REVIEW: Post-Translational Oxidative Modifications of Hemostasis Proteins: Structure, Function, and Regulation

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Mark A. Rosenfeld^1,a*, Lyubov V. Yurina¹, Elizaveta S. Gavrilina¹, and Alexandra D. Vasilyeva¹

¹Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, 119334 Moscow, Russia

Received July 8, 2023; Revised September 1, 2023; Accepted September 5, 2023

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Reactive oxygen species (ROS) are constantly generated in a living organism. An imbalance between the amount of generated reactive species in the body and their destruction leads to the development of oxidative stress. Proteins are extremely vulnerable targets for ROS molecules, which can cause oxidative modifications of amino acid residues, thus altering structure and function of intra- and extracellular proteins. The current review considers the effect of oxidation on the structural rearrangements and functional activity of hemostasis proteins: coagulation system proteins such as fibrinogen, prothrombin/thrombin, factor VII/VIIa; anticoagulant proteins – thrombomodulin and protein C; proteins of the fibrinolytic system such as plasminogen, tissue plasminogen activator and plasminogen activator inhibitor-1. Structure and function of the proteins, oxidative modifications, and their detrimental consequences resulting from the induced oxidation or oxidative stress in vivo are described. Possible effects of oxidative modifications of proteins in vitro and in vivo leading to disruption of the coagulation and fibrinolysis processes are summarized and systematized, and the possibility of a compensatory mechanism in maintaining hemostasis under oxidative stress is analyzed.

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KEY WORDS: oxidation, oxidative stress, hemostasis proteins, structure, function, regulation

DOI: 10.1134/S0006297924140025

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