Cysteine and methionine oxidation in thrombotic disorders. Curr Opin Chem Biol 2023 Oct;76:102350
Date
06/19/2023Pubmed ID
37331217Pubmed Central ID
PMC10527720DOI
10.1016/j.cbpa.2023.102350Scopus ID
2-s2.0-85162072148 (requires institutional sign-in at Scopus site) 1 CitationAbstract
Thrombosis is the leading cause of death in many diseased conditions. Oxidative stress is characteristic of these conditions. Yet, the mechanisms through which oxidants become prothrombotic are unclear. Recent evidence suggests protein cysteine and methionine oxidation as prothrombotic regulators. These oxidative post-translational modifications occur on proteins that participate in the thrombotic process, including Src family kinases, protein disulfide isomerase, β2 glycoprotein I, von Willebrand factor, and fibrinogen. New chemical tools to identify oxidized cysteine and methionine proteins in thrombosis and hemostasis, including carbon nucleophiles for cysteine sulfenylation and oxaziridines for methionine, are critical to understanding why clots occur during oxidative stress. These mechanisms will identify alternative or novel therapeutic approaches to treat thrombotic disorders in diseased conditions.
Author List
Yang M, Smith BCAuthor
Brian C. Smith PhD Associate Professor in the Biochemistry department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
CysteineHumans
Methionine
Oxidation-Reduction
Proteins
Racemethionine
Thrombosis
