Cysteine and methionine oxidation in thrombotic disorders.

Moua Yang, Brian C Smith

Journal: Current opinion in chemical biology 2023;76():102350

PMID: 37331217

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Abstract

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.

Address: Division of Hemostasis and Thrombosis, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, MA 02115, USA. Electronic address: [email protected].; Department of Biochemistry, Medical College of Wisconsin, Milwaukee, WI 53226, USA; Program in Chemical Biology, Medical College of Wisconsin, Milwaukee, WI 53226, USA. Electronic address: [email protected].

DOI: 10.1016/j.cbpa.2023.102350