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REVIEW: The Role of Halogenative Stress in Atherogenic Modification of Low-Density Lipoproteins

O. M. Panasenko1,a*, T. I. Torkhovskaya1,2, I. V. Gorudko3, and A. V. Sokolov1,4,b

1Federal Research and Clinical Center of Physico-Chemical Medicine, Federal Medical Biological Agency, 119435 Moscow, Russia

2Orekhovich Institute of Biomedical Chemistry, 119121 Moscow, Russia

3Belarusian State University, 220030 Minsk, Belarus

4Institute of Experimental Medicine, 197376 St. Petersburg, Russia

* To whom correspondence should be addressed.

Received March 26, 2019; Revised April 15, 2019; Accepted April 18, 2019
This review discusses formation of reactive halogen species (RHS) catalyzed by myeloperoxidase (MPO), an enzyme mostly present in leukocytes. An imbalance between the RHS production and body’s ability to remove or neutralize them leads to the development of halogenative stress. RHS reactions with proteins, lipids, carbohydrates, and antioxidants in the content of low-density lipoproteins (LDLs) of the human blood are described. MPO binds site-specifically to the LDL surface and modifies LDL properties and structural organization, which leads to the LDL conversion into proatherogenic forms captured by monocytes/macrophages, which causes accumulation of cholesterol and its esters in these cells and their transformation into foam cells, the basis of atherosclerotic plaques. The review describes the biomarkers of MPO enzymatic activity and halogenative stress, as well as the involvement of the latter in the development of atherosclerosis.
KEY WORDS: myeloperoxidase, reactive halogen species, halogenative stress, low-density lipoproteins, modification of low-density lipoproteins, biomarkers of halogenative stress, atherosclerosis

DOI: 10.1134/S0006297920140035