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

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Abstract

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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Abbreviations

APC:

activated protein C

Fg:

fibrinogen

Thr:

thrombin

FVII:

coagulation factor VII

TM:

thrombomodulin

HOCl:

hypochlorous acid

Met:

methionine

MetO:

methionine sulfoxide

MPO:

myeloperoxidase

PC:

protein C

PLG:

plasminogen

PL:

plasmin

PAI-1:

PLG activator inhibitor type 1

PTOMs:

post-translational oxidative modifications

ROS:

reactive oxygen species

SOD:

superoxide dismutase

TF:

tissue factor

tPA:

tissue plasminogen activator

uPA:

urokinase plasminogen activator

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Funding

The work was financially supported by the Ministry of Education and Science of the Russian Federation within the framework of the state assignment of the Institute of Biochemical Physics, Russian Academy of Sciences (project no. 122041300210-2).

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Authors and Affiliations

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

    Mark A. Rosenfeld, Lyubov V. Yurina, Elizaveta S. Gavrilina & Alexandra D. Vasilyeva

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  1. Mark A. Rosenfeld
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  2. Lyubov V. Yurina
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  3. Elizaveta S. Gavrilina
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Contributions

M.A.R. conceptualization, writing (original draft preparation, supervision, reviewing and editing). L.V.Yu. visualization, writing (original draft preparation). E.S.G. visualization, writing (original draft preparation). A.D.V. writing (original draft preparation, visualization, reviewing and editing).

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Correspondence to Mark A. Rosenfeld.

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This work does not contain any studies involving human and animal subjects. The authors of this work declare that they have no conflicts of interest.

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Translated from Uspekhi Biologicheskoi Khimii, 2024, Vol. 64, pp. 29-72.

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Rosenfeld, M.A., Yurina, L.V., Gavrilina, E.S. et al. Post-Translational Oxidative Modifications of Hemostasis Proteins: Structure, Function, and Regulation. Biochemistry Moscow 89 (Suppl 1), S14–S33 (2024). https://doi.org/10.1134/S0006297924140025

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