Protective Effect of Dinitrosyl Iron Complexes with Glutathione in Red Blood Cell Lysis Induced by Hypochlorous Acid

Шумаев, К. Б.; Gorudko, Irina V.; Kosmachevskaya, O. V.; Grigorieva, Daria V.; Панасенко, О. М.; Vanin, Anatoly F.; Топунов, А. Ф.; Терехова, М. С.; Sokolov, A. V.; Черенкевич, С. Н.; Ruuge, E. K.

doi:10.1155/2019/2798154

Cited by 20 publications

(18 citation statements)

References 83 publications

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“…In this regard, we would like to note the following. We have previously shown, that physiological metabolites of NO-dinitrosyl iron complexes (DNICs) can protect both: Hb against peroxide-caused oxidative stress [196,197] and RBCs against hemolysis induced with hypochlorous acid [198]. Taking into account that we have obtained DNICs containing carnosine as a ligand [199], it is possible to suggest that carnosine DNICs can protect RBCs under carbonyl stress, by combining the protective properties of both components.…”

Section: Pharmacological Interventions and Future Perspectivesmentioning

confidence: 94%

Carbonyl Stress in Red Blood Cells and Hemoglobin

2021

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The paper overviews the peculiarities of carbonyl stress in nucleus-free mammal red blood cells (RBCs). Some functional features of RBCs make them exceptionally susceptible to reactive carbonyl compounds (RCC) from both blood plasma and the intracellular environment. In the first case, these compounds arise from the increased concentrations of glucose or ketone bodies in blood plasma, and in the second—from a misbalance in the glycolysis regulation. RBCs are normally exposed to RCC—methylglyoxal (MG), triglycerides—in blood plasma of diabetes patients. MG modifies lipoproteins and membrane proteins of RBCs and endothelial cells both on its own and with reactive oxygen species (ROS). Together, these phenomena may lead to arterial hypertension, atherosclerosis, hemolytic anemia, vascular occlusion, local ischemia, and hypercoagulation phenotype formation. ROS, reactive nitrogen species (RNS), and RCC might also damage hemoglobin (Hb), the most common protein in the RBC cytoplasm. It was Hb with which non-enzymatic glycation was first shown in living systems under physiological conditions. Glycated HbA1c is used as a very reliable and useful diagnostic marker. Studying the impacts of MG, ROS, and RNS on the physiological state of RBCs and Hb is of undisputed importance for basic and applied science.

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Section: Pharmacological Interventions and Future Perspectivesmentioning

confidence: 94%

Carbonyl Stress in Red Blood Cells and Hemoglobin

2021

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“…Кроме тиолов, лигандами ДНКЖ могут быть остатки цистеина и гистидина в белках, а также анионы фосфата [3,7]. Известно, что ДНКЖ играют важную роль в реализации биологической активности NO; в частности, они обладают антиоксидантным, цитопротекторным и гипотензивным действием [4,5,[7][8][9][10][11][12][13]. В биологических системах ДНКЖ образуются с участием пула "лабильного" железа, который пополняется за счёт железосодержащих белков [4,11].…”

Section: Introductionunclassified

“…В биологических системах ДНКЖ образуются с участием пула "лабильного" железа, который пополняется за счёт железосодержащих белков [4,11]. Ранее нами показано, что низкомолекулярные и связанные с белками ДНКЖ реагируют с активными формами кислорода и азота [7][8][9][10][11][12]. Считается, что благодаря антиоксидантным свойствам глутатион-содержащие ДНКЖ (GS-ДНКЖ) защищают кардиомиоциты в условиях окислительного стресса [13], а эритроциты при галогенирующем стрессе, вызванном гипохлоритом [12].…”

Section: Introductionunclassified

“…Ранее нами показано, что низкомолекулярные и связанные с белками ДНКЖ реагируют с активными формами кислорода и азота [7][8][9][10][11][12]. Считается, что благодаря антиоксидантным свойствам глутатион-содержащие ДНКЖ (GS-ДНКЖ) защищают кардиомиоциты в условиях окислительного стресса [13], а эритроциты при галогенирующем стрессе, вызванном гипохлоритом [12]. Вместе с тем, механизмы влияния NO и ДНКЖ на процессы свободнорадикального окисления различных биомолекул и липид-белковых комплексов остаются предметом дискуссии [1,2,[10][11][12].…”

Section: Introductionunclassified

“…Считается, что благодаря антиоксидантным свойствам глутатион-содержащие ДНКЖ (GS-ДНКЖ) защищают кардиомиоциты в условиях окислительного стресса [13], а эритроциты при галогенирующем стрессе, вызванном гипохлоритом [12]. Вместе с тем, механизмы влияния NO и ДНКЖ на процессы свободнорадикального окисления различных биомолекул и липид-белковых комплексов остаются предметом дискуссии [1,2,[10][11][12]. Исходя из вышесказанного, нам представлялось важным исследовать антиоксидантное действие ДНКЖ с различными лигандами в ходе свободнорадикального окисления липосом и липопротеинов низкой плотности (ЛНП), а также в условиях генерирования супероксидного анион-радикала.…”

Section: Introductionunclassified

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Possible mechanism of antioxidant action of dinitrosyl iron complexes

et al. 2021

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The antioxidant effect of dinitrosyl iron complexes (DNICs) was studied in various model systems. DNICs with glutathione ligands effectively inhibited Cu2+-induced peroxidation of low density lipoproteins (LDL). The antioxidant effect of DNICs with phosphate ligands and free reduced glutathione (GSH) was less pronounced. In addition, DNICs with glutathione suppressed the formation of reactive oxygen species during co-oxidation of lecithin liposomes and glucose. Free radical oxidation in this system was induced with a lipophilic azo initiator and evaluated by luminol-dependent chemiluminescence. NO sharply stimulated chemiluminescence during co-oxidation of glucose and liposomes, thus suggesting the formation of potent oxidants under these conditions. Glutathione DNICs scavenge the superoxide radical anion generated in the xanthine-xanthine oxidase system. Superoxide production was assessed by lucigenin-dependent chemiluminescence and electron paramagnetic resonance (EPR) spectroscopy. Chemiluminescence revealed the dose-dependent character of antiradical effect of glutathione DNICs; moreover, these complexes turned out to be more efficient than GSH. EPR spectra of the adducts of the DEPMPO spin trap with free radicals suggest that the interaction of glutathione DNICs and superoxide does not result in the formation of the thiyl radical of glutathione. Here we propose a mechanism of the antioxidant action of glutathione DNICs, suggesting that unstable intermediate complexes are formed upon their interaction with superoxide or lipid radicals. Further, as a result of intramolecular rearrangement, these intermediates decompose without the free radical as the by-products.

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The Biologically Relevant Coordination Chemistry of Iron and Nitric Oxide: Electronic Structure and Reactivity

et al. 2021

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Nitric oxide (NO) is an important signaling molecule that is involved in a wide range of physiological and pathological events in biology. Metal coordination chemistry, especially with iron, is at the heart of many biological transformations involving NO. A series of heme proteins, nitric oxide synthases (NOS), soluble guanylate cyclase (sGC), and nitrophorins, are responsible for the biosynthesis, sensing, and transport of NO. Alternatively, NO can be generated from nitrite by heme- and copper-containing nitrite reductases (NIRs). The NO-bearing small molecules such as nitrosothiols and dinitrosyl iron complexes (DNICs) can serve as an alternative vehicle for NO storage and transport. Once NO is formed, the rich reaction chemistry of NO leads to a wide variety of biological activities including reduction of NO by heme or non-heme iron-containing NO reductases and protein post-translational modifications by DNICs. Much of our understanding of the reactivity of metal sites in biology with NO and the mechanisms of these transformations has come from the elucidation of the geometric and electronic structures and chemical reactivity of synthetic model systems, in synergy with biochemical and biophysical studies on the relevant proteins themselves. This review focuses on recent advancements from studies on proteins and model complexes that not only have improved our understanding of the biological roles of NO but also have provided foundations for biomedical research and for bio-inspired catalyst design in energy science.

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Protective Effect of Dinitrosyl Iron Complexes with Glutathione in Red Blood Cell Lysis Induced by Hypochlorous Acid

Cited by 20 publications

References 83 publications

Carbonyl Stress in Red Blood Cells and Hemoglobin

Carbonyl Stress in Red Blood Cells and Hemoglobin

Possible mechanism of antioxidant action of dinitrosyl iron complexes

The Biologically Relevant Coordination Chemistry of Iron and Nitric Oxide: Electronic Structure and Reactivity

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