Механизмы взаимодействия гипохлорита и гипохлорит-образующих систем с органическими гидропероксидами
Диссертация
Какой из механизмов, молекулярный или радикальный, преобладает in vivo и играет решающую роль в повреждении мембранных липидов гипохлоритом? Если судить по количеству образующихся продуктов и задействованных функциональных групп липидов, то можно полагать, что это молекулярный механизм, поскольку концентрация образующихся хлоргидринов (особенно в экспериментах in vitro) значительно превышает… Читать ещё >
Список литературы
- Ахметов Н.С. Неорганическая химия. Москва: Высшая школа, 1975, 304−311.
- Владимиров Ю.А., Арчаков А. И. Перекисное окисление липидов в биологических мембранах. Москва: Наука, 1972.
- Владимиров Ю. А., Азизова О. А., Деев А. И., Козлов А. В., Осипов А. Н., Рощупкин Д. И. Свободные радикалы в живых системах. Итоги науки и Техники, Биофизика, Москва. ВИНИТИ, 1992,29: 3−250.
- Владимиров Ю. А. Свободнорадикальное окисление липидов и физические свойства липидного слоя биологических мембран. Биофизика. 1987,38(3): 390−396.
- Владимиров Ю.А., Литвин Ф. Ф. Исследование сверхслабых свечений в биологических системах. Биофизика. 1959,4(5): 601−605.
- Говорова Н.Ю., Шаронов Б. П., Лызлова С. Н. Влияние низкомолекулярных соединений на хемилюминесценцию люминола, обусловленную действием продуктов миелопероксидазного катализа и экзогенного гипохлорита. Биохимия, 1988,53:2025−2032.
- Говорова Н.Ю., Шаронов Б. П., Лызлова С. Н. Окислительное повреждение эритроцитов миелопероксидазой. Защитное действие сывороточных белков. Бюлл. эксперим. биол. и мед. 1989,107:428−430.
- Горбатенкова Е.А., Науменко К. В., Сергиенко В. И. Свойства производных каталазы и пероксидазы, образованных при непрямом электрохимическом окислении. В кн.: Электрохимические методы в медицине. Москва: НИИ ФХМ МЗ РСФСР, 1991, 5−6.
- Евгина С.А., Панасенко О. М., Сергиенко В. И., Владимиров Ю. А. Перекисное окисление липопротеинов крови человека, индуцированное гипохлорит-анионом. Биол. мембраны, 1992,9: 946−953.
- Осипов А.Н. (1983) Изучение свободных радикалов, образующихся при перекисном окислении, методом ЭПР. Дисс. канд. биол. наук, Изд-во МГУ, Москва.
- Маянский А.Н., Маянский Д. Н. Очерки о нейтрофше и макрофаге. Новосибирск: Наука, 1985.
- Несмеянов А.Н., Несмеянов Н. А. Начала органической химии. Москва: Химия. 1974, 1,249.
- Панасенко О.М., Арнхольд Ю., Сергиенко В. И., Арнольд К., Владимиров Ю. А. Стехиометрия взаимодействия гипохлорита с ненасыщенными связями фосфатидилхолина и свободных жирных кислот в составе липосом. Биол. мембраны, 1996,13: 271−281.
- Панасенко О.М., Арнхольд Ю., Арнольд К., Владимиров Ю. А., Сергиенко В. И. Взаимодействие гипохлорита с гидропероксидами и другими продуктами окисления фосфатидилхолиновых липосом. Биохимия, 1995, 60: 1419−1429.
- Панасенко О.М., Арнхольд Ю., Сергиенко В. И. Влияние рН на перекисное окисление фосфолипидных липосом, индуцированное гипохлоритом. Биофизика, 1998,43:463−469.
- Панасенко О.М., Арнхольд Ю., Шиллер Ю. Гипохлорит взаимодействует с органическим гидропероксидом с образованием свободных радикалов, но не синглетного кислорода, инициируя перекисное окисление липидов. Биохимия, 1997, 62: 1111−1121.
- Панасенко О.М., Арнхольд Ю. Механизм гипохлорит-индуцированного перекисного окисления липидов фосфолипидных липосом. Биол. мембраны, 1996, 13: 89−99.
- Панасенко О.М., Арнхольд Ю., Арнольд К., Владимиров Ю. А., Сергиенко В. И. Взаимодействие гипохлорита с гидропероксидами и другими продуктами окисления фосфатидилхолиновых липосом. Биохимия, 1995, 60: 1419−1429.
- Панасенко О.М., Арнхольд Ю., Арнольд К., Владимиров Ю. А., Сергиенко В. И. Сравнительное исследование кинетики пероксидации фосфолипидных липосом, индуцированной гипохлоритом и в системе Fe2+ + аскорбат. Биофизика, 1996,41: 334−341.
- Панасенко О.М., Арнхольд Ю., Арнольд К., Владимиров Ю. А., Сергиенко В. И. Применение метода хемилюминисценции в исследовании кинетики взаимодействия гипохлорита с фосфатидилхолиновыми липосомами. Биофизика, 1995,40: 1234−1242.
- Панасенко О.М., Евгина С. А., Дремина Е. С., Шаров B.C., Владимиров Ю. А., Сергиенко В, И. Роль Fe2+ в перекисном окислении липидов липосомальных мембран, инициированном гипохлоритом натрия. Биол. мембраны, 1995,12: 191 196.
- Панасенко О.М., Осипов А. Н., Шиллер Ю., Арнхольд Ю. Взаимодействие экзогенного гипохлорита, продуцируемого в системе миелопероксидаза + Н202 + С1-, с ненасыщенными фосфадилхолинами. Биохимия, 2002, 67: 1071−1084.
- Черный В.В., Стожкова И. Н., Мирский В. М., Ястребова Т. Н., Соколов B.C. Изменение свойств липидного бислоя под действием гипохлорита натрия. II. Исследование действия гипохлорита натрия на модельные липидные системы. Биол. мембраны, 1992,9: 66−73.
- Шафран М.Г. Миелопероксидаза нейтрофильных гранулоцитов. Успехи соврем, биол., 1981,92(6): 365−379.
- Шаронов Б.П., Чурилова И. В. Окисление супероксиддисмутазы гипохлоритом. Появление изомеров, обладающих каталитической активностью. Докл. АН СССР, 1990,314: 1500−1502.
- Якутова Э.Ш., Осипов А. Н., Костенко О. В., Арнхольд Ю., Арнольд К., Владимиров Ю. А. Взаимодействие гипохлорита с оксигемоглобином приводит к освобождению железа в каталитически активной форме. Биофизика, 1992,37: 1021−1028.
- Якутова Э.Ш., Дремина Е. С., Евгина С. А., Осипов А. Н., Шаров B.C., Панасенко О. М., Владимиров Ю. А. Образование свободных радикалов при взаимодействии гипохлорита с ионами железа (И). Биофизика, 1994,39: 275−279.
- Anbar М., Taube Н. The exchange of hypochlorite and of hypobromite ions with water. J.Am.Chem.Soc., 1958,80: 1073−1077.
- Akanmu D., Cecchini R., Aruoma O.I., Halliwell B. The antioxidant action of eTgothione’me.Arch.Biochem.Biophys., 1991,288: 10−16.
- Aruoma O.I., Halliwell B. Action of hypochlorous acid on the antioxidant protective enzymes superoxide dismutase, catalase and glutathione peroxidase. Biochem.J., 1987, 248: 973−976.
- Arnhold J., Mueller S., Arnold K., Sonntag K. Mechanisms of inhibition of chemiluminescence in the oxidation of luminol by sodium hypochlorite. J.BioIumin.Chemilumin., 1993,6: 307−313.
- Aruoma O.I., Laughton M.J., Halliwell B. Carnosine, homocarnosine and anserine: could they act as antioxidants in vivo? Biochem.J., 1989,264: 863−869.
- Albrich J.M., McCarthy С.A., Hurst J. Biological reactivity of hypochlorous acid: Implications for microbicidal mechanisms of leucocyte myeloperoxidase. Proc.Natl.Acad.Sci.USA, 1981,78: 210−214.
- Arnhold J., Hammerschmidt S., Wagner M., Mueller S., Arnold K., Grimm E. On the action of hypochlorite on human serum albumin. Biomed.Biochim.Acta, 1990,49: 991 997.
- Arnhold J., Mueller S., Arnold K., Grimm E. Chemiluminescence intensities and spectra of luminol oxidation by sodium hypochlorite in the presence of hydrogen peroxide.
- J. Biolumin. Chemilumin., 1991,6: 189−192.
- Arnhold J., Osipov A.N., Spalteholz H., Panasenko O.M., Schiller J. Effects of hypochlorous acid on unsaturated phosphatidylcholines. Free Radic. Biol. Med. 2001,31: 1111−1119.
- Babior B.M. Oxygen dependent microbial killing by phagocytes. N. Engl. J. Med. 1978, 298: 659−668.
- Bekkenist R.J., De Boer J.E.G., Plat H., Wever R. The halide complexes of myeloperoxidase and the mechanism of halogenation reactions. Biochim.Biophys.Acta, 1980,613:337−348.
- Bernofsky C., O’Dea S.W. Nucleotide modification, a radical mechanism of oxidative toxicity. Free Radic.Res.Commun., 1986,2: 129−136.
- Boyum A. Separation of white blood cells. Nature. 1964,204: 793−794.
- Boyum A. Isolation of mononuclear cells and granulocytes from human blood. Isolation of mononuclear cells by one centrifugation, and of granulocytes by combiningbcentrifugation and sedimentation at 1 g. Scand. J. Clin. Lab. Invest. 1968,21: 74−89.
- Candeias L.P., Stratford M.R., Wardman P. Formation of hydroxyl radicals on reaction of hypochlorous acid with ferrocyanide, a model iron (II) complex. Free Radic.Res., 1994, 20: 241−249.
- Candeias L.P., Patel K.B., Stratford M.R., Wardman P. Free hydroxyl radicals are formed on reaction between the meutrophil-derived species superoxide anion and hypochlorous acid.FEBSLett., 1993,333: 151−153.
- Carr A.C., van den Berg J.J., Winterbourn C.C. Chlorination of cholesterol in cell membranes by hypochlorous acid. Arch.Biochem.Biophys., 1996,332: 63−69.
- Carr A.C., Winterbourn C.C., Blunt J.W., Phillips A.J., Abell A.D. Nuclear magnetic resonance characterization of 6-alpha-chloro-5-beta-cholestane-3-beta, 5-diol formed from the reaction of hypochlorous acid with cholesterol. Lipids, 1997,32: 363−367.
- Chamulitrat W, Mason RP. Alkyl free radicals from the beta-scission of fatty acid alkoxyl radicals asdetected by spin trapping in a lipoxygenase system. Arch Biochem Biophys. 1990,282(1): 65−69.
- Chamulirat W., Conet M.S., Mason R.P. Free radical formation from organic hydroperoxides in isolated human polymorphohuclear neutrophils. Free Radic. Biol. Medicin. 1991,11: 439−445.
- Chatham W.W., Blackburn W.D., Jr. Fixation of C3 to IgG attenuates neutrophil HOC1 generation and collagenase activation. J.Immunol., 1993,151: 949−958.
- Clark R.A., Pearson D.W. Inactivation of transferrin iron binding capacity by the neutrophil myeloperoxidase system. J.Biol.Chem., 1989,264: 9420−9427.
- Clark R.A., Szot S. Chemotactic factor inactivation by stimulated human neutriphils mediated by myeloperoxidase-catalyzed methionine oxidation. J.Immunol., 1981, 128: 1507−1513.
- Cuperus R.A., Muijsers A.O., Wever R. The superoxide dismutase activity of myeloperoxidase- formation of compound III. Biochim. Biophys. Acta, 1986,871: 78−84.
- Dai J., Meij J.T.A., Padua R., Panagia V. Depression of cardiac sarcolemmal phospholipase-D activity by oxidant-induced thiol modification. Circ.Res., 1992,71: 970−977.
- Darley Usmar V.M., Lelchuk R., O’Leary V.J., Knowles M., Rogers M.V., Severn A. Oxidation of low-density lipoprotein and macrophage derived foam cells. Biochem. Soc. Trans., 1990,18: 1064−1066.
- Davies M.J. Protein and peptide alkoxyl radicals can give rise to C-terminal decarboxylation and backbone cleavage. Arch. Biochem. Biophys. 1996, 336: 163−172.
- Davies, M. J., Fu, S., and Dean, R. T. Protein hydroperoxides can give rise to reactive free radicals. Biochem. J. 1995,305: 643−649.
- Davies J.M., Horwitz D.A., Davies K.J. Potential roles of hypochlorous acid and N-chloroamines in collagen breakdown by phagocytic cells in synovitis. Free Radic.Biol.Med., 1993,15: 637−643.
- Di Mascio P, Wefers H, Do-Thi HP, Lafleur MV, Sies H. Singlet molecular oxygen causes loss of biological activity in plasmid andbacteriophage DNA and induces single-strand breaks. Biochim Biophys Acta., 1989, 1007(2): 151−157.
- Dikalov SI, Mason RP. Spin trapping of polyunsaturated fatty acid-derived peroxyl radicals: reassignment to alkoxyl radical adducts. Free Radio Biol Med. 2001,30(2): 187 197.
- Drozdz R., Naskalski J. W. & Sznajd J. Oxidation of amino acids and peptides in reaction with myeloperoxidase, chloride and hydrogen peroxide. Arch Biochem. Biophys., 1988, 957:47−52.
- Duling, D.R. Simulation of multiple isotropic spin-trap EPR spectra. J. Magn. Reson., 1994. В 104: 105−110.
- Edwards S.W. Biochemistry and physiology of the neutrophil. Cambridge: Cambridge University press, 1994.
- Fliss H., Menard M. Hypochlorous acid-induced mobilization of zinc from metalloproteins. Arch. Biochem. Biophys., 1991,287: 175−179.
- Floris R., Wever R. Reaction of myeloperoxidase with its product HOCI. Eur. J. Biochem., 1992,207: 697−702.
- Foote C.S., Goyne, Т.Е.- Lehrer R.I. Assessment of chlorination by human neutrophils. Nature. 1983, 301: 715−726.
- Freeman B. A., Sharman M. C., and Mudd L. Reaction of ozone with phospholipid vesicles and human erythrocyte ghosts. Arch Biochem Biophys. 1979, 197: 264−272.
- Furtmuller PG, Burner U, Jantschko W, Regelsberger G, Obinger C. Two-electron reduction and one-electron oxidation of organic hydroperoxides by human myeloperoxidase. FEBSLett. 2000, 484(2): 139−43.
- Girotti A.W. Lipid hydroperoxide generation, turnover, and effector action in biological systems. J. Lipid Res. 1998, 39: 1529−1542., Review.
- Girotti AW. Photodynamic lipid peroxidation in biological systems., Photochem. and Photobiol. 1990,51: 497−509., Review.
- Granger D.L., Taintor R.R., Boockvar K.S., Hibbs J.B. Measurement of nitrate and nitrite in biological samples using nitrate reductase and Griss reaction. Methods Enzymol., 1996, 268: 142−151.
- Grisham M.B., Jefferson M.M., Thomas E.L. Role of monochloramine in the oxidation of erythrocyte hemoglobin by stimulated neutrophils. J.Biol.Chem., 1984., 259: 6757−6765.
- Halliwell В., Gutteridge J.M.C. Free radicals in Biology and Medicine. Oxford. University Press. 2000.
- Harrison J.E., Schultz J. Studies on the chlorinating activity of myeloperoxidase. J.Biol.Chem., 1976,251: 1371−1374.
- Harrison J.E. The functional mechanism of myeloperoxidase. In: Cancer Enzymology. Eds. Schultz J., Cameron B.F. New York: Academic Press, 1976,305−317.
- Hazell L.J., Stocker R. Oxidation of low-density lipoprotein with hypochlorite causes transformation of the lipoprotein into a high-uptake form for macrophages. Biochem.J., 1993,290: 165−172.
- Hawkins C. L. and Davies M. J. Hypochlorite-induced damage to proteins: formation of nitrogen-centred radicals from lysine residues and their role in protein fragmentation. Biochem.J. 1998,332:617−625.
- Hawkins C.L., Davies M.J. Degradation of hyaluronic acid, poly- and monosaccharides, and model compounds by hypochlorite: evidence for radical intermediates and fragmentation. Free Radic. Biol. Med. 1998,24: 1396−1410.
- Hawkins C.L., Davies M.J. Hypochlorite-induced damage to proteins: formation of nitrogen-centred radicals from lysine residues and their role in protein fragmentation. BiochemJ. 1998,332:617−625.
- Headlam HA, Davies MJ. Cell-mediated reduction of protein and peptide hydroperoxides to reactive free radicals. Free Radic Biol Med. 2003,34(l):44−55.
- Heinecke J.W., Li W., Daehnke H.L., Goldstein J.A. Dityrosine, a specific marker of oxidation, is synthesized by the myeloperoxidase-hydrogen peroxide system of human neutrophils and macrophages. J.Biol.Chem., 1993,268:4069−4077.
- Heinecke J.W., Li W., Mueller D.M., Bohrer A., Turk J. Cholesterol chlorohydrin synthesis by the myeloperoxidase-hydrogen peroxide-chloride system: potential markers for lipoproteins oxidatively damaged by phagocytes. Biochemistry, 1994,33: 1 012 710 136.
- Heinecke J.W., Li W., Daehnke H.L., Goldstein J.A. Dityrosine, a specific marker of oxidation, is synthesized by the myeloperoxidase-hydrogen peroxide system of human neutrophils and macrophages. J.Biol.Chem., 1993, 268:4069−4077.
- Heller A., Koch Т., Schmeck J., van Ackern K. Lipid mediators in inflammatory disorder. Drugs. 1998, 55:487−496.
- Hoogland H., Dekker H.L., Riel C., Kuilenburg A., Muijsers A.O., Wever R. A steady-state study on the formation of II and III of myeloperoxidase. Biochim.Biophys.Acta, 1988, 955: 337−345.
- Howard J.A., Ingold K.U. The self-reaction of sec-butylperoxy radicals. Conformation of the Russell mechanism. J.A.Chem.Soc., 1968,90: 1056−1058.
- Hu M.L., Louie S., Cross C.E., Motchnik P., Halliwell B. Antioxidant protection against hypochlorous acid in human plasma. J.Lab.Clin.Med., 1993, 121: 257−262.
- Hurst J.K. Myeloperoxidase active site structure and catalytic machanism. In: Everse K.- Grisham M.B., eds., Peroxidases in chemistry and biology 1 st ed Boca Ration: CRC Press- 1991,37−62.
- Iwahashi H. Some polyphenols inhibit the formation of pentyl radical and octanoic acid radical in the reaction mixture of linoleic acid hydroperoxide with ferrousions. Biochem. J. 2000,346: 265−73.
- Iwahashi H. High-performance liquid chromatographic determination of linoleic acid peroxide-derived radicals using electrochemical detection. J Chromatogr A. 2000, 904(2): 197−202.
- Iwamoto H., Kobayashi Т., Hasegawa E., Morita Y. Reaction of human myeloperoxidase with hydrogen peroxide and its true catalase activity. J.Biochem., 1987,101: 1407−1412.
- Iwase H, Sakurada К, Hatanaka К, Kobayashi M, Takatori Т. Effect of cytochrome с on the linoleic acid-degrading activity of porcine leukocyte 12-lipoxygenase. Free Radio. Biol. Med. 2000, 28(6): 912−918.
- Iwase H, Takatori T, Sakurada K, Nagao M, Niijima H, Matsuda Y, Kobayashi M. Calcium is required for quasi-lipoxygenase activity of hemoproteins. Free Radio. Biol. Med. 1998,25(8): 943−52.
- Jasin H.E. Oxidative modification of inflammatory synovial fluid immunoglobulin G. Inflammation, 1993,17: 167−181.
- Johnson D.W., Margerum D.W. Non-metal redox kinetics: a reexamination of the mechanism of the reaction between hypochlorite and nitrite ions. Inorg.Chem., 1991,30: 4845−4851.
- Kalyanaraman В., Sohnle P.G. Generation of free radical intermediates from foreign compounds by neutrophil-derived oxidants .J.Clin. Invest., 1985, 75: 1618−1622.
- Kanofsky J.R. Singlet oxygen production by biological systems. Chem.-Biol. Interact., 1989, 70: 1−28.
- Kettle A. J., Winterbourn C.C. Assays for the chlorination activity of myeloperoxidase.
- Methods Enzymol., 1994,233: 502−512.
- Kettle A.J., Winterbourn C.C. Mechanism of inhibition of myeloperoxidase by antiinflammatory drugs. Biochem.Pharmacol., 1991,41: 1485−1492.
- Kettle A. J., Winterbourn C.C. Superoxide modulates the activity of myeloperoxidase andoptimizes the production of hypochlorous acid. Biochem. J., 1988, 252: 529−536.
- Kettle A.J., Winterbourn C.C. Oxidation of hydroquinone by myeloperoxidase.
- Mechanism of stimulation by benzoquinone. J.Biol.Chem., 1992,267: 8319−8324.
- Kettle A. J., Winterbourn C.C. Myeloperoxidase: A key regulator of neutrophil of oxidantproduction. Redox. Rep. 1997,3: 3−15.
- Khan A.U., Kasha M. Chemiluminescence arising from simultaneous transitions in pairs of singlet oxygen molecules. J.Am.Chem.Soc., 1970,92: 3293−3300.
- Klebanoff S.J., Clark R.A. The neutrophil: Function and clinical disorders. Amsterdam:
- Elsevier-North Holland, 1978.
- Kukreja R.C., Weaver A.B., Hess M.L. Stimulated human neutrophils damage cardiacsarcoplasmic reticulum function by generation of oxidants. Biochim.Biophys.Acta, 1989, 990: 198−205.
- Kukreja R.C., Weaver A.B., Hess M.L. Sarcolemmal Na±K±ATPase: inactivation byneutrophil-derived free radicals and oxidants. Am.J.Physiol., 1990, 259: H1330-H1336.
- LapennaD., DeGioia S., Ciofani G., Mezzetti A., Consoli A., Di Ilio C., Cuccurullo F.
- Hypochlorous acid-induced zinc release from thiolate bonds: a potential protective mechanism towards biomolecules oxidant damage during inflammation. Free Radic.Res., 1994,20: 165−170.
- Lindgren F.T. Preparative ultracetrifugal laboratory procedures and suggest ions forlipoprotein analysis. In: Analisis of Lipids and Lipoproteins., Ed. Perkins E.G. Champaign (III), Amer. Oil. Chemists. Soc. 1975,204−224.
- Long C.A., Bielski B.H.J. Rate of reaction of superoxide radical with chloride-containingspecies. J.Phys. Chem., 1980,84: 555−557.
- Malle E., et al., Int. J. Lipoxygenase and hydroperoxy/hydroxy-eicosatetraenoic acidformation. Biochem. 1987,19: 1013.
- Marietta M.A., Yoon P. S., Iyenger R., Leaf C.D., Wishok J.S. Macrophage oxidation of Larginine to nitrite and nitrate: nitric oxide is an intermediate. Biochemistry, 1988,27: 8706−8711.
- Mashino Т., Fridovich I. Reactions of hypochlorite with catalase. Biochim.Biophys.Acta, 1988, 956: 63−69.
- Matheson N.R., Travis J. Differential effects of oxidizing agents on human plasma aiproteinase inhibitor and human neutrophil myeloperoxidase. Biochemistry, 1985,24: 1941−1945.
- Matsuoka Т., Kato M., Kako K.J. Effect of oxidants on Na+, K±ATPase and its reversal.
- Basic.Res.Cardiol., 1990,85: 330−341.
- Metzger J.O. Herstellung (Erzeugung) von Radikalen durch homolytische SpaltungvonC, H-Bindungen mit Radikalen. In: Houben-Weyl. Methoden der Organischen Chemie. 4. Auflage, Bd. El9a, C-Radikale, Georg-Thieme Verlag, Stuttgart-New York, 1989, 60−145.
- Michaelis J., Vissers M.C., Winterbourn C.C. Different effects of hypochlorous acid onhuman neutrophil metalloproteinases: activation of collagenase and inactivation of collagenase and gelatinase. Arch.Biochem.Biophys., 1992,292: 555−562.
- McGiff J. C. Cytochrome P-450 metabolism of arachidonic acid. Annu. Rev. Farmacol.1. Toxicol 1991,31:339−369.
- Monboisse J.C., Borel J.P. Oxidative damage to collagen. EXS., 1992,62: 323−327.
- Morris J.C. The acid ionization constant of HOCl from 5 to 35 °C. J.Phys.Chem., 1966, 70:3798−3805.
- Nakamori К., Koyama I., Nakamura Т., Yoshida Т., Umeda M., Inoue K. Effectiveness oftaurine in protecting biomembrane against oxidant. Chem.Pharm.Bull.Tokyo., 1990,38: 3116−3119.
- Nauseef W.M.- Malech H.L. Analysis of the peptide subunits of human neutrophilmyeloperoxidase. Blood., 1986,67: 1504−1507.
- Noguchi N, Nakada A, Itoh Y, Watanabe A, Niki E. Formation of active oxygen speciesand lipid peroxidation induced by hypochlorite. Arch. Biochem. Biophys. 2002,397(2): 440−7.
- Panasenko O.M., Arnhold J. Linoleic acid hydroperoxide favours hypochlorite- andmyeloperoxidase-induced lipid peroxidation. Free Radic Res. 1999,30(6):479−87.
- Panasenko O.M., Vol’nova T.V., Osipov A.N., Azizova O.A., Vladimirov Yu.A. Freeradical generation by monocytes and neutrophils: a possible cause of plasma lipoprotein modification. Biomed.Sci., 1991,2: 581−589.
- Panasenko O.M., Arnhold J., Vladimirov Yu.A., Arnold K., Sergienko V.I. Peroxidationof egg yolk phosphatidylcholine liposomes by hypochlorous acid. Biochim. Biophys. Acta., 1994,1215:259−266.
- Panasenko O.M., Evgina S.A., Andyraliev R.P., Sergienko V.I., Vladimirov Yu.A.
- Peroxidation of blood lipoproteins induced by exogenous hypochlorite generated in the system of myeloperoxidase + H202 + СГ. Free Radic.Biol.Med., 1994,16: 143−148.
- Panasenko O.M. The mechanism of the hypochlorite-induced lipid peroxidation.
- BioFactors. 1997,6: 181−190.
- Panasenko O.M., Arnhold J., Vladimirov Yu.A., Arnold K., Sergienko V. I Reaction ofhypochlorous acid with hydrogen peroxide and tert-butyl hydroperoxide. 'H NMR spectroscopy and chemiluminescence analysis. Z. Naturforsch., 1996,51: 386−394.
- Panasenko O.M., Arnhold J., Vladimirov Yu.A., Arnold K., Sergienko V.I. Hypochloriteinduced peroxidation of phosphatidylcholine is mediated by hydroperoxides. Free Radic. Res., 1997,27: 1−12.
- Panasenko O.M., Briviba K., Klotz L.-O., Sies H. Oxidative modification and nitration of human low-density lipoproteins by the reaction of hypochlorous acid with nitrite. Arch.Biochem.andBiophys., 1997,343: 254−259.
- Panasenko O.M., Sergienko V.I. Hypochlorite, oxidative modification of plasmalipoproteins, and atherosclerosis. Bull. Exp. Biol. Med. 2001,31(5): 407−15. Review.
- Panasenko O.M., Panasenko O.O., Briviba K., Sies H. Hypochlorite destroys carotenoidsin low density lipoproteins thus decreasing their resistance to peroxidative modification. Biochemistry. 1997, 62(10): 1140−5.
- Panasenko O.M., Evgina S.A., Driomina E.S., Sharov V.S., Sergienko V.I., Vladimirov
- Yu.A. Hypochlorite induces lipid peroxidation in blood lipoproteins and phospholipid liposomes. Free Radic.Biol.Med., 1995,19: 133−140.
- Piazza. G.J. Lipoxygenase catalyzed hydroperoxide formation in microemulsionscontaining nonionic surfactant. Biotechnol. Lett. 1992,14: 1153.
- Penner M.H., Osuga D.T., Meares C.F., Feeney R.E. The interaction of anions with nativeand phenylglyoxal-modified human serum transferrin. Arch.Biochem.Biophys., 1987., 252: 7−14.
- Peppin G.J., Weiss S.J. Activation of the endogenous metalloproteinase, gelatinase, bytriggered human neutrophils. Proc.Natl.Acad.Sci.U.S.A., 1986,83:4322−4326.
- Podrez E.A., Abu-Soud H.M., Hazen S.L. Myeloperoxidase-generated oxidation andatherosclerosis. Free Radic. Biol. & Med. 2000, 28(12): 1717−1725.
- Pryor W.A. The formation of free radicals and the consequences of their reactions in vivo.
- Photochem. and Photobiol. 1978,28:787−801.
- Pryor W.A. Mechanisms of radical formation from reactions of ozone with target moleculsin the lung. Free Radical Biol.Med. 1994,17: 451−465.
- Qian SY, Guo Q, Mason RP. Identification of spin trapped carbon-centered radicals insoybean lipoxygenase-dependent peroxidations of omega-3 polyunsaturated fatty acids by LC/ESR, LC/MS, and tandem MS. Free Radic Biol Med. 2003, 35(l):33−44.
- Rao S. I., Wilks A., Hamberg M., Ortis de Montellano P. R. The lipoxygenase activity ofmyoglobin. J. Biol. Chem. 1994,269: 7210−7216.
- Rice-Evans C., Leake D., Bruckdorfer K.R., Diplock A.T. Practical approaches to lowdensity lipoprotein oxidation: whys, wherefores and pitfalls. Free Radic.Res., 1996,25: 285−311.
- Russell G.A. Deuterium-isotope effects in the autoxidation of aralkyl hydrocarbons.
- Mechanism of the interaction of peroxy radicals. J. Am. Chem. Soc. 1957, 79: 3871−3877.
- Saari H., Sorsa Т., Lindy О., Suomalainen К., Halinen S., Konttinen Y.T. Reactive oxygen species as regulators of human neutrophil and fibroblast interstitial collagenases. Int.J.Tissue React., 1992,14: 113−120.
- Sayuri Miyamoto, Glaucia R. Martinez, Marisa H. G. Medeiros, and Paolo Di Mascio.
- Singlet Molecular Oxygen Generated from Lipid Hydroperoxides by the Russell1 Я
- Mechanism: Studies Using O-Labeled Linoleic Acid Hydroperoxide and Monomol Light Emission Measurements. J. Am. Chem. Soc. 2003, 125(20): 6172 6179.
- Sepe S.M., Clark R.A. Oxidant membrane injury by the neutrophil myeloperoxidasesystem. 1. Characterization of a liposome model and injury by myeloperoxidase, hydrogen peroxide, and halides. J.Immunol., 1985,134: 1888−1895.
- Sepe S.M., Clark R.A. Oxidant membrane injury by the neutrophil myeloperoxidase system. 2. Injury by stimulated neutrophils and protection by lipid-soluble antioxidants. J. Immunol., 1985,134: 1896−1901.
- Sies H., Stahl W., Sundquist A.R. Antioxidant functions of vitamins. Vitamins E and C, beta-carotene, and other carotenoids. Ann.N.Y.Acad.Sci., 1992,669: 7−20.
- Shanlin F., Wang H., Davies M. & Dean R. Reactions of hypochlorous acid with tyrosineand peptidyl-tyrosyl residues give dichlorinated and aldehydic products in additions to 3-chlorotyrosine. J.Biol.Chem., 2000, 275: 10 858−10 858.
- Sharov V.S., Briviba K., Sies H. Assessment of the C-525 laser dye as a chemiluminescence sensitizer for lipid peroxidation in biological membranes: a comparison with chlorophyll-a. Free Radic Biol Med. 1996,21(6): 833−43.
- Sharov V.S., Dremina E.S., Vladimirov Iu.A. Activation of Fe2±inducedchemiluminescence in human blood low density lipoproteins by the fluorescent dye C-525. Biofizika., 1995,40(2): 428−33.
- Sharov V.S., Vladimirov Iu.A. Chemiluminescence of liposomes activated with rare earth ions. Biofizika. 1982,27(2): 327−9.
- Sharonov B.P., Churilova I.V. Inactivation and oxidative modification of Cu, Znsuperoxide dismutase by stimulated neutrophils: the appearance of new catalytically active structures. Biochem.Biophys.Res.Commun., 1992, 189: 1129−1135.
- Sharonov B.P., Govorova N.I., Lyzlova S.N. A comparative study of serum proteinsability to scavenge active oxygen species: «O2*. and ОСГ. Biochem.Int., 1988,17: 783 790.
- Sharonov B.P., Govorova N.I., Lyzlova S.N. Serum protein degradation by hypochlorite. Biochem.Int., 1989,19: 27−35.
- Sharonov BP, Govorova NIu. Oxidation of ceruloplasmin by hypochlorite. The loss of blue color and preservation of oxidase activity. Biokhimiia. 1990,55(6): 1145−1148.
- Schaur J.R., Jerlich A., Stelmaszynska T. Hypochlorous acid as reactive oxygen species.
- Current Topics in Biophysics. 1998,22: 176−185.
- Schiller J., Arnhold J., Grunder W., Arnold K. The action of hypochlorous acid on polymeric components of cartilage. Biol.Chem.Hoppe Seyler, 1994,375: 167−172.
- Schiller J., Arnhold J., Arnold K. Action of hypochlorous acid on polymeric componentsof cartilage. Use of 13C-NMR spectroscopy. ZNaturforsch., 1995,50: 721−728.
- Schraufstatter I., Hyslop P.A., Jackson J.H., Cochrane C.G. Oxidant-induced DNA damage of target cells. J.Clin.Invest., 1988, 82: 1040−1050.
- Schraufstatter I.U., Browne K., Harris A., Hyslop P.A., Jackson J.H., Quehenberger O.,
- Cochrane C.G. Mechanisms of hypochlorite injury of target cells. J.Clin.Invest., 1990, 85: 554−562.
- Schultz Y., Kaminver K. Myeloperoxidase of the leukocyte of normal human blood.
- Content and localization. Arch.Biochem., 1962,96: 465−467.
- Soriani M., Mazzuca S., Quaresima V., Minetti M. Oxidation of desferoxamine tonitroxide free radical by activated human neutrophils. Free Radic.Biol.Med., 1993,14: 589−599.
- Spickett C.M., Jerlich A., Panasenko O.M., Arnhold J., Pitt A.R., Stelmaszynska Т.,
- Schaur R.J. The reactions of hypochlorous acid, the reactive oxygen species produced by myeloperoxidase, with lipids. Acta Biochim. Polonica. 2000,47: 889−899.
- Stark J.A., Henderson A.R. In vitro effect of elastase and cathepsin G from humanneutrophils on creatine kinase and lactate dehydrogenase isoenzymes. Clin. Chem1993, 39: 986−992.
- Steven P. Stratton and Daniel C. Liebler. Determination of Singlet Oxygen-Specific versus
- Radical-Mediated Lipid Peroxidation in Photosensitized Oxidation of Lipid Bilayers: Effect of p-Carotene and cc-Tocopherol. Biochemistry 1997,36(42): 12 911 12 920.
- Stocker R., Peterhans E. Antioxidant properties of conjugated bilirubin and biliverdin: biologically relevant scavenging of hypochlorous acid. Free Radic. Res.Commun., 1989, 6: 57−66.
- Soriani M., Mazzuca S., Quaresima V., Minetti M. Oxidation of desferoxamine tonitroxide free radical by activated human neutrophils. Free Radic.Biol.Med., 1993,14: 589−599.
- Suzuki S., Kaneko M., Chapman D.C., Dhalla N.S. Alterations in cardiac contractile proteins due to oxygen free radicals. Biochim.Biophys.Acta, 1991,1074: 95−100.
- Terada L.S., Beehler C.J., Banerjee A., Brown J.M., Grosso M.A., Harken A.H., McCord
- J.M., Repine J.E. Hyperoxia and self- or neutrophil-generated O2 metabolites inactivate xanthine oxidase. J.Appl.Physiol., 1988., 65: 2349−2353.
- Uppu R. M., Cueto R., Squadrito G. L., Pryor W. A. What does ozone react at the air/lunginterface? Model studies using human red blood cell membranes. Arch Biochem Biophys. 1995,319: 257−266.
- Van Rensburg C.E., Van Staden A.M., Anderson R., Van Rensburg E.J. Hypochlorousacid potentiates hydrogen peroxide-mediated DNA-strand breaks in human mononuclear leucocytes. Mutat.Res., 1992,265: 255−261.
- Van Rensburg C.E., Van Staden A.M., Anderson R. Inactivation of poly (ADP-ribose)polymerase by hypochlorous acid. Free Radic.Biol.Med., 1991,11: 285−291.
- Van Zyl J.M., Basson K., Kriegler A., Van der Walt B.J. Activation of chlorpromazine bythe myeloperoxidase system of the human neutrophil. Biochem. Pharmacol., 1990, 40: 947−954.
- Vissers M.C., Winterbourn C.C. Myeloperoxidase-dependent oxidative inactivation ofneutrophil neutral proteinases and microbicidal enzymes. Biochem. J., 1987,245: 277 280.
- Vissers M.C., Fantone J.C. Inhibition of hypochlorous acid-mediated reactions bydesferoxamine. Implications for the mechanism of cellular injury by neutrophils. Free Radic.Biol.Med., 1990,8: 331−337.
- Vissers M.C., Winterbourn C.C. Oxidative damage to fibronectin. I. The effects of theneutrophil myeloperoxidase system and HOCI. Arch.Biochem.Biophys., 1991., 285: 5359.
- Vladimirov Yu.A., Olenev V.I., Suslova T.B., Cheremisina Z.P. Lipid peroxidation in mitochondrial membrane. Adv. Lipid Res., 1980,17: 173−249.
- Vladimirov Y. A, Sharov V.S., Driomina E.S., Reznitchenko AV, Gashev SB. Coumarinderivatives enhance the chemiluminescence accompanying lipid peroxidation. Free Radic Biol Med. 1995,18(4):739−745.
- Weiss S.J. Neutrophil-mediated methemoglobin formation in the erythrocyte. The role ofsuperoxide and hydrogen peroxide. J.Biol.Chem., 1982,257: 2947−2953.
- Weiss S.J., Peppin G., Ortiz X., Ragsdale C., Test S.T. Oxidative autoactivation of latent collagenase by human neutrophils. Science, 1985,227: 747−749.
- Wefers H, Di Mascio P, Do-Thi HP, Schulte-Frohlinde D, Sies H. Effects of singletoxygen on the biological activity of DNA and its involvement in single strand-break formation. Basic Life Sci. 1988,49: 473−477.
- Wefers H, Melnik ВС, Flur M, Bluhm C, Lehmann P, Plewig G. Influence of UVirradiation on the composition of human stratum corneum lipids. J Invest Dermatol. 1991,96(6): 959−962.
- Wiess S.J.- Klein R.- Slivka A.- Wei. M. Chlorination of taurine by human neutrophils.
- Evidence for hypochlorous acid generation. J. Clin. Invest. 1982, 70: 598−607.
- Wiberg N. Lehrbuch der Anorganische Chemie. Berlin-New York: Walter de Gruyter.1985,422−425.
- Winterbourn C.C., van den Berg J.J., Roitman E., Kuypers F.A. Chlorohydrin formationfrom unsaturated fatty acids reacted with hypochlorous acid. Arch.Biochem.Biophys., 1992,296: 547−555.
- Winterbourn C.C., Carr A.C. Myeloperoxidase-dependent loss of malondialdehyde: alimitation for detecting neutrophil-mediated lipid peroxidation. Arch.Biochem.Biophys., 1993,302:461−467.
- Winterbourn C.C., Monteiro H.P., Galilee C.F. Ferritin-dependent lipid peroxidation bystimulated neutrophils: inhibition by myeloperoxidase-derived hypochlorous acid but not by endogenous lactoferrin. Biochim.Biophys.Acta, 1990,1055: 179−185.
- Winterbourn C.C., Molloy A.L. Susceptibilities of lactoferrin and transferrin to myeloperoxidase-dependent loss of iron-binding capacity. Biochem.J., 1988,250: 613 616.
- Winterbourn C.C. Comparative reactivities of various biological compounds with myeloperoxidase-hydrogen peroxide-chloride, and similarity of the oxidant to hypochlorite. Biochim.Biophys.Acta, 1985,840: 204−210.
- Winterbourn C.C., Garcia R.C., Segal A.W. Production of the superoxide adduct of myeloperoxidase (compound III) by stimulated human neutrophils and its reactivity with hydrogen peroxide and chloride. Biochem.J., 1985,228: 583−592.
- Wright A, Bubb WA, Hawkins CL, Davies MJ. Singlet oxygen-mediated protein oxidation: evidence for the formation of reactive side chain peroxides on tyrosine residues. Photochem Photobiol. 2002, 76: 35−46.
- Wright A, Hawkins CL, Davies MJ. Photo-oxidation of cells generates long-lived intracellular protein peroxides. Free Radic Biol Med. 2003, 34(6): 637−647.
- Yamashita H., Nakamura A., Noguchi N., Niki E., Ktihn H. Oxidation of low densitylipoprotein and plasma by 15-lipoxygenase and free radicals., FEBS Letters. 1999, 445: 287−290.
- Zibon V. A., Miller С. C., Cho Y. H. Metabolism of polyunsaturated fatty acids by skinepidermal enzymes: generation of anti-inflammatory and antiproliferative metabolites. Amer. J. Clin. Nutr. 2000, 71: 361 366.
- Zgliczynsky J.M., Stelmaszynska Т., Domanski J., Ostrowski W. Chloramines asintermediates of oxidation reaction of amino acids by myeloperoxidase. Biochim.Biophys.Acta, 1971,235: 419−424.