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

ABSTRACT: Significance: 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. Recent Advances: The oxidoreductase activity of thiol isomerases in thrombus formation is controlled by the redox environment via oxidative changes to active site cysteines. Specific alterations can now be detected owing to advances in the chemical biology of oxidative cysteine modifications. Critical I

SUBMITTER: Yang M 

PROVIDER: S-EPMC8817710 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature