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

AbstractReactive 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 o r oxidative stressin  vivo are described. Possible effects of oxidative modifications of proteinsin  vitro andin  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.

Source: Biochemistry (Moscow) - January 1, 2024 Category: Biochemistry Source Type: research