Institute of Chemistry, Federal University of Rio de Janeiro (UFRJ), Brazil.
Institute of Chemistry, Federal University of Rio de Janeiro (UFRJ), Brazil.
Arch Biochem Biophys. 2021 Jan 15;697:108701. doi: 10.1016/j.abb.2020.108701. Epub 2020 Nov 28.
During cellular respiration, radicals, such as superoxide, are produced, and in a large concentration, they may cause cell damage. To combat this threat, the cell employs the enzyme Cu/Zn Superoxide Dismutase (SOD1), which converts the radical superoxide into molecular oxygen and hydrogen peroxide, through redox reactions. Although this is its main function, recent studies have shown that the SOD1 has other functions that deviates from its original one including activation of nuclear gene transcription or as an RNA binding protein. This comprehensive review looks at the most important aspects of human SOD1 (hSOD1), including the structure, properties, and characteristics as well as transcriptional and post-translational modifications (PTM) that the enzyme can receive and their effects, and its many functions. We also discuss the strategies currently used to analyze it to better understand its participation in diseases linked to hSOD1 including Amyotrophic Lateral Sclerosis (ALS), cancer, and Parkinson.
在细胞呼吸过程中,自由基(如超氧化物)会产生,在高浓度下,它们可能会导致细胞损伤。为了应对这一威胁,细胞利用酶 Cu/Zn 超氧化物歧化酶(SOD1),通过氧化还原反应将自由基超氧化物转化为分子氧和过氧化氢。尽管这是其主要功能,但最近的研究表明,SOD1 还有其他与其原始功能不同的功能,包括激活核基因转录或作为 RNA 结合蛋白。本综述全面探讨了人类 SOD1(hSOD1)的最重要方面,包括酶的结构、性质和特征,以及转录和翻译后修饰(PTM)及其影响,以及其许多功能。我们还讨论了目前用于分析它的策略,以更好地了解其在与 hSOD1 相关疾病中的参与,包括肌萎缩侧索硬化症(ALS)、癌症和帕金森病。