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Oxidative Cysteine Modification of Thiol Isomerases in Thrombotic Disease: A Hypothesis.

PMID: 34121445 (view PubMed database entry)
DOI: 10.1089/ars.2021.0108 (read at publisher's website )

Moua Yang, Robert Flaumenhaft,

<b><i>Significance:</i></b> Oxidative stress is a characteristic of many systemic diseases associated with thrombosis. Thiol isomerases are a family of oxidoreductases important in protein folding and are exquisitely sensitive to the redox environment. They are essential for thrombus formation and represent a previously unrecognized layer of control of the thrombotic process. Yet, the mechanisms by which thiol isomerases function in thrombus formation are unknown. <b><i>Recent Advances:</i></b> The oxidoreductase activity of thiol isomerases in thrombus formation is controlled by the redox environment <i>via</i> oxidative changes to active site cysteines. Specific alterations can now be detected owing to advances in the chemical biology of oxidative cysteine modifications. <b><i>Critical Issues:</i></b> Understanding of the role of thiol isomerases in thrombus formation has focused largely on identifying single disulfide bond modifications in isolated proteins (<i>e.g.</i>, α<sub>IIb</sub>β<sub>3</sub>, tissue factor, vitronectin, or glycoprotein Ibα [GPIbα]). An alternative approach is to conceptualize thiol isomerases as effectors in redox signaling pathways that control thrombotic potential by modifying substrate networks. <b><i>Future Directions:</i></b> Cysteine-based chemical biology will be employed to study thiol-dependent dynamics mediated by the redox state of thiol isomerases at the systems level. This approach could identify thiol isomerase-dependent modifications of the disulfide landscape that are prothrombotic.

Antioxid Redox Signal (Antioxidants & redox signaling)
[2021, 35(13):1134-1155]

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