| Literature DB >> 33259795 |
Elis Cristina Araujo Eleutherio1, Rayne Stfhany Silva Magalhães2, Aline de Araújo Brasil2, José Raphael Monteiro Neto2, Luan de Holanda Paranhos2.
Abstract
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.Entities:
Keywords: Aging; Cancer; Neurodegenerative diseases; Post-translational modifications; Superoxide dismutase 1
Year: 2020 PMID: 33259795 DOI: 10.1016/j.abb.2020.108701
Source DB: PubMed Journal: Arch Biochem Biophys ISSN: 0003-9861 Impact factor: 4.013