 Jan 1;20(1):38-48. doi: 10.1021/acs.jproteome.0c00474. Epub 2020 Oct 5.
This review focuses on discussing key mechanisms in disease pathogenesis mediated by the protein post-translational modification citrullination. These processes are discussed in depth in the context of complex diseases such as rheumatoid arthritis, cancer, central nervous system disorders, and cardiovascular disease. Additionally, a critical evaluation of challenges in laboratory detection of citrullination sites is also outlined. In this context, the role of mass spectrometry is discussed with a focus on contemporary techniques that offer promising options to detect the exact site of protein citrullination. Novel methods described in the paper have the potential to detect and quantify the occurrence of post-translational modification sites for diagnosis and therapeutic purposes with a high degree of specificity and sensitivity. Furthermore, they offer a much faster performance than traditional techniques making them ideal for large-scale experimentation.
本文重点讨论了蛋白质翻译后修饰精氨酸化介导的疾病发病机制中的关键机制。这些过程在类风湿关节炎、癌症、中枢神经系统疾病和心血管疾病等复杂疾病的背景下进行了深入讨论。此外，还对精氨酸化检测中实验室面临的挑战进行了批判性评估。在这方面，讨论了质谱在检测精氨酸化位点方面的作用，重点介绍了一些当代技术，这些技术为检测蛋白质精氨酸化的确切位点提供了有前途的选择。本文所述的新方法有可能为诊断和治疗目的检测和定量翻译后修饰位点的发生，具有高度的特异性和敏感性。此外，它们的性能比传统技术快得多，非常适合大规模实验。
