Laboratory of physical-chemical methods of investigation and analysis is a part of the Department of Biophysics, the FSBIS SRI PCM FMBA of Russia. The laboratory was established on March 01, 1999 by an order of the Director of the Institute, Prof. Yu.M. Lopukhin, a Full Member of the Russian Academy of Medical Sciences.
Tel., fax: +7 (499) 246-44-90;
Panasenko, Oleg Mikhailovich
Doctor of Biological Sciences, Professor, a recipient of the Russian Federation Government Award
Murina, Marina Alexeevna, Doctor of Biological Sciences, Principal Researcher, Doctor of Biological Sciences, Professor, a recipient of the Russian Federation Government Award
Vakhrusheva, Tatyana Valentinovna, Senior Researcher, Candidate of Biological Sciences
Vlasova, Irina Ivanovna, Senior Researcher, Candidate of Physical and Mathematical Sciences
Sokolov, Alexej Victorovich, Senior Researcher, Candidate of Biological Sciences
Chekanov, Andrei Vasilievich, Researcher, Candidate of Biological Sciences
Chudina, Nataliya Alexandrovna, Senior Researcher, Candidate of Medical Sciences
Kostevich, Valeriya Alexandrovna, Junior Researcher
Petrova, Anastasiya Olegovna, Junior Researcher, Candidate of Biological Sciences
Fesenko, Oksana Dmitrievna, Research Assistant
Timofeyev, Igor Olegovich, Research Assistant
Topics of scientific interest
Problem under research:
Elucidation of the mechanisms underlying the damage caused to the components of blood and vessel wall by activated phagocytes in the conditions of oxidative/galogenative stress and inflammation.
Lines of research:
- Regulating myeloperoxidase activity to reveal the mechanisms for the directed synthesis of hypohalous acids at inflammatory sites and the reduction of hypohalous acid-induced damage to healthy tissue.
- Role of myeloperoxidase in the modification of blood lipoproteins and the development of atherosclerosis.
- Halogenated lipids, proteins and lipoproteins as modulators of cell activity and inflammation.
- Modulation of blood cell functions following the binding of MPO to the cell membrane in the conditions of the development of oxidative/halogenative stress and inflammation.
- Degradation of single-walled carbon nanotubes by myeloperoxidase-generated oxidants as a mechanism for reducing carbon nanotube toxicity and improving their biocompatibility.
- A physical chemical study of the reactivity properties and the structural basis of stability of amino acid chloramines formed upon phagocyte activation, and an investigation of their action on blood cells.
- Development of antithrombotic drugs designed on the basis of the analogues of taurine chloramine.
Major scientific achievements
Regulating myeloperoxidase activity to reveal the mechanisms for the directed synthesis of hypohalous acids at inflammatory sites and the reduction of hypohalous acid-induced damage to healthy tissue
Myeloperoxidase (MPO), a heme-containing enzyme, is secreted by activated neutrophils and monocytes into extracellular space at sites of inflammation. The major function of MPO is the production of hypohalous acids (HOCl, HOBr) which are strong oxidants. On the one hand, due to such enzymatic activity, MPO fulfills its antimicrobial role, defending the body from pathogens. On the other hand, MPO participates in a number of events involved in damage of the body’s own tissues. In our study, the factors that can influence in vivo the halogenating activity of MPO were investigated. As the results show, lowering pH and the presence of small amounts of phenolic peroxidase substrates can cause an increase in HOCl production by MPO.
Ceruloplasmin (CP), an acute phase inflammatory protein, was found to inhibit, by binding to MPO, the enzyme activity. This was proved by three independent methods: chemiluminescence; estimation of MPO chlorination activity with the taurine chlorination assay; estimation of MPO peroxidase activity. The bigger the substrate molecule size was, the higher the inhibitory effect of CP on MPO peroxidase activity. Thus, the inhibitory effect of CP at the level of the MPO-CP complex was apparently due to steric hindrance, which resulted from the MPO-CP interaction, for substrate binding to the MPO molecule.
Role of myeloperoxidase in the modification of blood lipoproteins and the development of atherosclerosis
Human blood low-density lipoproteins (LDL) modified by HOCl cause cholesterol accumulation in vascular wall cells, thus promoting the development of atherosclerosis. HOCl is produced by the enzyme myeloperoxidase (MPO) during the halogenation cycle. In our study, we showed by affinity chromatography on Sepharose-bound MPO that LDL binds to MPO. The binding was inhibited at ionic strength greater than 0.3 M NaCl or at pH lower than 3.6, indicating the ionic nature of the interaction between MPO and LDL. Using lipid spin probes, we found that interaction of MPO with LDL had no effect on the surface lipid domain on the LDL particle, which suggested that LDL lipids were not involved in the MPO-LDL interaction. At the same time, antibodies against apo B-100 blocked MPO binding to LDL. Among synthetic anionic peptides (1EEEMLEN7, 53VELEVPQ59 and 445EQIQDDCTGDED456) mimicking the apo B-100 sequence fragments, only the latter was able to dissociate MPO from the MPO-LDL complex. Thus, the most probable site for MPO binding on LDL involves the apo B-100 sequence stretch 445 – 456.
We investigated the effects of the peptide 445EQIQDDCTGDED456 (P445-4456) as well as of inhibitors and modulators of the halogenating activity of MPO, such as ceruloplasmin (CP), 4-aminobenzoic acid hydrazide (ABAH) and thiocyanate (SCN-), on the accumulation of cholesterol and its esters in monocytes/macrophages during incubation with LDL that had been variously modified by MPO-dependent oxidation and halogenation. Based on the results, we suggest the summarized scheme (Fig.) for the participation of MPO, MPO-generated reactive halogen species, the uncoupling agent P445-456 and inhibitors/modulators of the halogenating MPO activity (ABAH, CP, SCN-) in the pro-atherogenic modification of LDL and the formation of foam cells.
MPO binding to LDL results in the site-specific modification, which involves mainly the LDL protein, as well as in the halogenation/peroxidation of lipids by HOCl and HOBr, the species produced by MPO during the halogenation cycle. Modified LDL can stimulate leukocyte activation, thus inducing the oxidative burst and MPO exocytosis from neutrophils and monocytes (Fig. exemplifies these events for monocytes). The released MPO binds to LDL and causes, by using leukocyte-produced H2O2 as a substrate, their further modification, thereby forming the vicious circle to produce modified LDL. The modified LDL within the MPO-LDL complex is engulfed by monocytes/macrophages, which leads to intracellular cholesterol accumulation and foam cell formation. Inhibitors/modulators of the halogenating MPO activity (ABAH, CP, SCN-) as well as the uncoupling agent P445-456 prevent LDL oxidative/halogenative modification. This decreases LDL uptake by macrophages and, hence, decreases the intracellular accumulation of cholesterol and its esters. This also breaks the vicious circle involving neutrophil/monocyte activation and the formation of modified LDL. The presented hypothesis is supported by our finding of the complexes of MPO and apo B-100-containing lipoproteins in atherosclerotic patients whose plasma MPO levels were higher than 800 ng/ml.
Halogenated lipids, proteins and lipoproteins as modulators of cell activity and inflammation
Halogenated lipids, which are formed in MPO-catalyzed reactions, may play a role of a regulator of the functional activity of cells. We investigated the effects chloro- and bromohydrins formed in the reactions of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) with HOCl or HOBr, respectively, may have on several functional responses of human neutrophils, such as H2O2 production, degranulation (MPO exocytosis) and aggregation. Chloro- and bromohydrins of POPC were shown to induce neutrophil priming, which was manifested in a marked increase in cellular response to stimuli such as N-formyl-Met-Leu-Phe and Solanum tuberosum lectin. Results allow the proposal that halogenated lipids, which may form in vivo in MPO-catalyzed reactions, may be considered as a novel class of biologically active compounds, which are potentially able to exert a priming effect on myeloid cells at sites of inflammation and, hence, may be involved in modulation of inflammatory response.
Secretory phospholipase A2, group IIA (group II sPLA2) is actively involved in inflammation. The enzyme damages the bacterial cell wall and induces the formation of bioactive lipid mediators. Halogenated phospholipids (chloro- and bromohydrins) are formed along with oxidized phospholipids as a result of the reaction of HOCl or HOBr with unsaturated bonds of acyl chains. In our study, we investigated the influence of chloro- and bromohydrins of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) on the activity of group II sPLA2. Contrary to POPC, chloro- and bromohydrins of POPC (POPC-Cl and POPC-Br, respectively) were not susceptible to hydrolysis by group II sPLA2. Moreover, the enzyme failed in the presence of POPC-Cl or POPC-Br to cleave phospholipids that are its substrates. In contrast to oxidized phospholipids, which stimulate group II sPLA2 activity, halogenohydrins of POPC inhibited the purified group II sPLA2 as well as group II sPLA2 in blood serum of patients. The results suggest that halogenated phospholipids formed in vivo in MPO-dependent reactions may be considered as a novel class of biologically active compounds that are potentially capable of regulating group II sPLA2 activity at sites of inflammation and, hence, may be important modulators of inflammatory response.
Human serum albumin (HSA) modified with HOCl or HOBr (HSA-Cl/Br) was shown to induce degranulation of azurophilic granules (release of MPO), degranulation of specific granules (release of lactoferrin), NADPH-oxidase activation , cell shape distortion, actin cytoskeleton reorganization and to increase luminol-dependent chemiluminescence after stimulation with phorbol-12-myristate-13-acetate. HSA-Cl/Br-induced neutrophil activation, as observed by H2O2 generation and MPO exocytosis, was inhibited by anti-CD18 (an antibody directed against β-subunit of β2-integrins), genistein (a tyrosine kinase inhibitor) or wortmannin (a phosphatidylinositol-3-kinase (PI3K) inhibitor). Thus, MPO-dependent modification of HSA renders it the ability to activate neutrophil effector functions (by integrin-dependent pathways through activation of tyrosine kinases and PI3K and cytoskeleton reorganization), operating on the principle of positive feedback and acting as an inflammatory mediator.
Neutrophil incubation with HOCl- or HOBr-modified human blood low-density lipoproteins (LDL) resulted in a significant increase in the release of MPO (a marker for azurophilic granules), as observed by an increase in the MPO concentration and activity in the extracellular medium. At the same time, no increase in the extracellular amount of lactoferrin, a marker for specific granules, was detected. The results suggest that LDL modified in the conditions of oxidative/halogenative stress at sites of inflammation may play a regulatory role in the selective exocytosis of MPO.
A significant positive correlation was found between MPO activity in the blood plasma from children with severe burns and a degree of the increase in luminol-dependent chemiluminescence in neutrophils isolated from the blood of healthy donors and activated by phorbol-12-myristate-13-acetate in the presence of the albumin fraction obtained from the corresponding sample of the burn patient plasma. The results support the hypothesis that proteins modified with MPO in the conditions of oxidative/halogenative stress stimulate neutrophil activation, which leads to exocytosis of MPO, a key element in halogenative stress, and closing the vicious circle of neutrophil activation at inflammatory sites.
Patients suffering from diabetes mellitus without vascular diseases or diabetes mellitus complicated with ischemic heart disease exhibited elevated plasma levels of the activity and concentration of MPO, a marker for neutrophil azurophilic granules. Plasma levels of lactoferrin, a marker for neutrophil specific granules, however, did not differ from those in healthy donors. In vitro experiments showed that HOCl-modified HSA, an in vivo product of MPO, induces selective degranulation of azurophilic granules, which is manifested by an increase in the extracellular concentration and activity of MPO. The results obtained suggest that the HOCl-modified protein found at inflammatory sites may act as a regulator of the selective exocytosis of MPO in neutrophils, increasing neutrophil bactericidal activity on the principle of positive feedback or by closing the vicious circle of cytotoxic effects of oxidants produced in MPO-dependent reactions.
Modulation of blood cell functions following the binding of MPO to the cell membrane in the conditions of the development of oxidative/halogenative stress and inflammation
Human platelets were examined for structural and functional changes caused by MPO. Using confocal laser microscopy, we detected the carbohydrate-independent binding of MPO to the platelet plasma membrane. MPO was found to potentiate ADP- and thrombin-induced platelet aggregation, which was associated with the depolymerization of perimembranous F-actin and an increase in the concentration of intracellular free calcium ions (Ca2+) due to store-operated Ca2+ entry into the cytoplasm. The data obtained suggest that MPO is a pro-inflammatory risk factor capable of increasing thrombus formation upon inflammation and associated pathologies.
MPO binding onto the erythrocyte surface was found to affect plasma membrane stability, causing a decrease in cell resistance to acid and osmotic hemolysis. The increase in hemolysis in the presence of MPO was mediated directly by the binding of MPO to the plasma membrane components, but not by MPO’s enzymatic activity. Using neuraminidase and different carbohydrates, we found a contribution of carbohydrate-mediated electrostatic interactions to the MPO-dependent changes in structural properties of erythrocytes. The effect under discussion was found to be caused by MPO binding to the glycosylated components of the erythrocyte plasma membrane.
Degradation of single-walled carbon nanotubes by myeloperoxidase-generated oxidants as a mechanism for reducing carbon nanotube toxicity and improving their biocompatibility
Comparison of the ability of different peroxidases to degrade single-walled carbon nanotubes allowed us to conclude that only HOCl, a major oxidant produced by myeloperoxidase, may act as an agent capable of degrading the nanotubes in vivo. Single-walled carbon nanotubes treated with HOCl exerted less negative impact, as compared with that of intact nanotubes, on the immune system after intraperitoneal injection of the nanotubes in experimental animals. Single-walled carbon nanotubes were shown to cause platelet aggregation and neutrophil activation in whole blood samples. Coating the nanotubes with serum albumin reduced their capacity to induce platelet aggregation.
A physical chemical study of the reactivity properties and the structural basis of stability of amino acid chloramines formed upon phagocyte activation, and an investigation of their action on blood cells
We found a new class of covalent inhibitors (antiaggregants) of platelet activity, which represent chloramine derivatives of biogenic compounds such as amino acids, taurine and peptides. In blood, these inhibitors exhibit a marked selectivity for the interaction with platelets. They all, independently of the type, have a generalized action, inhibiting all functional activities of platelets.
Development of antithrombotic drugs designed on the basis of the analogues of taurine chloramine
We purpose designed and studied new taurine chloramine analogues that have high stability, hemoselectivity for sulfhydryl groups in proteins, and specific antiaggregant pharmacological activity. In these compounds, the chemically reactive group is the chloramine group which covalently modifies proteins of the platelet plasma membrane.
Since the beginning of the laboratory, its present and past members authored the dissertations listed below.
Candidate of Sciences dissertations:
1. Adnoral, N.V.: “The mechanism of the antithrombotic action of biogenic chloramines” (1999), a Candidate of Medical Sciences dissertation in Biophysics.
2. Chudina, N.A.: “Physical-chemical properties and antiaggregatory action of biogenic chloramines” (2002), a Candidate of Medical Sciences dissertation in Biophysics.
3. Pestryaeva, L.A.: “Development of informative laboratory criteria for assessing the severity of autointoxication during pathological pregnancy” (2002), a Candidate of Biological Sciences dissertation in Biochemistry and Clinical Diagnostics.
4. Belakina, N.S.: “Luminol-enhanced chemiluminescence of stimulated neutrophils: intracellular and extracellular sources of luminescence, the role of active chlorine compounds” (2004), a Candidate of Medical Sciences dissertation in Biophysics.
5. Chekanov, A.V.: “Mechanism of the interaction of hypochlorite and hypochlorite generating systems with organic hydroperoxides” (2004), a Candidate of Biological Sciences dissertation in Biophysics and Biochemistry.
6. Mel’nichenko, A.A.: “Aggregation of circulating modified low-density lipoproteins. The role in intracellular cholesterol accumulation” (2006), a Candidate of Biological Sciences dissertation in Biochemistry and Biophysics.
7. Aksyonov, D.V.: “Modulation of the aggregation of human blood low-density lipoproteins” (2007), a Candidate of Medical Sciences dissertation in Pathological Physiology.
8. Petrova, A.O.: “Amino acid chloramines as inhibitors of platelet aggregation: the physical-chemical properties and mechanism of action” (2012), a Candidate of Biological Sciences dissertation in Biophysics.
Doctor of Sciences dissertations:
1. Panasenko, O.M.: “Hypochlorite and oxidative modification of human blood lipoproteins” (1998), a Doctor of Biological Sciences dissertation in Biophysics and Biochemistry.
2. Murina, M.A.: “Physical-chemical mechanisms of the action of chloramine derivatives of biogenic compounds and sodium hypochlorite on platelets” (2000), a Doctor of Biological Sciences dissertation in Biophysics.
Our laboratory has its own or has access to facilities and equipment for instrumental methods such as:
- Spin label and probe method
- Spin-trapping method
- Mass spectrometry
For many years the laboratory collaborated and continues the collaboration with a number of research groups in and outside the country, namely, within:
- Department of Biophysics, Medical-Biological Faculty, N.I. Pirogov Russian National Research Medical University, Moscow, Russia; Head of the Department: Prof. A.N. Osipov
- Department of Molecular Genetics, Research Institute of Experimental Medicine, Saint-Petersburg, Russia; Head of the Department: Prof. V.B. Vasiliev
- Department of Biophysics, Belarusian State University, Minsk, Belarus; Head of the Department: Prof. S.N. Cherenkevich
- Institute of Medical Physics and Biophysics, University of Leipzig, Germany; Director of the Institute: Prof. K. Arnold
- Institute of Physiological Chemistry 1, University of Duesseldorf, Germany; Director of the Institute: Prof. Sies
- Center for Free Radical Research, Department of Environmental and Occupational Health, Graduate School of Public Health, University of Pittsburgh, USA; Head of the Center: Prof. V. Kagan
Our current projects, which are supported by the Russian Foundation for Basic Research (RFBR), are listed below:
- «Elucidation of the mechanisms of regulation of cell functions by natural reactive oxidants representing the irreversible inhibitors of molecular targets» (RFBR Grant No. 12-04-00951-а, 2012-2014; Principal Investigator: Murina, M.A)
- «Non-covalent functionalization of single-walled carbon nanotubes as a way to regulate their interaction with platelets and neutrophils » (RFBR Grant No. 12-04-01293-a, 2012-2014; Principal Investigator: Vlasova, I.I)
- «The role of body’s pro- and anti-halogenative systems in the generation of halogenative stress and in low density lipoprotein modification leading to the development of atherosclerosis» (RFBR Grant No. 14-04-00807a, 2014-2016; Principal Investigator: Panasenko, O.M.)
- Sokolov A.V., Kostevich V.A., Runova O.L., Gorudko I.V., Vasilyev V.B., Cherenkevich S.N., Panasenko O.M. Proatherogenic modification of LDL by surface-bound myeloperoxidase. Chem. Phys. Lipids. 2014. V. 180. P. 72-80.
- Gorudko I.V., Grigorieva D.V., Shamova E.V., Kostevich V.A., Sokolov A.V., Mikhalchik E.V., Cherenkevich S.N., Arnhold J., Panasenko O.M. Hypohalous acid-modified human serum albumin induces neutrophil NADPH oxidase activation, degranulation, and shape change. Free Radic. Biol. Med. 2014. V. 68. P. 326-334.
- Panasenko O.M., Gorudko I.V., Sokolov A.V. Hypochlorous Acid as a precursor of free radicals in living systems. Biochemistry (Mosc). 2013. V. 78(13). P. 1466-1489.
- Gorudko I.V., Sokolov A.V., Shamova E.V., Grudinina N.A., Drozd E.S., Shishlo L.M., Grigorieva D.V., Bushuk S.B., Bushuk B.A., Chizhik S.A., Cherenkevich S.N., Vasilyev V.B., Panasenko O.M. Myeloperoxidase modulates human platelet aggregation via actin cytoskeleton reorganization and store-operated calcium entry. Biology Open. 2013. V. 2. P. 916-923.
- Vakhrusheva T.V, Gusev A.A., Gusev S.A., Vlasova I.I. Albumin reduces thrombogenic potential of single-walled carbon nanotubes. Toxicology Letters. 2013. V. 221(2). P. 137-145.
- Grigorieva D.V., Gorudko I.V., Sokolov A.V., Kosmachevskaya O.V., Topunov A.F., Buko I.V., Konstantinova E.E., Cherenkevich S.N., Panasenko O.M. Measurement of plasma hemoglobin peroxidase activity. Bull. Exp. Biol. Med. 2013. V. 155(1). P. 118-121.
- Korotaeva A., Samoilova E., Pavlunina T., Panasenko O.M. Halogenated phospholipids regulate secretory phospholipase A2 group IIA activity. Chem. Phys. Lipids. 2013. V. 167-168. P. 51-56.
- Mikhalchik E.V., Smolina N.V., Astamirova T.S., Gorudko I.V., Grigorieva D.V., Ivanov V.A., Sokolov A.V., Kostevich V.A., Cherenkevich S.N., Panasenko O.M. Human serum albumin modified under oxidative/halogenative stress enhances luminal-dependent chemiluminescence of human neutrophils Biophysics. 2013. V. 58 (4). P. 530–536.
- Vlasova I.I., Vakhrusheva T.V., Sokolov A.V., Kostevich V.A., Gusev A.A., Gusev S.A., Melnikova V.I., Lobach A.S. PEGylated single-walled carbon nanotubes activate neutrophils to increase production of hypochlorous acid, the oxidant capable of degrading nanotubes. Toxicology and Applied Pharmacology. 2012. V. 264(1). P. 131-142.
- Gorudko I.V., Shamova E.V., Shishlo L.M., Mukhortova A.V., Prokhorova V.I., Panasenko O.M., Gusev S.A., Cherenkevich S.N.. Glutathione-dependent regulation of platelet aggregation with neutrophils and tumor cells. Biophysics. 2012. V. 57 (1). P. 76-80.
- Sokolov A.V., Solovyov K.V., Kostevich V.A., Chekanov A.V., Pulina M.O., Zakharova E.T., Shavlovski M.M., Panasenko O.M., Vasilyev V.B. Protection of ceruloplasmin by lactoferrin against hydroxyl radicals is pH dependent. Biochem. Cell Biol. 2012. V. 90. P. 397–404.
- Gorudko I.V., Kostevich V.A., Sokolov A.V., Shamova E.V., Buko I.V., Konstantinova E.E., Vasiliev V.B., Cherenkevich S.N., Panasenko O.M. Functional activity of neutrophils in diabetes Mellitus and coronary heart disease: role of myeloperoxidase in the development of oxidative stress. Bull. Exp. Biol. Med. 2012. V. 154 (1). P. 23-26.
- Melnichenko A.A., Aksenov D.V., Myasoedova V.A., Panasenko O.M., Yaroslavov A.A., Sobenin I.A., Bobryshev Y.V., Orekhov A.N. Pluronic block copolymers inhibit low density lipoprotein self-association. Lipids. 2012. V. 47. P. 995-1000.
- Gorudko I.V., Kostevich V.A., Sokolov F.V., Buko I.V., Konstantinova E.E., Tsapaeva N.L., Mironova E.V., Zakharova E.T., Vasilyev V.B., Cherenkevich S.N., Panasenko O.M. Increased myeloperoxidase activity is a risk factor for ischemic heart disease in patients with diabetes mellitus. Biochemistry (Moscow). Supp. Series B: Biomedical Chemistry. 2011. V. 5. P. 307-312.
- Roshchupkin D.I., Murina M.A., Sergienko V.I.. Covalent chloramine inhibitors of blood platelet functions: computational indices for their reactivity and antiplatelet activity. Biophysics. 2011. V. 56 (5). P. 897-904.
- Sokolov A.V., Chekanov A.V., Kostevich V.A., Aksenov D.V., Vasilyev V.B., Panasenko O.M. Revealing binding sites for myeloperoxidase on the surface of human low density lipoproteins. Chem. Phys. Lipids. 2011. V. 164. P. 49–53.
- Baranova O.A., Chekanov A.V., Karneev A.N., Mironova O.P., Miachin I.V., Panasenko O.M., Solov'eva E.Iu., Fedin A.I. A search for new markers of oxidative stress in brain ischemia for the optimization of treatment approaches. Zh. Nevrol. Psikhiatr. Im. S.S. Korsakova. 2011. V. 111(12). P. 25-31.
- Vlasova I.I., Sokolov A.V., Arnhold J. The free amino acid tyrosine enhances the chlorinating activity of human myeloperoxidase. Journal of Inorganic Biochemistry. 2012. V. 106(1). P. 76-83.
- Vlasova I.I., Feng W.H., Goff J.P., Giorgianni A., Do D., Gollin S.M., Lewis D.W., Kagan V.E., Yalowich J.C. Myeloperoxidase-dependent oxidation of etoposide in human myeloid progenitor CD34+ cells. Molecular Pharmacology. 2011. V. 79(3). P. 479-487.
- Vlasova I.I., Sokolov A.V., Chekanov A.V., Kostevich V.A., Vasilyev V.B.. Myeloperoxidase-induced biodegradation of single-walled carbon nanotubes
is mediated by hypochlorite. Russian Journal of Bioorganic Chemistry. 2011. V. 37(4). P. 453-463.
- Vlasova I.I., Vakhrusheva T.V., Sokolov A.V., Kostevich V.A., Ragimov A.A. Peroxidase-induced degradation of single-walled carbon nanotubes: hypochlorite is a major oxidant capable of in vivo degradation of carbon nanotubes. Journal of Physics: Conference Series. 2011. V. 291: 012056.
- Sokolov A.V., Aseychev A.V., Kostevich V.A., Gusev A.A., Gusev S.A., Vlasova I.I. Functionalization of single-walled carbon nanotubes regulates their effect on hemostasis. Journal of Physics: Conference Series. 2011. V. 291: 012054.
- Panasenko O.M., Sergienko V.I. Halogenizing stress and its biomarkers. Vestn. Ross. Akad. Med. Nauk. 2010. № 1. P. 27-39.
- Sokolov A.V., Ageeva K.V., Cherkalina O.S., Pulina M.O., Zakharova E.T., Prozorovskii V.N., Aksenov D.V., Vasilyev V.B., Panasenko O.M. Identification and properties of complexes formed by myeloperoxidase with lipoproteins and ceruloplasmin. Chem. Phys. Lipids. 2010. V. 163. P. 347–355.
- Gorudko I.V., Vakhrusheva T.V., Mukhortova A.V., Cherenkevich S.N., Timoshenko A.V., Sergienko V.I., Panasenko V.I. The priming effect of halogenated phospholipids on the functional responses of human neutrophils. Biochemistry (Moscow), Series A: Membrane and Cell Biology. 2010. V. 4 (3). P. 262-271.
- Kagan V.E., Konduru N.V., Feng W., Allen B.L., Conroy J., Volkov Y., Vlasova I.I., Belikova N.A., Yanamala N., Kapralov A., Tyurina Y.Y., Shi J., Kisin E.R., Murray A.R., Franks J., Stolz D., Gou P., Klein-Seetharaman J., Fadeel B., Star A., Shvedova A.A. Carbon nanotubes degraded by neutrophil myeloperoxidase induce less pulmonary inflammation. Nature Nanotechnology. 2010. V. 5(5). P. 354-359.
- Gorudko I.V., Tcherkalina O.S., Sokolov A.V., Pulina M.O., Zakharova E.T., Vasilyev V.B., Cherenkevich S.N., Panasenko O.M.. New approaches to the measurement of the concentration and peroxidase activity of myeloperoxidase in human blood plasma. Russian Journal of Bioorganic Chemistry. 2009. V. 35(5). P. 566-575.
- Murina M.A., Roshchupkin D.I., Chudina N.A., Petrova A.O., Sergienko V.I. Antiaggregant effect of taurine chloramines in the presence of serum albumin. Bull. Exp. Biol. Med. 2009. V. 147 (6). P. 704-707.
- Kapralov A., Vlasova I.I., Feng W., Maeda A., Walson K., Tyurin V.A., Huang Z., Aneja R.K., Carcillo J., Bayir H., Kagan V.E. Peroxidase activity of hemoglobin x haptoglobin complexes: covalent aggregation and oxidative stress in plasma and macrophages. Journal of Biological Chemistry. 2009. V. 284 (44). P. 30395-30407.
- Panasenko O.M., Chekanov A.V., Vlasova I.I., Sokolov A.V., Ageeva K.V., Pulina M.O., Cherkalina O.S., Vasil’ev V.B. Influence of ceruloplasmin and lactoferrin on the chlorination activity of leukocyte myeloperoxidase assayed by chemiluminescence. Biophysics. 2008. V. 53 (4). P. 268-272.
- Sokolov A.V., Ageeva K.V., Pulina M.O., Cherkalina O.S., Samygina V.R., Vlasova I.I., Panasenko O.M., Zakharova E.T., Vasilyev V.B. Ceruloplasmin and myeloperoxidase in complex affect the enzymatic properties of each other. Free Rad. Res. 2008. V. 42. P. 989-998.
- Murina M.A., Roshchupkin D.I., Kravchenko N.N., Petrova A.O., Sergienko V.I.. Antiaggregant effects of biogenic chloramines. Bull. Exp. Biol. Med. 2007. V. 144 (3). P. 464-470.
- Panasenko O.M., Mel’nichenko A.A., Aksenov D.V., Tertov V.V., Kaplun V.V., Sobenin I.A., Orekhov A.N. Oxidation-induced aggregation of LDL increases their uptake by smooth muscle cells from human aorta. Bull. Exp. Biol. Med. 2007. V. 143 (2). P. 200-203.
- Chekanov A.V., Osipov A.N., Vladimirov Yu.A., Sergienko V.I., Panasenko O.M. A comparative spin trapping study of the interaction of hypobromous and hypochlorous acids with tert-butyl hydroperoxide. Biophysics. 2007. V. 52 (1). P. 1-7.
- Panasenko O.M., Vakhrusheva T.V., Vlasova I.I., Chekanov A.V., Baranov Yu.V., Sergienko V.I. Role of myeloperoxidase-mediated modification of human blood lipoproteins in atherosclerosis development. Bull. Exp. Biol. Med. 2007. V. 144 (3). P. 428-431.
- Lankin V.Z., Tikhaze A.K., Kapel’ko V.I., Shepel’kova G.S., Shumaev K.B., Panasenko O.M., Konovalova G.G., Belenkov Yu.N. Mechanisms of oxidative modification of low density lipoproteins under conditions of oxidative and carbonyl stress. Biochemistry (Moscow). 2007. V. 72 (10). P. 1081-1090.
- Panasenko O.M., Vakhrusheva T., Tretyakov V., Spalteholz H., Arnhold J. Influence of chloride on modification of unsaturated phosphatidylcholines by the myeloperoxidase/hydrogen peroxide/bromide system. Chem. Phys. Lipids. 2007. V. 149. P. 40–51.
- Roshchupkin D.I., Belakina N.S., Murina M.A. Luminol-enhanced chemiluminescence of rabbit polymorphonuclear leukocytes: The nature of oxidants that directly cause luminol oxidation. Biophysics. 2006. V. 51 (1). P. 79-86.
- Murina M.A., Savel’eva E.L., Roshchupkin D.I. Mechanism of the action of biogenic chloramines and hypochlorite on the initial aggregation of platelets. Biophysics. 2006. V. 51 (2). P. 258-263.
- Vlasova I.I., Tyurin V.A., Kapralov A.A., Kurnikov I.V., Osipov A.N., Potapovich M.V., Stoyanovsky D.A., Kagan V.E. Nitric oxide inhibits peroxidase activity of cytochrome C cardiolipin complex and blocks cardiolipin oxidation. J. Biol. Chem. 2006. V. 281. P. 14554-14562.
- Spalteholz H., Panasenko O.M., Arnhold J. Formation of reactive halide species by myeloperoxidase and eosinophil peroxidase. Arch. Biochem. Biophys. 2006. V. 445. P. 225-234.
- Vakhrusheva T., Panasenko O. Chondroitin 6-sulfate and dextran sulfate promote hypochlorite-induced peroxidation of phosphatidylcholine liposomes. Chem. Phys. Lipids. 2006. V. 140. P. 18-27.
- Panasenko O.M., Spalteholz H., Schiller J., Arnhold J. Leukocytic myeloperoxidase-mediated formation of bromohydrins and lysophospholipids from unsaturated phosphatidylcholines. Biochemistry (Moscow). 2006. V. 71 (5). P. 571-580.
- Vlasova I.I., Arnhold J., Osipov A.N., Panasenko O.M. pH-Dependent regulation of myeloperoxidase activity. Biochemistry (Moscow). 2006. V. 71 (6). P. 667-677.
- Chekanov A.V., Panasenko O.M., Osipov A.N., Matveeva N.S., Kazarinov K.D., Vladimirov Yu.A., Sergienko V.I. Reaction of hypochlorite with fatty acid hydroperoxide results in free radical formation. Biophysics. 2005. V. 50 (1). P. 8-14.
- Dobretsov G.E., Gularyan S.K., Panasenko O.M., Orekhov A.N., Isakova S.I. Low-density lipoproteins with different aggregation ability. Biophysics. 2005. V. 50 (2). P. 265-268.
- Melnichenko A.A., Tertov V.V., Ivanova O.A., Aksenov D.V., Sobenin I.A., Popov E.V., Kaplun V.V., Suprun I.V., Panasenko O.M., Orekhov A.N. Desialylation decreases the resistance of apo B-containing lipoproteins to aggregation and increases their atherogenic potential. Bull. Exp. Biol. Med. 2005. V. 140 (1). P. 51-54.
- Panasenko O.M., Chekanov A.V., Arnhold J., Sergienko V.I., Osipov A.N., Vladimirov Yu.A. Generation of free radicals during decomposition of hydroperoxide in the presence of myeloperoxidase or activated neutrophils. Biochemistry (Moscow). 2005. V. 70 (9). P. 998-1004.
- Aksenov D.V., Melnichenko A.A., Suprun I.V., Yanushevskaya E.V., Vlasik T.N., Sobenin I.A., Panasenko O.M., Orekhov A.N. Phospholipid hydrolysis with phospholipases A2 and C impairs apolipoprotein B-100 conformation on the surface of low density lipoproteins by reducing their association resistance. Bull. Exp. Biol. Med. 2005. V. 140 (4). P. 419-422.
- Panasenko O.M., Aksenov D.V., Melnichenko A.A., Suprun I.V., Yanushevskaya E.V., Vlasik T.N., Sobenin I.A., Orekhov A.N. Proteolysis of apoprotein B-100 impairs its topography on LDL surface and reduces LDL association resistance. Bull. Exp. Biol. Med. 2005. V. 140 (5). P. 521-525.
- Vakhrusheva T.V., Panasenko O.M., Melnichenko A.A., Orekhov A.N. A comparative spin probe study of the lipid phase in native and circulating multiply modified low-density lipoproteins of human blood. Biophysics. 2005. V. 50 (4). P. 571-577.
- Murina M.A., Roshchupkin D.I., Belakina N.S., Filippov S.V., Khalilov E.M. Chemiluminescence in the stimulated polymorphonuclear leukocytes-luminol system: suppression by thiols. Biophysics. 2005. V. 50 (6). P. 949-952.
- Spalteholz H., Wenske K., Panasenko O.M., Schiller J., Arnhold J. Evaluation of products upon the reaction of hypochlorous acid with unsaturated phosphatidylcholines. Chem. Phys. Lipids. 2004. V. 129. P. 85-96.
- Suprun I.V., Melnichenko A.A., Yanushevskaya E.V., Vlasik T.N., Sobenin I.A., Panasenko O.M., Orekhov A.N. Antigenic differences between apo-B in native and circulating modified low-density lipoproteins. Bull. Exp. Biol. Med. 2004. V. 138 (1). P. 42-44.
- Panasenko O.M., Suprun I.V., Melnichenko A.A., Sobenin I.A., Orekhov A.N. Low ionic strength promotes association of circulating modified LDL in human blood. Bull. Exp. Biol. Med. 2004. V. 138 (3). P. 248-250.
- Suprun I.V., Melnichenko A.A., Sobenin I.A., Panasenko O.M., Orekhov A.N. Resistance of native and circulating modified low-density lipoproteins in human blood to association. Bull. Exp. Biol. Med. 2004. V. 138 (4). P. 380-383.
- Murina M.A., Chudina N.A., Roshchupkin D.I., Belakina N.S., Sergienko V.I. Structure and oxidation capacity of amino acid chloramine derivatives and their effects on platelet aggregation. Bull. Exp. Biol. Med. 2004. V. 138 (6). P. 559-561.
- Murina M.A., Belakina N.S., Roshchupkin D.I. Luminol chemiluminescence from resting polymorphonuclear leukocytes in the presence of biogenic chloramines. Biophysics. 2004. V. 49 (6). P. 986-990.
- Panasenko O.M., Spalteholz H., Schiller J., Arnhold J. Myeloperoxidase-induced formation of chlorohydrins and lysophospholipids from unsaturated phosphatidylcholines. Free Radic. Biol. Med. 2003. V. 34. P. 553-562.
- Panasenko O.M., Osipov A.N., Chekanov A.V., Arnhold J., Sergienko V.I. Peroxyl radical is produced upon the interaction of hypochlorite with tert-butyl hydroperoxide. Biochemistry (Moscow). 2002. V. 67 (8). P. 880-888.
- Panasenko O.M., Osipov A.N., Schiller J., Arnhold J. Interaction of exogenous hypochlorite or hypochlorite produced by myeloperoxidase+H2O2+Cl- system with unsaturated phosphatidylcholines. Biochemistry (Moscow). 2002. V. 67 (8). P. 889-900.
- Osipov A.N., Panasenko O.M., Chekanov A.V., Arnhold J. Interaction of tert-butyl hydroperoxide with hypochlorous acid. A spin trapping and chemiluminescence study. Free Rad. Res. 2002. V. 36. P. 749-754.
- Arnhold J., Osipov A.N., Spalteholz H., Panasenko O.M., Schiller J. Formation of lyso-phospholipids from unsaturated phosphatidylcholines under the influence of hypochlorous acid. Biochim. Biophys. Acta. 2002. V. 1572. P. 91-100.
- Chekanov A.V., Panasenko O.M., Osipov A.N., Arnhold J., Kazarinov K.D., Vladimirov Yu.A., Sergienko V.I. Interaction od tert-butyl hydroperoxide with sodium hypochlorite gives rise to peroxide radicals: a chemiluminescence study. Biophysics. 2002. V. 47 (5). P. 731-737.
- Roshchupkin D.I., Chudina N.A., Murina M.A. Chemiluminescence during luminol oxidation by chloramine derivatives of biogenic compounds. Biophysics. 2002. V. 47 (1). P. 23-26.
- Roshchupkin D.I., Chudina N.A., Murina M.A. Kinetic features of luminol chemiluminescence induced by biogenic chloramine compounds. Biophysics. 2002. V. 47 (2). P. 202-209.
- Murina M.A., Fesenko O.D., Sergienko V.I., Chudina N.A., Roshchupkin D.I. Antithrombotic activity of N,N-dichlorotaurine on mouse model of thrombosis in vivo. Bull. Exp. Biol. Med. 2002. V. 134 (1). P. 36-38.
- Panasenko O.M., Sergienko V.I. Hypochlorite, oxidative modification of plasma lipoproteins, and atherosclerosis. Bull. Exp. Biol. Med. 2001. V. 131 (5). P. 407-415.
- Arnhold J., Osipov A.N., Spalteholz H., Panasenko O.M., Schiller J. Effects of hypochlorous acid on unsaturated phosphatidylcholines. Free Radic. Biol. Med. 2001. V. 31. P. 1111-1119.
- Panasenko O.M., Sharov V.S., Briviba K., Sies H. Interaction of peroxinitrite with carotenoids in human low density lipoproteins. Arch. Biochem. and Biophys. 2000. V. 373. P. 302-305.
- Spickett C.M., Jerlich A., Panasenko O.M., Arnhold J., Pitt A.R., Stelmaszynska T., Schaur R.J. The reaction of hypochlorous acid, the reactive oxygen species produced by myeloperoxidase, with lipids. Acta Biochimica Polonica. 2000. V. 47. P. 889-899.