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Oxidative Medicine and Cellular Longevity
Volume 2016, Article ID 8386362, 26 pages
http://dx.doi.org/10.1155/2016/8386362
Review Article

Chlorinated Phospholipids and Fatty Acids: (Patho)physiological Relevance, Potential Toxicity, and Analysis of Lipid Chlorohydrins

Institute for Medical Physics and Biophysics, Faculty of Medicine, Leipzig University, Leipzig, Germany

Received 5 September 2016; Revised 24 October 2016; Accepted 6 November 2016

Academic Editor: Kota V. Ramana

Copyright © 2016 Jenny Schröter and Jürgen Schiller. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. R. Medzhitov, “Origin and physiological roles of inflammation,” Nature, vol. 454, no. 7203, pp. 428–435, 2008. View at Publisher · View at Google Scholar · View at Scopus
  2. S. Frisenda, C. Perricone, and G. Valesini, “Cartilage as a target of autoimmunity: a thin layer,” Autoimmunity Reviews, vol. 12, no. 5, pp. 591–598, 2013. View at Publisher · View at Google Scholar · View at Scopus
  3. A. Manda-Handzlik and U. Demkow, “Neutrophils: the role of oxidative and nitrosative stress in health and disease,” in Pulmonary Infection, vol. 857 of Advances in Experimental Medicine and Biology, pp. 51–60, Springer, Berlin, Germany, 2015. View at Publisher · View at Google Scholar
  4. J. H. Forman and A. B. Fischer, “Antioxidants in the lung,” in CRC Handbook of Methods for Oxygen Radical Research, R. A. Greenwald, Ed., pp. 359–364, CRC Press, Boca Raton, Fla, USA, 1985. View at Google Scholar
  5. M. J. Gray, W.-Y. Wholey, and U. Jakob, “Bacterial responses to reactive chlorine species,” Annual Review of Microbiology, vol. 67, pp. 141–160, 2013. View at Publisher · View at Google Scholar · View at Scopus
  6. R. Senthilmohan and A. J. Kettle, “Bromination and chlorination reactions of myeloperoxidase at physiological concentrations of bromide and chloride,” Archives of Biochemistry and Biophysics, vol. 445, no. 2, pp. 235–244, 2006. View at Publisher · View at Google Scholar · View at Scopus
  7. F. H. Greig, S. Kennedy, and C. M. Spickett, “Physiological effects of oxidized phospholipids and their cellular signaling mechanisms in inflammation,” Free Radical Biology and Medicine, vol. 52, no. 2, pp. 266–280, 2012. View at Publisher · View at Google Scholar · View at Scopus
  8. C. Prasse, D. Stalter, U. Schulte-Oehlmann, J. Oehlmann, and T. A. Ternes, “Spoilt for choice: a critical review on the chemical and biological assessment of current wastewater treatment technologies,” Water Research, vol. 87, pp. 237–270, 2015. View at Publisher · View at Google Scholar · View at Scopus
  9. C. H. Jeong, C. Postigo, S. D. Richardson et al., “Occurrence and comparative toxicity of haloacetaldehyde disinfection byproducts in drinking water,” Environmental Science and Technology, vol. 49, no. 23, pp. 13749–13759, 2015. View at Publisher · View at Google Scholar · View at Scopus
  10. D. Kim, G. L. Amy, and T. Karanfil, “Disinfection by-product formation during seawater desalination: a review,” Water Research, vol. 81, pp. 343–355, 2015. View at Publisher · View at Google Scholar · View at Scopus
  11. C. M. Spickett, “Chlorinated lipids and fatty acids: an emerging role in pathology,” Pharmacology and Therapeutics, vol. 115, no. 3, pp. 400–409, 2007. View at Publisher · View at Google Scholar · View at Scopus
  12. G. O. Frühwirth, A. Loidl, and A. Hermetter, “Oxidized phospholipids: from molecular properties to disease,” Biochimica et Biophysica Acta (BBA)—Molecular Basis of Disease, vol. 1772, no. 7, pp. 718–736, 2007. View at Publisher · View at Google Scholar · View at Scopus
  13. C. Mauerhofer, M. Philippova, O. V. Oskolkova, and V. N. Bochkov, “Hormetic and anti-inflammatory properties of oxidized phospholipids,” Molecular Aspects of Medicine, vol. 49, pp. 78–90, 2016. View at Publisher · View at Google Scholar
  14. V. N. Bochkov, O. V. Oskolkova, K. G. Birukov, A.-L. Levonen, C. J. Binder, and J. Stöckl, “Generation and biological activities of oxidized phospholipids,” Antioxidants & Redox Signaling, vol. 12, no. 8, pp. 1009–1059, 2010. View at Publisher · View at Google Scholar · View at Scopus
  15. X. Han and R. W. Gross, “Global analyses of cellular lipidomes directly from crude extracts of biological samples by ESI mass spectrometry: a bridge to lipidomics,” Journal of Lipid Research, vol. 44, no. 6, pp. 1071–1079, 2003. View at Publisher · View at Google Scholar · View at Scopus
  16. G. Astarita, A. C. Kendall, E. A. Dennis, and A. Nicolaou, “Targeted lipidomic strategies for oxygenated metabolites of polyunsaturated fatty acids,” Biochimica et Biophysica Acta (BBA)—Molecular and Cell Biology of Lipids, vol. 1851, no. 4, pp. 456–468, 2015. View at Publisher · View at Google Scholar · View at Scopus
  17. S. V. Pande and J. F. Mead, “Inhibition of enzyme activities by free fatty acids,” The Journal of Biological Chemistry, vol. 243, no. 23, pp. 6180–6185, 1968. View at Google Scholar · View at Scopus
  18. N. Borregaard, “Neutrophils, from marrow to microbes,” Immunity, vol. 33, no. 5, pp. 657–670, 2010. View at Publisher · View at Google Scholar · View at Scopus
  19. E. Kolaczkowska and P. Kubes, “Neutrophil recruitment and function in health and inflammation,” Nature Reviews Immunology, vol. 13, no. 3, pp. 159–175, 2013. View at Publisher · View at Google Scholar · View at Scopus
  20. G. Wang and W. M. Nauseef, “Salt, chloride, bleach, and innate host defense,” Journal of Leukocyte Biology, vol. 98, no. 2, pp. 163–172, 2015. View at Publisher · View at Google Scholar · View at Scopus
  21. Y. Kato, “Neutrophil myeloperoxidase and its substrates: Formation of specific markers and reactive compounds during inflammation,” Journal of Clinical Biochemistry and Nutrition, vol. 58, no. 2, pp. 99–104, 2016. View at Publisher · View at Google Scholar
  22. B. Amulic, C. Cazalet, G. L. Hayes, K. D. Metzler, and A. Zychlinsky, “Neutrophil function: from mechanisms to disease,” Annual Review of Immunology, vol. 30, pp. 459–489, 2012. View at Publisher · View at Google Scholar · View at Scopus
  23. T. Strowig, J. Henao-Mejia, E. Elinav, and R. Flavell, “Inflammasomes in health and disease,” Nature, vol. 481, no. 7381, pp. 278–286, 2012. View at Publisher · View at Google Scholar · View at Scopus
  24. E. Minichiello, L. Semerano, and M.-C. Boissier, “Time trends in the incidence, prevalence, and severity of rheumatoid arthritis: a systematic literature review,” Joint, Bone, Spine, vol. 83, no. 6, pp. 625–630, 2016. View at Publisher · View at Google Scholar
  25. J. Schiller, S. Benard, S. Reichl, J. Arnhold, and K. Arnold, “Cartilage degradation by stimulated human neutrophils: reactive oxygen species decrease markedly the activity of proteolytic enzymes,” Chemistry and Biology, vol. 7, no. 8, pp. 557–568, 2000. View at Publisher · View at Google Scholar · View at Scopus
  26. H. R. Jones, C. T. Robb, M. Perretti, and A. G. Rossi, “The role of neutrophils in inflammation resolution,” Seminars in Immunology, vol. 28, no. 2, pp. 137–145, 2016. View at Google Scholar
  27. S. de Oliveira, E. E. Rosowski, and A. Huttenlocher, “Neutrophil migration in infection and wound repair: going forward in reverse,” Nature Reviews Immunology, vol. 16, no. 6, pp. 378–391, 2016. View at Google Scholar
  28. L. Zuo, T. Zhou, B. K. Pannell, A. C. Ziegler, and T. M. Best, “Biological and physiological role of reactive oxygen species—the good, the bad and the ugly,” Acta Physiologica, vol. 214, no. 3, pp. 329–348, 2015. View at Publisher · View at Google Scholar · View at Scopus
  29. J. Huang, A. Milton, R. D. Arnold et al., “Methods for measuring myeloperoxidase activity toward assessing inhibitor efficacy in living systems,” Journal of Leukocyte Biology, vol. 99, no. 4, pp. 541–548, 2016. View at Publisher · View at Google Scholar
  30. L. A. Marquez and H. B. Dunford, “Kinetics of oxidation of tyrosine and dityrosine by myeloperoxidase compounds I and II: implications for lipoprotein peroxidation studies,” The Journal of Biological Chemistry, vol. 270, no. 51, pp. 30434–30440, 1995. View at Publisher · View at Google Scholar · View at Scopus
  31. P. G. Furtmuller, U. Burner, and C. Obinger, “Reaction of myeloperoxidase compound I with chloride, bromide, iodide, and thiocyanate,” Biochemistry, vol. 37, no. 51, pp. 17923–17930, 1998. View at Publisher · View at Google Scholar · View at Scopus
  32. J. Arnhold and J. Flemmig, “Human myeloperoxidase in innate and acquired immunity,” Archives of Biochemistry and Biophysics, vol. 500, no. 1, pp. 92–106, 2010. View at Publisher · View at Google Scholar · View at Scopus
  33. O. M. Panasenko, I. V. Gorudko, and A. V. Sokolov, “Hypochlorous acid as a precursor of free radicals in living systems,” Biochemistry, vol. 78, no. 13, pp. 1466–1489, 2013. View at Publisher · View at Google Scholar · View at Scopus
  34. A. Korotaeva, E. Samoilova, T. Pavlunina, and O. M. Panasenko, “Halogenated phospholipids regulate secretory phospholipase A2 group IIA activity,” Chemistry and Physics of Lipids, vol. 167-168, pp. 51–56, 2013. View at Publisher · View at Google Scholar · View at Scopus
  35. M. Katrantzis, M. S. Baker, C. J. Handley, and D. A. Lowther, “The oxidant hypochlorite (OCl), a product of the myeloperoxidase system, degrades articular cartilage proteoglycan aggregate,” Free Radical Biology and Medicine, vol. 10, no. 2, pp. 101–109, 1991. View at Publisher · View at Google Scholar · View at Scopus
  36. D. I. Pattison, M. J. Davies, and C. L. Hawkins, “Reactions and reactivity of myeloperoxidase-derived oxidants: differential biological effects of hypochlorous and hypothiocyanous acids,” Free Radical Research, vol. 46, no. 8, pp. 975–995, 2012. View at Publisher · View at Google Scholar · View at Scopus
  37. K. M. Pruitt, D. N. Kamau, K. Miller, B. Månsson-Rahemtulla, and F. Rahemtulla, “Quantitative, standardized assays for determining the concentrations of bovine lactoperoxidase, human salivary peroxidase, and human myeloperoxidase,” Analytical Biochemistry, vol. 191, no. 2, pp. 278–286, 1990. View at Publisher · View at Google Scholar · View at Scopus
  38. Z. Wang, S. J. Nicholls, E. R. Rodriguez et al., “Protein carbamylation links inflammation, smoking, uremia and atherogenesis,” Nature Medicine, vol. 13, no. 10, pp. 1176–1184, 2007. View at Publisher · View at Google Scholar · View at Scopus
  39. J. P. Henderson, J. Byun, M. V. Williams, D. M. Mueller, M. L. McCormick, and J. W. Heinecke, “Production of brominating intermediates by myeloperoxidase. A transhalogenation pathway for generating mutagenic nucleobases during inflammation,” The Journal of Biological Chemistry, vol. 276, no. 11, pp. 7867–7875, 2001. View at Publisher · View at Google Scholar · View at Scopus
  40. T. M. Aune and E. L. Thomas, “Oxidation of protein sulfhydryls by products of peroxidase-catalyzed oxidation of thiocyanate ion,” Biochemistry, vol. 17, no. 6, pp. 1005–1010, 1978. View at Publisher · View at Google Scholar · View at Scopus
  41. J. D. Chandler and B. J. Day, “Thiocyanate: a potentially useful therapeutic agent with host defense and antioxidant properties,” Biochemical Pharmacology, vol. 84, no. 11, pp. 1381–1387, 2012. View at Publisher · View at Google Scholar · View at Scopus
  42. J.-U. Dahl, M. J. Gray, and U. Jakob, “Protein quality control under oxidative stress conditions,” Journal of Molecular Biology, vol. 427, no. 7, pp. 1549–1563, 2015. View at Publisher · View at Google Scholar · View at Scopus
  43. A. Sassa, N. Kamoshita, T. Matsuda et al., “Miscoding properties of 8-chloro-2′-deoxyguanosine, a hypochlorous acid-induced DNA adduct, catalysed by human DNA polymerases,” Mutagenesis, vol. 28, no. 1, pp. 81–88, 2013. View at Publisher · View at Google Scholar · View at Scopus
  44. R. S. Ray and A. Katyal, “Myeloperoxidase: bridging the gap in neurodegeneration,” Neuroscience and Biobehavioral Reviews, vol. 68, pp. 611–620, 2016. View at Google Scholar
  45. S. J. Klebanoff, A. M. Waltersdorph, and H. Rosen, “Antimicrobial activity of myeloperoxidase,” Methods in Enzymology, vol. 105, pp. 399–403, 1984. View at Publisher · View at Google Scholar
  46. B. Fuchs, C. Schober, G. Richter, A. Nimptsch, R. Süß, and J. Schiller, “The reactions between HOCl and differently saturated phospholipids: physiological relevance, products and methods of evaluation,” Mini-Reviews in Organic Chemistry, vol. 5, no. 3, pp. 254–261, 2008. View at Publisher · View at Google Scholar · View at Scopus
  47. A. J. Kettle, A. M. Albrett, A. L. Chapman et al., “Measuring chlorine bleach in biology and medicine,” Biochimica et Biophysica Acta (BBA)—General Subjects, vol. 1840, no. 2, pp. 781–793, 2014. View at Publisher · View at Google Scholar · View at Scopus
  48. B. S. Crow, J. Quiñones-González, B. G. Pantazides et al., “Simultaneous measurement of 3-chlorotyrosine and 3,5-cichlorotyrosine in whole blood, serum and plasma by isotope dilution HPLC-MS-MS,” Journal of Analytical Toxicology, vol. 40, no. 4, pp. 264–271, 2016. View at Publisher · View at Google Scholar
  49. J. P. Gaut, J. Byun, H. D. Tran, and J. W. Heinecke, “Artifact-free quantification of free 3-chlorotyrosine, 3-bromotyrosine, and 3-nitrotyrosine in human plasma by electron capture-negative chemical ionization gas chromatography mass spectrometry and liquid chromatography-electrospray ionization tandem mass spectrometry,” Analytical Biochemistry, vol. 300, no. 2, pp. 252–259, 2002. View at Publisher · View at Google Scholar · View at Scopus
  50. S. Fu, H. Wang, M. Davies, and R. Dean, “Reactions of hypochlorous acid with tyrosine and peptidyl-tyrosyl residues give dichlorinated and aldehydic products in addition to 3-chlorotyrosine,” The Journal of Biological Chemistry, vol. 275, no. 15, pp. 10851–10858, 2000. View at Publisher · View at Google Scholar · View at Scopus
  51. N. M. Domigan, T. S. Charlton, M. W. Duncan, C. C. Winterbourn, and A. J. Kettle, “Chlorination of tyrosyl residues in peptides by myeloperoxidase and human neutrophils,” The Journal of Biological Chemistry, vol. 270, no. 28, pp. 16542–16548, 1995. View at Publisher · View at Google Scholar · View at Scopus
  52. A. R. Mani, S. Ippolito, J. C. Moreno, T. J. Visser, and K. P. Moore, “The metabolism and dechlorination of chlorotyrosine in vivo,” The Journal of Biological Chemistry, vol. 282, no. 40, pp. 29114–29121, 2007. View at Publisher · View at Google Scholar · View at Scopus
  53. J. Talib, G. J. Maghzal, D. Cheng, and R. Stocker, “Detailed protocol to assess in vivo and ex vivo myeloperoxidase activity in mouse models of vascular inflammation and disease using hydroethidine,” Free Radical Biology & Medicine, vol. 97, pp. 124–135, 2016. View at Google Scholar
  54. M. B. Grisham, M. M. Jefferson, D. F. Melton, and E. L. Thomas, “Chlorination of endogenous amines by isolated neutrophils. Ammonia-dependent bactericidal, cytotoxic, and cytolytic activities of the chloramines,” The Journal of Biological Chemistry, vol. 259, no. 16, pp. 10404–10413, 1984. View at Google Scholar · View at Scopus
  55. N. R. Stanley, D. I. Pattison, and C. L. Hawkins, “Ability of hypochlorous acid and N-chloramines to chlorinate DNA and its constituents,” Chemical Research in Toxicology, vol. 23, no. 7, pp. 1293–1302, 2010. View at Publisher · View at Google Scholar · View at Scopus
  56. J. Marcinkiewicz and E. Kontny, “Taurine and inflammatory diseases,” Amino Acids, vol. 46, no. 1, pp. 7–20, 2014. View at Publisher · View at Google Scholar · View at Scopus
  57. J. M. Dypbukt, C. Bishop, W. M. Brooks, B. Thong, H. Eriksson, and A. J. Kettle, “A sensitive and selective assay for chloramine production by myeloperoxidase,” Free Radical Biology and Medicine, vol. 39, no. 11, pp. 1468–1477, 2005. View at Publisher · View at Google Scholar · View at Scopus
  58. O. Skaff, D. I. Pattison, and M. J. Davies, “The vinyl ether linkages of plasmalogens are favored targets for myeloperoxidase-derived oxidants: a kinetic study,” Biochemistry, vol. 47, no. 31, pp. 8237–8245, 2008. View at Publisher · View at Google Scholar · View at Scopus
  59. D. T. Harwood, A. J. Kettle, and C. C. Winterbourn, “Production of glutathione sulfonamide and dehydroglutathione from GSH by myeloperoxidase-derived oxidants and detection using a novel LC–MS/MS method,” Biochemical Journal, vol. 399, no. 1, pp. 161–168, 2006. View at Publisher · View at Google Scholar · View at Scopus
  60. E.-M. Daphna, S. Michaela, P. Eynat, A. Irit, and S. Rimon, “Association of myeloperoxidase with heparin: oxidative inactivation of proteins on the surface of endothelial cells by the bound enzyme,” Molecular and Cellular Biochemistry, vol. 183, no. 1-2, pp. 55–61, 1998. View at Publisher · View at Google Scholar · View at Scopus
  61. J. Leßig, H. Spalteholz, U. Reibetanz et al., “Myeloperoxidase binds to non-vital spermatozoa on phosphatidylserine epitopes,” Apoptosis, vol. 12, no. 10, pp. 1803–1812, 2007. View at Publisher · View at Google Scholar · View at Scopus
  62. C. C. Winterbourn, “Reconciling the chemistry and biology of reactive oxygen species,” Nature Chemical Biology, vol. 4, no. 5, pp. 278–286, 2008. View at Publisher · View at Google Scholar · View at Scopus
  63. N. Thieblemont, H. L. Wright, S. W. Edwards, and V. Witko-Sarsat, “Human neutrophils in auto-immunity,” Seminars in Immunology, vol. 28, no. 2, pp. 159–173, 2016. View at Publisher · View at Google Scholar
  64. M. Deborde and U. von Gunten, “Reactions of chlorine with inorganic and organic compounds during water treatment—kinetics and mechanisms: a critical review,” Water Research, vol. 42, no. 1-2, pp. 13–51, 2008. View at Publisher · View at Google Scholar · View at Scopus
  65. D. I. Pattison, C. L. Hawkins, and M. J. Davies, “Hypochlorous acid-mediated oxidation of lipid components and antioxidants present in low-density lipoproteins: absolute rate constants, product analysis, and computational modeling,” Chemical Research in Toxicology, vol. 16, no. 4, pp. 439–449, 2003. View at Publisher · View at Google Scholar · View at Scopus
  66. C. L. Hawkins and M. J. Davies, “Reaction of HOCl with amino acids and peptides: EPR evidence for rapid rearrangement and fragmentation reactions of nitrogen-centred radicals,” Journal of the Chemical Society, Perkin Transactions, vol. 2, no. 9, pp. 1937–1946, 1998. View at Google Scholar
  67. C. L. Hawkins and M. J. Davies, “Hypochlorite-induced damage to DNA, RNA, and polynucleotides: formation of chloramines and nitrogen-centered radicals,” Chemical Research in Toxicology, vol. 14, pp. 1071–1081, 2001. View at Google Scholar
  68. M. D. Rees, C. L. Hawkins, and M. J. Davies, “Hypochlorite-mediated fragmentation of hyaluronan, chondroitin sulfates, and related N-acetyl glycosamines: evidence for chloramide intermediates, free radical transfer reactions, and site-specific fragmentation,” Journal of the American Chemical Society, vol. 125, no. 45, pp. 13719–13733, 2003. View at Publisher · View at Google Scholar · View at Scopus
  69. Y. Kawai, H. Kiyokawa, Y. Kimura, Y. Kato, K. Tsuchiya, and J. Terao, “Hypochlorous acid-derived modification of phospholipids: characterization of aminophospholipids as regulatory molecules for lipid peroxidation,” Biochemistry, vol. 45, no. 47, pp. 14201–14211, 2006. View at Publisher · View at Google Scholar · View at Scopus
  70. J. Arnhold, S. Hammerschmidt, M. Wagner, S. Mueller, K. Arnold, and E. Grimm, “On the action of hypochlorite on human serum albumin,” Biomedica Biochimica Acta, vol. 49, no. 10, pp. 991–997, 1990. View at Google Scholar · View at Scopus
  71. A. Robaszkiewicz, G. Bartosz, and M. Soszyński, “Effect of N-chloroamino acids on the erythrocyte,” Free Radical Research, vol. 42, no. 1, pp. 30–39, 2008. View at Publisher · View at Google Scholar · View at Scopus
  72. S. A. Salama and R. M. Snapka, “Amino acid chloramine damage to proliferating cell nuclear antigen in mammalian cells,” In Vivo, vol. 26, no. 4, pp. 501–517, 2012. View at Google Scholar · View at Scopus
  73. J. Schiller, B. Fuchs, J. Arnhold, and K. Arnold, “Contribution of reactive oxygen species to cartilage degradation in rheumatic diseases: molecular pathways, diagnosis and potential therapeutic strategies,” Current Medicinal Chemistry, vol. 10, no. 20, pp. 2123–2145, 2003. View at Publisher · View at Google Scholar · View at Scopus
  74. C. L. Hawkins, D. I. Pattison, and M. J. Davies, “Hypochlorite-induced oxidation of amino acids, peptides and proteins,” Amino Acids, vol. 25, no. 3-4, pp. 259–274, 2003. View at Publisher · View at Google Scholar · View at Scopus
  75. Z. Cai and L.-J. Yan, “Protein oxidative modifications: beneficial roles in disease and health,” Journal of Biochemical and Pharmacological Research, vol. 1, no. 1, pp. 15–26, 2013. View at Google Scholar
  76. A. V. Peskin, R. Turner, G. J. Maghzal, C. C. Winterbourn, and A. J. Kettle, “Oxidation of methionine to dehydromethionine by reactive halogen species generated by neutrophils,” Biochemistry, vol. 48, no. 42, pp. 10175–10182, 2009. View at Publisher · View at Google Scholar · View at Scopus
  77. B. S. Rayner, D. T. Love, and C. L. Hawkins, “Comparative reactivity of myeloperoxidase-derived oxidants with mammalian cells,” Free Radical Biology and Medicine, vol. 71, pp. 240–255, 2014. View at Publisher · View at Google Scholar · View at Scopus
  78. Y. Kawai, H. Morinaga, H. Kondo et al., “Endogenous formation of novel halogenated 2′-deoxycytidine: hypohalous acid-mediated DNA modification at the site of inflammation,” The Journal of Biological Chemistry, vol. 279, no. 49, pp. 51241–51249, 2004. View at Publisher · View at Google Scholar · View at Scopus
  79. V. Kuttappan-Nair, F. Samson-Thibault, and J. R. Wagner, “Generation of 2′-deoxyadenosine N6-aminyl radicals from the photolysis of phenylhydrazone derivatives,” Chemical Research in Toxicology, vol. 23, no. 1, pp. 48–54, 2010. View at Publisher · View at Google Scholar · View at Scopus
  80. T. Asahi, H. Kondo, M. Masuda et al., “Chemical and immunochemical detection of 8-halogenated deoxyguanosines at early stage inflammation,” The Journal of Biological Chemistry, vol. 285, no. 12, pp. 9282–9291, 2010. View at Publisher · View at Google Scholar · View at Scopus
  81. B. I. Fedeles, B. D. Freudenthal, E. Yau et al., “Intrinsic mutagenic properties of 5-chlorocytosine: a mechanistic connection between chronic inflammation and cancer,” Proceedings of the National Academy of Sciences of the United States of America, vol. 112, no. 33, pp. E4571–E4580, 2015. View at Publisher · View at Google Scholar · View at Scopus
  82. N. Güngör, A. M. Knaapen, A. Munnia et al., “Genotoxic effects of neutrophils and hypochlorous acid,” Mutagenesis, vol. 25, no. 2, pp. 149–154, 2010. View at Publisher · View at Google Scholar · View at Scopus
  83. A. Valavanidis, T. Vlachogianni, and C. Fiotakis, “8-Hydroxy-2′-deoxyguanosine (8-OHdG): a critical biomarker of oxidative stress and carcinogenesis,” Journal of Environmental Science and Health Part C: Environmental Carcinogenesis and Ecotoxicology Reviews, vol. 27, no. 2, pp. 120–139, 2009. View at Publisher · View at Google Scholar · View at Scopus
  84. C. Badouard, M. Masuda, H. Nishino, J. Cadet, A. Favier, and J.-L. Ravanat, “Detection of chlorinated DNA and RNA nucleosides by HPLC coupled to tandem mass spectrometry as potential biomarkers of inflammation,” Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences, vol. 827, no. 1, pp. 26–31, 2005. View at Publisher · View at Google Scholar · View at Scopus
  85. N. Y. Tretyakova, A. Groehler, and S. Ji, “DNA-protein cross-links: formation, structural identities, and biological outcomes,” Accounts of Chemical Research, vol. 48, no. 6, pp. 1631–1644, 2015. View at Publisher · View at Google Scholar · View at Scopus
  86. C. L. Hawkins, D. I. Pattison, and M. J. Davies, “Reaction of protein chloramines with DNA and nucleosides: evidence for the formation of radicals, protein-DNA cross-links and DNA fragmentation,” Biochemical Journal, vol. 365, no. 3, pp. 605–615, 2002. View at Publisher · View at Google Scholar · View at Scopus
  87. P. A. Kulcharyk and J. W. Heinecke, “Hypochlorous acid produced by the myeloperoxidase system of human phagocytes induces covalent cross-links between DNA and protein,” Biochemistry, vol. 40, no. 12, pp. 3648–3656, 2001. View at Publisher · View at Google Scholar · View at Scopus
  88. B. Fuchs and J. Schiller, “Glycosaminoglycan degradation by selected reactive oxygen species,” Antioxidants & Redox Signaling, vol. 21, no. 7, pp. 1044–1062, 2014. View at Publisher · View at Google Scholar · View at Scopus
  89. J. Arnhold, O. M. Panasenko, J. Schiller, Y. A. Vladimirov, and K. Arnold, “The action of hypochlorous acid on phosphatidylcholine liposomes in dependence on the content of double bonds. Stoichiometry and NMR analysis,” Chemistry and Physics of Lipids, vol. 78, no. 1, pp. 55–64, 1995. View at Publisher · View at Google Scholar · View at Scopus
  90. W. A. Prütz, “Hypochlorous acid interactions with thiols, nucleotides, DNA, and other biological substrates,” Archives of Biochemistry and Biophysics, vol. 332, no. 1, pp. 110–120, 1996. View at Publisher · View at Google Scholar · View at Scopus
  91. D. I. Pattison and M. J. Davies, “Absolute rate constants for the reaction of hypochlorous acid with protein side chains and peptide bonds,” Chemical Research in Toxicology, vol. 14, no. 10, pp. 1453–1464, 2001. View at Publisher · View at Google Scholar · View at Scopus
  92. A. Akeel, S. Sibanda, S. W. Martin, A. W. J. Paterson, and B. J. Parsons, “Chlorination and oxidation of heparin and hyaluronan by hypochlorous acid and hypochlorite anions: effect of sulfate groups on reaction pathways and kinetics,” Free Radical Biology and Medicine, vol. 56, pp. 72–88, 2013. View at Publisher · View at Google Scholar · View at Scopus
  93. M. D. Rees, C. L. Hawkins, and M. J. Davies, “Hypochlorite and superoxide radicals can act synergistically to induce fragmentation of hyaluronan and chondroitin sulphates,” The Biochemical Journal, vol. 381, no. 1, pp. 175–184, 2004. View at Publisher · View at Google Scholar · View at Scopus
  94. C. Termeer, J. P. Sleeman, and J. C. Simon, “Hyaluronan—magic glue for the regulation of the immune response?” Trends in Immunology, vol. 24, no. 3, pp. 112–114, 2003. View at Publisher · View at Google Scholar · View at Scopus
  95. G. Richter, C. Schober, R. Süß, B. Fuchs, C. Birkemeyer, and J. Schiller, “Comparison of the positive and negative ion electrospray ionization and matrix-assisted laser desorption ionization-time-of-flight mass spectra of the reaction products of phosphatidylethanolamines and hypochlorous acid,” Analytical Biochemistry, vol. 376, no. 1, pp. 157–159, 2008. View at Publisher · View at Google Scholar · View at Scopus
  96. L. J. Hazell, M. J. Davies, and R. Stocker, “Secondary radicals derived from chloramines of apolipoprotein B-100 contribute to HOCl-induced lipid peroxidation of low-density lipoproteins,” The Biochemical Journal, vol. 339, no. 3, pp. 489–495, 1999. View at Publisher · View at Google Scholar · View at Scopus
  97. M. R. M. Domingues, A. Reis, and P. Domingues, “Mass spectrometry analysis of oxidized phospholipids,” Chemistry and Physics of Lipids, vol. 156, no. 1-2, pp. 1–12, 2008. View at Publisher · View at Google Scholar · View at Scopus
  98. B. Fuchs, K. Bresler, and J. Schiller, “Oxidative changes of lipids monitored by MALDI MS,” Chemistry and Physics of Lipids, vol. 164, no. 8, pp. 782–795, 2011. View at Publisher · View at Google Scholar · View at Scopus
  99. C. M. Spickett and A. R. Pitt, “Oxidative lipidomics coming of age: advances in analysis of oxidized phospholipids in physiology and pathology,” Antioxidants & Redox Signaling, vol. 22, no. 18, pp. 1646–1666, 2015. View at Publisher · View at Google Scholar · View at Scopus
  100. C. Code, A. K. Mahalka, K. Bry, and P. K. J. Kinnunen, “Activation of phospholipase A2 by 1-palmitoyl-2-(9′-oxo-nonanoyl)-sn-glycero-3-phosphocholine in vitro,” Biochimica et Biophysica Acta—Biomembranes, vol. 1798, no. 8, pp. 1593–1600, 2010. View at Publisher · View at Google Scholar · View at Scopus
  101. W. P. Evans, “Über die Abspaltungsgeschwindigkeiten von Chlorwasserstoff aus Chlorhydrinen und ihre Beziehung zur stereochemischen Konstitution,” Zeitschrift für Physikalische Chemie, vol. 7, pp. 337–357, 1981. View at Google Scholar
  102. P. Petrenko-Kritschenko and A. Konschin, “Ueber die Leichtigkeit der Bildung ringförmiger Verbindungen,” Justus Liebig's Annalen der Chemie, vol. 342, no. 1, pp. 51–59, 1905. View at Publisher · View at Google Scholar
  103. J. Schröter, H. Griesinger, E. Reuß et al., “Unexpected products of the hypochlorous acid-induced oxidation of oleic acid: a study using high performance thin-layer chromatography-electrospray ionization mass spectrometry,” Journal of Chromatography A, vol. 1439, pp. 89–96, 2016. View at Publisher · View at Google Scholar
  104. W.-Y. Wang, C. J. Albert, and D. A. Ford, “Approaches for the analysis of chlorinated lipids,” Analytical Biochemistry, vol. 443, no. 2, pp. 148–152, 2013. View at Publisher · View at Google Scholar · View at Scopus
  105. N. E. Braverman and A. B. Moser, “Functions of plasmalogen lipids in health and disease,” Biochimica et Biophysica Acta—Molecular Basis of Disease, vol. 1822, no. 9, pp. 1442–1452, 2012. View at Publisher · View at Google Scholar · View at Scopus
  106. H. Goldfine, “The appearance, disappearance and reappearance of plasmalogens in evolution,” Progress in Lipid Research, vol. 49, no. 4, pp. 493–498, 2010. View at Publisher · View at Google Scholar · View at Scopus
  107. B. Fuchs, K. Müller, U. Paasch, and J. Schiller, “Lysophospholipids: potential markers of diseases and infertility?” Mini-Reviews in Medicinal Chemistry, vol. 12, no. 1, pp. 74–86, 2012. View at Publisher · View at Google Scholar · View at Scopus
  108. R. C. Murphy, “Free-radical-induced oxidation of arachidonoyl plasmalogen phospholipids: antioxidant mechanism and precursor pathway for bioactive eicosanoids,” Chemical Research in Toxicology, vol. 14, no. 5, pp. 463–472, 2001. View at Publisher · View at Google Scholar · View at Scopus
  109. J. Leßig and B. Fuchs, “HOCl-mediated glycerophosphocholine and glycerophosphoethanolamine generation from plasmalogens in phospholipid mixtures,” Lipids, vol. 45, no. 1, pp. 37–51, 2010. View at Publisher · View at Google Scholar · View at Scopus
  110. S. Wallner and G. Schmitz, “Plasmalogens the neglected regulatory and scavenging lipid species,” Chemistry and Physics of Lipids, vol. 164, no. 6, pp. 573–589, 2011. View at Publisher · View at Google Scholar · View at Scopus
  111. J. Leßig, J. Schiller, J. Arnhold, and B. Fuchs, “Hypochlorous acid-mediated generation of glycerophosphocholine from unsaturated plasmalogen glycerophosphocholine lipids,” The Journal of Lipid Research, vol. 48, no. 6, pp. 1316–1324, 2007. View at Publisher · View at Google Scholar · View at Scopus
  112. A. Üllen, G. Fauler, H. Köfeler et al., “Mouse brain plasmalogens are targets for hypochlorous acid-mediated modification in vitro and in vivo,” Free Radical Biology and Medicine, vol. 49, no. 11, pp. 1655–1665, 2010. View at Publisher · View at Google Scholar · View at Scopus
  113. O. Cynshi and R. Stocker, “Inhibition of lipoprotein lipid oxidation,” Handbook of Experimental Pharmacology, no. 170, pp. 563–590, 2005. View at Google Scholar
  114. D. Hasanally, R. Chaudhary, and A. Ravandi, “Role of phospholipases and oxidized phospholipids in inflammation,” in Phospholipases in Health and Disease, pp. 55–72, Springer, New York, NY, USA, 2014. View at Google Scholar
  115. B. Davis, G. Koster, L. J. Douet et al., “Electrospray ionization mass spectrometry identifies substrates and products of lipoprotein-associated phospholipase A2 in oxidized human low density lipoprotein,” The Journal of Biological Chemistry, vol. 283, no. 10, pp. 6428–6437, 2008. View at Publisher · View at Google Scholar · View at Scopus
  116. M. G. Salgo, F. P. Corongiu, and A. Sevanian, “Enhanced interfacial catalysis and hydrolytic specificity of phospholipase A2 toward peroxidized phosphatidylcholine vesicles,” Archives of Biochemistry and Biophysics, vol. 304, no. 1, pp. 123–132, 1993. View at Publisher · View at Google Scholar · View at Scopus
  117. D. N. Bateman, “Household products,” Medicine, vol. 40, no. 3, pp. 125–126, 2012. View at Publisher · View at Google Scholar · View at Scopus
  118. S. D. Richardson, M. J. Plewa, E. D. Wagner, R. Schoeny, and D. M. DeMarini, “Occurrence, genotoxicity, and carcinogenicity of regulated and emerging disinfection by-products in drinking water: a review and roadmap for research,” Mutation Research—Reviews in Mutation Research, vol. 636, no. 1–3, pp. 178–242, 2007. View at Publisher · View at Google Scholar · View at Scopus
  119. H. R. Spencer, V. Ike, and P. A. Brennan, “Review: the use of sodium hypochlorite in endodontics—potential complications and their management,” British Dental Journal, vol. 202, no. 9, pp. 555–559, 2007. View at Publisher · View at Google Scholar · View at Scopus
  120. A. Nzeusseu Toukap, C. Delporte, C. Noyon et al., “Myeloperoxidase and its products in synovial fluid of patients with treated or untreated rheumatoid arthritis,” Free Radical Research, vol. 48, no. 4, pp. 461–465, 2014. View at Publisher · View at Google Scholar · View at Scopus
  121. W. Wang, Z. Jian, J. Guo, and X. Ning, “Increased levels of serum myeloperoxidase in patients with active rheumatoid arthritis,” Life Sciences, vol. 117, no. 1, pp. 19–23, 2014. View at Publisher · View at Google Scholar · View at Scopus
  122. L. K. Stamp, I. Khalilova, J. M. Tarr et al., “Myeloperoxidase and oxidative stress in rheumatoid arthritis,” Rheumatology, vol. 51, no. 10, pp. 1796–1803, 2012. View at Publisher · View at Google Scholar · View at Scopus
  123. J. Schiller, J. Arnhold, K. Sonntag, and K. Arnold, “NMR studies on human, pathologically changed synovial fluids: role of hypochlorous acid,” Magnetic Resonance in Medicine, vol. 35, no. 6, pp. 848–853, 1996. View at Publisher · View at Google Scholar · View at Scopus
  124. J. Ilisson, M. Zagura, K. Zilmer et al., “Increased carotid artery intima-media thickness and myeloperoxidase level in children with newly diagnosed juvenile idiopathic arthritis,” Arthritis Research & Therapy, vol. 17, article 180, pp. 1–7, 2015. View at Publisher · View at Google Scholar · View at Scopus
  125. C. Pruunsild, K. Heilman, K. Zilmer et al., “Plasma level of myeloperoxidase in children with juvenile idiopathic arthritis (a pilot study),” Open Medicine, vol. 5, no. 1, pp. 36–40, 2010. View at Google Scholar
  126. L. Q. Chen, A. Rohatgi, C. R. Ayers et al., “Race-specific associations of myeloperoxidase with atherosclerosis in a population-based sample: the Dallas Heart Study,” Atherosclerosis, vol. 219, no. 2, pp. 833–838, 2011. View at Publisher · View at Google Scholar · View at Scopus
  127. A. V. Sokolov, K. V. Ageeva, O. S. Cherkalina et al., “Identification and properties of complexes formed by myeloperoxidase with lipoproteins and ceruloplasmin,” Chemistry and Physics of Lipids, vol. 163, no. 4-5, pp. 347–355, 2010. View at Publisher · View at Google Scholar · View at Scopus
  128. S. Sugiyama, Y. Okada, G. K. Sukhova, R. Virmani, J. W. Heinecke, and P. Libby, “Macrophage myeloperoxidase regulation by granulocyte macrophage colony-stimulating factor in human atherosclerosis and implications in acute coronary syndromes,” The American Journal of Pathology, vol. 158, no. 3, pp. 879–891, 2001. View at Publisher · View at Google Scholar · View at Scopus
  129. A. Daugherty, J. L. Dunn, D. L. Rateri, and J. W. Heinecke, “Myeloperoxidase, a catalyst for lipoprotein oxidation, is expressed in human atherosclerotic lesions,” The Journal of Clinical Investigation, vol. 94, no. 1, pp. 437–444, 1994. View at Publisher · View at Google Scholar · View at Scopus
  130. H. Rangé, J. Labreuche, L. Louedec et al., “Periodontal bacteria in human carotid atherothrombosis as a potential trigger for neutrophil activation,” Atherosclerosis, vol. 236, no. 2, pp. 448–455, 2014. View at Publisher · View at Google Scholar · View at Scopus
  131. J. A. Ronald, J. W. Chen, Y. Chen et al., “Enzyme-sensitive magnetic resonance imaging targeting myeloperoxidase identifies active inflammation in experimental rabbit atherosclerotic plaques,” Circulation, vol. 120, no. 7, pp. 592–599, 2009. View at Publisher · View at Google Scholar · View at Scopus
  132. M. Begum, J. Ashok Kumar, H. P. D'Souza et al., “Myeloperoxidase, malondialdehyde and serum lipids in type 2 diabetes mellitus,” Journal of Investigational Biochemistry, vol. 4, no. 1, pp. 13–17, 2015. View at Google Scholar
  133. Y. E. Eksi, Z. E. Karaali, K. Incekara, and H. A. Ergen, “Myeloperoxidase and glutamate-cysteine ligase polymorphisms in type 2 diabetes mellitus: a preliminary study,” Journal of Medical Biochemistry, vol. 33, no. 2, pp. 156–161, 2013. View at Publisher · View at Google Scholar · View at Scopus
  134. J. J. Wiersma, M. C. Meuwese, J. N. I. Van Miert et al., “Diabetes mellitus type 2 is associated with higher levels of myeloperoxidase,” Medical Science Monitor, vol. 14, no. 8, pp. CR406–CR410, 2008. View at Google Scholar · View at Scopus
  135. K. Uchimura, A. Nagasaka, R. Hayashi et al., “Changes in superoxide dismutase activities and concentrations and myeloperoxidase activities in leukocytes from patients with diabetes mellitus,” Journal of Diabetes and Its Complications, vol. 13, no. 5-6, pp. 264–270, 1999. View at Publisher · View at Google Scholar · View at Scopus
  136. S. Tzikas, D. Schlak, K. Sopova et al., “Increased myeloperoxidase plasma levels in patients with Alzheimer's disease,” Journal of Alzheimer's Disease, vol. 39, no. 3, pp. 557–564, 2014. View at Publisher · View at Google Scholar · View at Scopus
  137. R. A. Maki, V. A. Tyurin, R. C. Lyon et al., “Aberrant expression of myeloperoxidase in astrocytes promotes phospholipid oxidation and memory deficits in a mouse model of Alzheimer disease,” The Journal of Biological Chemistry, vol. 284, no. 5, pp. 3158–3169, 2009. View at Publisher · View at Google Scholar · View at Scopus
  138. P. S. Green, A. J. Mendez, J. S. Jacob et al., “Neuronal expression of myeloperoxidase is increased in Alzheimer's disease,” Journal of Neurochemistry, vol. 90, no. 3, pp. 724–733, 2004. View at Publisher · View at Google Scholar · View at Scopus
  139. D.-K. Choi, S. Pennathur, C. Perier et al., “Ablation of the inflammatory enzyme myeloperoxidase mitigates features of Parkinson's disease in mice,” The Journal of Neuroscience, vol. 25, no. 28, pp. 6594–6600, 2005. View at Publisher · View at Google Scholar · View at Scopus
  140. E. Gray, T. L. Thomas, S. Betmouni, N. Scolding, and S. Love, “Elevated activity and microglial expression of myeloperoxidase in demyelinated cerebral cortex in multiple sclerosis,” Brain Pathology, vol. 18, no. 1, pp. 86–95, 2008. View at Publisher · View at Google Scholar · View at Scopus
  141. R. M. Nagra, B. Becher, W. W. Tourtellotte et al., “Immunohistochemical and genetic evidence of myeloperoxidase involvement in multiple sclerosis,” Journal of Neuroimmunology, vol. 78, no. 1-2, pp. 97–107, 1997. View at Publisher · View at Google Scholar · View at Scopus
  142. R. W. Telles, G. A. Ferreira, N. P. Da Silva, and E. I. Sato, “Increased plasma myeloperoxidase levels in systemic lupus erythematosus,” Rheumatology International, vol. 30, no. 6, pp. 779–784, 2010. View at Publisher · View at Google Scholar · View at Scopus
  143. M. Koziol-Montewka, A. Kolodziejek, and J. Oles, “Study on myeloperoxidase role in antituberculous defense in the context of cytokine activation,” Inflammation, vol. 28, no. 2, pp. 53–58, 2004. View at Publisher · View at Google Scholar · View at Scopus
  144. A. Zhu, D. Ge, J. Zhang et al., “Sputum myeloperoxidase in chronic obstructive pulmonary disease,” European Journal of Medical Research, vol. 19, article 12, pp. 1–11, 2014. View at Publisher · View at Google Scholar · View at Scopus
  145. C. O'Donnell, P. Newbold, P. White, B. Thong, H. Stone, and R. A. Stockley, “3-Chlorotyrosine in sputum of COPD patients: relationship with airway inflammation,” COPD: Journal of Chronic Obstructive Pulmonary Disease, vol. 7, no. 6, pp. 411–417, 2010. View at Publisher · View at Google Scholar · View at Scopus
  146. V. M. Keatings and P. J. Barnes, “Granulocyte activation markers in induced sputum: comparison between chronic obstructive pulmonary disease, asthma, and normal subjects,” American Journal of Respiratory and Critical Care Medicine, vol. 155, no. 2, pp. 449–453, 1997. View at Publisher · View at Google Scholar · View at Scopus
  147. A. Van Der Vliet, M. N. Nguyen, M. K. Shigenaga, J. P. Eiserich, G. P. Marelich, and C. E. Cross, “Myeloperoxidase and protein oxidation in cystic fibrosis,” American Journal of Physiology—Lung Cellular and Molecular Physiology, vol. 279, no. 3, pp. L537–L546, 2000. View at Google Scholar · View at Scopus
  148. J. Schröter, R. Süß, and J. Schiller, “MALDI-TOF MS to monitor the kinetics of phospholipase A2-digestion of oxidized phospholipids,” Methods, vol. 104, pp. 41–47, 2016. View at Publisher · View at Google Scholar · View at Scopus
  149. F. Gruber, H. Mayer, B. Lengauer et al., “NF-E2-related factor 2 regulates the stress response to UVA-1-oxidized phospholipids in skin cells,” The FASEB Journal, vol. 24, no. 1, pp. 39–48, 2010. View at Publisher · View at Google Scholar · View at Scopus
  150. P. Bretscher, J. Egger, A. Shamshiev et al., “Phospholipid oxidation generates potent anti-inflammatory lipid mediators that mimic structurally related pro-resolving eicosanoids by activating Nrf2,” EMBO Molecular Medicine, vol. 7, no. 5, pp. 593–607, 2015. View at Publisher · View at Google Scholar · View at Scopus
  151. V. J. Hammond, A. H. Morgan, S. Lauder et al., “Novel keto-phospholipids are generated by monocytes and macrophages, detected in cystic fibrosis, and activate peroxisome proliferator-activated receptor-γ,” The Journal of Biological Chemistry, vol. 287, no. 50, pp. 41651–41666, 2012. View at Publisher · View at Google Scholar · View at Scopus
  152. A. Watson, N. Leitinger, and M. Navab, “Structural identification by mass spectrometry of oxidized phospholipids in minimally oxidized low density lipoprotein that induce monocyte/endothelial interactions,” Journal of Biological Chemistry, vol. 272, no. 21, pp. 13597–13607, 1997. View at Publisher · View at Google Scholar
  153. A. C. Carr, M. C. M. Vissers, N. M. Domigan, and C. C. Winterbourn, “Modification of red cell membrane lipids by hypochlorous acid and haemolysis by preformed lipid chlorohydrins,” Redox Report, vol. 3, no. 5-6, pp. 263–271, 1997. View at Publisher · View at Google Scholar · View at Scopus
  154. A. C. Carr, E. A. Decker, Y. Park, and B. Frei, “Comparison of low-density lipoprotein modification by myeloperoxidase-derived hypochlorous and hypobromous acids,” Free Radical Biology and Medicine, vol. 31, no. 1, pp. 62–72, 2001. View at Publisher · View at Google Scholar · View at Scopus
  155. M. C. M. Vissers, A. Stern, F. Kuypers, J. Van Den Berg, and C. C. Winterbourn, “Membrane changes associated with lysis of red blood cells by hypochlorous acid,” Free Radical Biology and Medicine, vol. 16, no. 6, pp. 703–712, 1994. View at Publisher · View at Google Scholar · View at Scopus
  156. M. C. M. Vissers, A. C. Carr, and C. C. Winterbourn, “Fatty acid chlorohydrins and bromohydrins are cytotoxic to human endothelial cells,” Redox Report, vol. 6, no. 1, pp. 49–56, 2001. View at Publisher · View at Google Scholar · View at Scopus
  157. M. C. M. Vissers, A. C. Carr, and A. L. P. Chapman, “Comparison of human red cell lysis by hypochlorous and hypobromous acids: insights into the mechanism of lysis,” Biochemical Journal, vol. 330, no. 1, pp. 131–138, 1998. View at Publisher · View at Google Scholar · View at Scopus
  158. G. Dever, L.-J. Stewart, A. R. Pitt, and C. M. Spickett, “Phospholipid chlorohydrins cause ATP depletion and toxicity in human myeloid cells,” FEBS Letters, vol. 540, no. 1–3, pp. 245–250, 2003. View at Publisher · View at Google Scholar · View at Scopus
  159. A. Robaszkiewicz, F. H. Greig, A. R. Pitt, C. M. Spickett, G. Bartosz, and M. Soszyński, “Effect of phosphatidylcholine chlorohydrins on human erythrocytes,” Chemistry and Physics of Lipids, vol. 163, no. 7, pp. 639–647, 2010. View at Publisher · View at Google Scholar · View at Scopus
  160. A. Robaszkiewicz, G. Bartosz, A. R. Pitt et al., “HOCl-modified phosphatidylcholines induce apoptosis and redox imbalance in HUVEC-ST cells,” Archives of Biochemistry and Biophysics, vol. 548, pp. 1–10, 2014. View at Publisher · View at Google Scholar · View at Scopus
  161. A. Robaszkiewicz, M. Pogorzelska, G. Bartosz, and M. Soszyński, “Chloric acid(I) affects antioxidant defense of lung epitelial cells,” Toxicology in Vitro, vol. 25, no. 7, pp. 1328–1334, 2011. View at Publisher · View at Google Scholar · View at Scopus
  162. N. Franco-Pons, J. Casas, G. Fabriàs et al., “Fat necrosis generates proinflammatory halogenated lipids during acute pancreatitis,” Annals of Surgery, vol. 257, no. 5, pp. 943–951, 2013. View at Publisher · View at Google Scholar · View at Scopus
  163. A. Petrelli and F. van Wijk, “CD8+ T cells in human autoimmune arthritis: the unusual suspects,” Nature Reviews Rheumatology, vol. 12, no. 7, pp. 421–428, 2016. View at Publisher · View at Google Scholar
  164. C. C. Winterbourn and A. J. Kettle, “Biomarkers of myeloperoxidase-derived hypochlorous acid,” Free Radical Biology and Medicine, vol. 29, no. 5, pp. 403–409, 2000. View at Publisher · View at Google Scholar · View at Scopus
  165. Y. Zhao, C. V. Forst, C. E. Sayegh, I.-M. Wang, X. Yang, and B. Zhang, “Molecular and genetic inflammation networks in major human diseases,” Molecular BioSystems, vol. 12, pp. 2318–2341, 2016. View at Publisher · View at Google Scholar
  166. E. Malle, G. Marsche, J. Arnhold, and M. J. Davies, “Modification of low-density lipoprotein by myeloperoxidase-derived oxidants and reagent hypochlorous acid,” Biochimica et Biophysica Acta—Molecular and Cell Biology of Lipids, vol. 1761, no. 4, pp. 392–415, 2006. View at Publisher · View at Google Scholar · View at Scopus
  167. M. G. Sorci-Thomas and M. J. Thomas, “Microdomains, inflammation, and atherosclerosis,” Circulation Research, vol. 118, no. 4, pp. 679–691, 2016. View at Publisher · View at Google Scholar · View at Scopus
  168. S. L. Hazen, F. F. Hsu, K. Duffin, and J. W. Heinecke, “Molecular chlorine generated by the myeloperoxidase-hydrogen peroxide-chloride system of phagocytes converts low density lipoprotein cholesterol into a family of chlorinated sterols,” The Journal of Biological Chemistry, vol. 271, no. 38, pp. 23080–23088, 1996. View at Publisher · View at Google Scholar · View at Scopus
  169. G. J. Dever, R. Benson, C. L. Wainwright, S. Kennedy, and C. M. Spickett, “Phospholipid chlorohydrin induces leukocyte adhesion to ApoE−/− mouse arteries via upregulation of P-selectin,” Free Radical Biology and Medicine, vol. 44, no. 3, pp. 452–463, 2008. View at Publisher · View at Google Scholar · View at Scopus
  170. J. Yang, Y. Cheng, R. Ji, and C. Zhang, “Novel model of inflammatory neointima formation reveals a potential role of myeloperoxidase in neointimal hyperplasia,” American Journal of Physiology—Heart and Circulatory Physiology, vol. 291, no. 6, pp. H3087–H3093, 2006. View at Publisher · View at Google Scholar · View at Scopus
  171. M. C. Messner, C. J. Albert, J. McHowat, and D. A. Ford, “Identification of lysophosphatidylcholine-chlorohydrin in human atherosclerotic lesions,” Lipids, vol. 43, no. 3, pp. 243–249, 2008. View at Publisher · View at Google Scholar · View at Scopus
  172. T. Matsumoto, T. Kobayashi, and K. Kamata, “Role of lysophosphatidylcholine (LPC) in atherosclerosis,” Current Medicinal Chemistry, vol. 14, no. 30, pp. 3209–3220, 2007. View at Publisher · View at Google Scholar · View at Scopus
  173. A. K. Thukkani, J. McHowat, F.-F. Hsu, M.-L. Brennan, S. L. Hazen, and D. A. Ford, “Identification of α-chloro fatty aldehydes and unsaturated lysophosphatidylcholine molecular species in human atherosclerotic lesions,” Circulation, vol. 108, no. 25, pp. 3128–3133, 2003. View at Publisher · View at Google Scholar · View at Scopus
  174. D. A. Ford, “Lipid oxidation by hypochlorous acid: chlorinated lipids in atherosclerosis and myocardial ischemia,” Clinical Lipidology, vol. 5, no. 6, pp. 835–852, 2010. View at Publisher · View at Google Scholar · View at Scopus
  175. O. A. Akerele and S. K. Cheema, “Fatty acyl composition of lysophosphatidylcholine is important in atherosclerosis,” Medical Hypotheses, vol. 85, no. 6, pp. 754–760, 2015. View at Publisher · View at Google Scholar · View at Scopus
  176. N. D. Hung, D.-E. Sok, and M. R. Kim, “Prevention of 1-palmitoyl lysophosphatidylcholine-induced inflammation by polyunsaturated acyl lysophosphatidylcholine,” Inflammation Research, vol. 61, no. 5, pp. 473–483, 2012. View at Publisher · View at Google Scholar · View at Scopus
  177. N. Aiyar, J. Disa, Z. Ao et al., “Lysophosphatidylcholine induces inflammatory activation of human coronary artery smooth muscle cells,” Molecular and Cellular Biochemistry, vol. 295, no. 1-2, pp. 113–120, 2007. View at Publisher · View at Google Scholar · View at Scopus
  178. K. A. Brown, “The polymorphonuclear cell in rheumatoid arthritis,” Rheumatology, vol. 27, no. 2, pp. 150–155, 1988. View at Publisher · View at Google Scholar · View at Scopus
  179. J. W. Hollingsworth, E. R. Siegel, and W. A. Creasey, “Granulocyte survival in synovial exudate of patients with rheumatoid arthritis and other inflammatory joint diseases,” Yale Journal of Biology and Medicine, vol. 39, no. 5, pp. 289–296, 1967. View at Google Scholar · View at Scopus
  180. A. Seven, S. Güzel, M. Aslan, and V. Hamuryudan, “Lipid, protein, DNA oxidation and antioxidant status in rheumatoid arthritis,” Clinical Biochemistry, vol. 41, no. 7-8, pp. 538–543, 2008. View at Publisher · View at Google Scholar · View at Scopus
  181. M. K. Kosinska, G. Liebisch, G. Lochnit et al., “A lipidomic study of phospholipid classes and species in human synovial fluid,” Arthritis & Rheumatism, vol. 65, no. 9, pp. 2323–2333, 2013. View at Publisher · View at Google Scholar · View at Scopus
  182. B. Fuchs, J. Schiller, U. Wagner, H. Häntzschel, and K. Arnold, “The phosphatidylcholine/lysophosphatidylcholine ratio in human plasma is an indicator of the severity of rheumatoid arthritis: investigations by 31P NMR and MALDI-TOF MS,” Clinical Biochemistry, vol. 38, no. 10, pp. 925–933, 2005. View at Publisher · View at Google Scholar · View at Scopus
  183. M. A. Duerr, R. Aurora, and D. A. Ford, “Identification of glutathione adducts of α-chlorofatty aldehydes produced in activated neutrophils,” Journal of Lipid Research, vol. 56, no. 5, pp. 1014–1024, 2015. View at Publisher · View at Google Scholar · View at Scopus
  184. B. Orosa, S. García, and C. Conde, “The autotaxin-lysophosphatidic acid pathway in pathogenesis of rheumatoid arthritis,” European Journal of Pharmacology, vol. 765, pp. 228–233, 2015. View at Publisher · View at Google Scholar · View at Scopus
  185. B. Orosa, S. García, P. Martínez, A. González, J. J. Gómez-Reino, and C. Conde, “Lysophosphatidic acid receptor inhibition as a new multipronged treatment for rheumatoid arthritis,” Annals of the Rheumatic Diseases, vol. 73, no. 1, pp. 298–305, 2014. View at Publisher · View at Google Scholar · View at Scopus
  186. I. Sevastou, E. Kaffe, M.-A. Mouratis, and V. Aidinis, “Lysoglycerophospholipids in chronic inflammatory disorders: the PLA2/LPC and ATX/LPA axes,” Biochimica et Biophysica Acta—Molecular and Cell Biology of Lipids, vol. 1831, no. 1, pp. 42–60, 2013. View at Publisher · View at Google Scholar · View at Scopus
  187. K. Moore and L. J. Roberts II, “Measurement of lipid peroxidation,” Free Radical Research, vol. 28, no. 6, pp. 659–671, 1998. View at Publisher · View at Google Scholar · View at Scopus
  188. K.-Y. Tserng and R. Griffin, “Quantitation and molecular species determination of diacylglycerols, phosphatidylcholines, ceramides, and sphingomyelins with gas chromatography,” Analytical Biochemistry, vol. 323, no. 1, pp. 84–93, 2003. View at Publisher · View at Google Scholar · View at Scopus
  189. O. Quehenberger, A. M. Armando, and E. A. Dennis, “High sensitivity quantitative lipidomics analysis of fatty acids in biological samples by gas chromatography-mass spectrometry,” Biochimica et Biophysica Acta—Molecular and Cell Biology of Lipids, vol. 1811, no. 11, pp. 648–656, 2011. View at Publisher · View at Google Scholar · View at Scopus
  190. G. Spiteller, “Linoleic acid peroxidation—the dominant lipid peroxidation process in low density lipoprotein-and its relationship to chronic diseases,” Chemistry and Physics of Lipids, vol. 95, no. 2, pp. 105–162, 1998. View at Publisher · View at Google Scholar · View at Scopus
  191. B. K. Wacker, C. J. Albert, B. A. Ford, and D. A. Ford, “Strategies for the analysis of chlorinated lipids in biological systems,” Free Radical Biology and Medicine, vol. 59, pp. 92–99, 2013. View at Publisher · View at Google Scholar · View at Scopus
  192. S. Tumanov, V. Bulusu, and J. J. Kamphorst, “Analysis of fatty acid Metabolism using stable isotope tracers and mass spectrometry,” Methods in Enzymology, vol. 561, pp. 197–217, 2015. View at Publisher · View at Google Scholar
  193. C. C. Winterbourn, J. J. M. van den Berg, E. Roitman, and F. A. Kuypers, “Chlorohydrin formation from unsaturated fatty acids reacted with hypochlorous acid,” Archives of Biochemistry and Biophysics, vol. 296, no. 2, pp. 547–555, 1992. View at Publisher · View at Google Scholar · View at Scopus
  194. A. C. Carr, J. J. M. van den Berg, and C. C. Winterbourn, “Chlorination of cholesterol in cell membranes by hypochlorous acid,” Archives of Biochemistry and Biophysics, vol. 332, no. 1, pp. 63–69, 1996. View at Publisher · View at Google Scholar · View at Scopus
  195. T. A. Isbell, R. Kleiman, and B. A. Plattner, “Acid-catalyzed condensation of oleic acid into estolides and polyestolides,” Journal of the American Oil Chemists' Society, vol. 71, no. 2, pp. 169–174, 1994. View at Publisher · View at Google Scholar · View at Scopus
  196. B. Fuchs, R. Süß, and J. Schiller, “An update of MALDI-TOF mass spectrometry in lipid research,” Progress in Lipid Research, vol. 49, no. 4, pp. 450–475, 2010. View at Publisher · View at Google Scholar · View at Scopus
  197. J. Arnhold, A. N. Osipov, H. Spalteholz, O. M. Panasenko, and J. Schiller, “Effects of hypochlorous acid on unsaturated phosphatidylcholines,” Free Radical Biology and Medicine, vol. 31, no. 9, pp. 1111–1119, 2001. View at Publisher · View at Google Scholar · View at Scopus
  198. J. Arnhold, A. N. Osipov, H. Spalteholz, O. M. Panasenko, and J. Schiller, “Formation of lysophospholipids from unsaturated phosphatidylcholines under the influence of hypochlorous acid,” Biochimica et Biophysica Acta—General Subjects, vol. 1572, no. 1, pp. 91–100, 2002. View at Publisher · View at Google Scholar · View at Scopus
  199. C. Schober, J. Schiller, F. Pinker, J. G. Hengstler, and B. Fuchs, “Lysophosphatidylethanolamine is—in contrast to—choline—generated under in vivo conditions exclusively by phospholipase A2 but not by hypochlorous acid,” Bioorganic Chemistry, vol. 37, no. 6, pp. 202–210, 2009. View at Google Scholar
  200. J. Wu, K. Teuber, M. Eibisch, B. Fuchs, and J. Schiller, “Chlorinated and brominated phosphatidylcholines are generated under the influence of the Fenton reagent at low pH—a MALDI-TOF MS study,” Chemistry and Physics of Lipids, vol. 164, no. 1, pp. 1–8, 2011. View at Publisher · View at Google Scholar · View at Scopus
  201. M. Saran, I. Beck-Speier, B. Fellerhoff, and G. Bauer, “Phagocytic killing of microorganisms by radical processes: consequences of the reaction of hydroxyl radicals with chloride yielding chlorine atoms,” Free Radical Biology and Medicine, vol. 26, no. 3-4, pp. 482–490, 1999. View at Publisher · View at Google Scholar · View at Scopus
  202. M. Saran and W. Bors, “Radiation chemistry of physiological saline reinvestigated: evidence that chloride-derived intermediates play a key role in cytotoxicity,” Radiation Research, vol. 147, no. 1, pp. 70–77, 1997. View at Publisher · View at Google Scholar · View at Scopus
  203. T. Jaskolla, B. Fuchs, M. Karas, and J. Schiller, “The new matrix 4-chloro-α-cyanocinnamic acid allows the detection of phosphatidylethanolamine chloramines by MALDI-TOF mass spectrometry,” Journal of the American Society for Mass Spectrometry, vol. 20, no. 5, pp. 867–874, 2009. View at Publisher · View at Google Scholar · View at Scopus
  204. M. B. O'Rourke, S. P. Djordjevic, and M. P. Padula, “The quest for improved reproducibility in MALDI mass spectrometry,” Mass Spectrometry Reviews, 2016. View at Publisher · View at Google Scholar
  205. M. Wang, C. Wang, R. H. Han, and X. Han, “Novel advances in shotgun lipidomics for biology and medicine,” Progress in Lipid Research, vol. 61, pp. 83–108, 2016. View at Publisher · View at Google Scholar
  206. J. Schiller, R. Süß, B. Fuchs, M. Müller, O. Zschörnig, and K. Arnold, “MALDI-TOF MS in lipidomics,” Frontiers in Bioscience, vol. 12, pp. 2568–2579, 2007. View at Google Scholar
  207. A. Jerlich, A. R. Pitt, R. J. Schaur, and C. M. Spickett, “Pathways of phospholipid oxidation by HOCl in human LDL detected by LC-MS,” Free Radical Biology and Medicine, vol. 28, no. 5, pp. 673–682, 2000. View at Publisher · View at Google Scholar · View at Scopus
  208. S. Miyamoto, G. R. Martinez, D. Rettori, O. Augusto, M. H. G. Medeiros, and P. Di Mascio, “Linoleic acid hydroperoxide reacts with hypochlorous acid, generating peroxyl radical intermediates and singlet molecular oxygen,” Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 2, pp. 293–298, 2006. View at Publisher · View at Google Scholar · View at Scopus
  209. A. Jerlich, L. Horakova, J. S. Fabjan, A. Giessauf, G. Jürgens, and R. J. Schaur, “Correlation of low-density lipoprotein modification by myeloperoxidase with hypochlorous acid formation,” International Journal of Clinical & Laboratory Research, vol. 29, no. 4, pp. 155–161, 1999. View at Publisher · View at Google Scholar · View at Scopus
  210. A. Jerlich, R. J. Schaur, A. R. Pitt, and C. M. Spickett, “The formation of phosphatidylcholine oxidation products by stimulated phagocytes,” Free Radical Research, vol. 37, no. 6, pp. 645–653, 2003. View at Publisher · View at Google Scholar · View at Scopus
  211. C. J. Albert, D. S. Anbukumar, M. C. Messner, and D. A. Ford, “Chromatographic methods for the analyses of 2-halofatty aldehydes and chlorohydrin molecular species of lysophosphatidylcholine,” Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences, vol. 877, no. 26, pp. 2768–2777, 2009. View at Publisher · View at Google Scholar · View at Scopus
  212. F.-F. Hsu, J. Turk, A. K. Thukkani, M. C. Messner, K. R. Wildsmith, and D. A. Ford, “Characterization of alkylacyl, alk-1-enylacyl and lyso subclasses of glycerophosphocholine by tandem quadrupole mass spectrometry with electrospray ionization,” Journal of Mass Spectrometry, vol. 38, no. 7, pp. 752–763, 2003. View at Publisher · View at Google Scholar · View at Scopus
  213. W. C. Byrdwell, “Atmospheric pressure chemical ionization mass spectrometry for analysis of lipids,” Lipids, vol. 36, no. 4, pp. 327–346, 2001. View at Publisher · View at Google Scholar · View at Scopus
  214. A. Kuksis, J.-P. Suomela, M. Tarvainen, and H. Kallio, “Lipidomic analysis of glycerolipid and cholesteryl ester autooxidation products,” Molecular Biotechnology, vol. 42, no. 2, pp. 224–268, 2009. View at Publisher · View at Google Scholar · View at Scopus
  215. C. Mesaros, S. H. Lee, and I. A. Blair, “Targeted quantitative analysis of eicosanoid lipids in biological samples using liquid chromatography-tandem mass spectrometry,” Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences, vol. 877, no. 26, pp. 2736–2745, 2009. View at Publisher · View at Google Scholar · View at Scopus
  216. J. van den Berg and C. Winterbourn, “Measurement of reaction products from hypochlorous acid and unsaturated lipids,” Methods in Enzymology, vol. 233, pp. 639–649, 1994. View at Google Scholar
  217. O. M. Panasenko, J. Amhold, J. Schiller, K. Arnold, and V. I. Sergienko, “Peroxidation of egg yolk phosphatidylcholine liposomes by hypochlorous acid,” Biochimica et Biophysica Acta—Lipids and Lipid Metabolism, vol. 1215, no. 3, pp. 259–266, 1994. View at Publisher · View at Google Scholar · View at Scopus
  218. J. Schiller, M. Müller, B. Fuchs, K. Arnold, and D. Huster, “31P NMR spectroscopy of phospholipids: from micelles to membranes,” Current Analytical Chemistry, vol. 3, no. 4, pp. 283–301, 2007. View at Publisher · View at Google Scholar · View at Scopus
  219. R. Servaty, J. Schiller, H. Binder, B. Kohlstrunk, and K. Arnold, “IR and NMR studies on the action of hypochlorous acid on chondroitin sulfate and taurine,” Bioorganic Chemistry, vol. 26, no. 1, pp. 33–43, 1998. View at Publisher · View at Google Scholar
  220. E. L. Thomas, M. B. Grisham, and M. M. Jefferson, “Preparation and characterization of chloramines,” Methods in Enzymology, vol. 132, pp. 569–585, 1986. View at Publisher · View at Google Scholar
  221. B. Fuchs, R. Süß, K. Teuber, M. Eibisch, and J. Schiller, “Lipid analysis by thin-layer chromatography—a review of the current state,” Journal of Chromatography A, vol. 1218, no. 19, pp. 2754–2774, 2011. View at Publisher · View at Google Scholar · View at Scopus
  222. B. Fuchs, J. Schiller, R. Süß et al., “Analysis of stem cell lipids by offline HPTLC-MALDI-TOF MS,” Analytical and Bioanalytical Chemistry, vol. 392, no. 5, pp. 849–860, 2008. View at Publisher · View at Google Scholar · View at Scopus
  223. H. Jin, T. S. Hallstrand, D. S. Daly et al., “A halotyrosine antibody that detects increased protein modifications in asthma patients,” Journal of Immunological Methods, vol. 403, no. 1-2, pp. 17–25, 2014. View at Publisher · View at Google Scholar · View at Scopus
  224. R. J. Goiffon, S. C. Martinez, and D. Piwnica-Worms, “A rapid bioluminescence assay for measuring myeloperoxidase activity in human plasma,” Nature Communications, vol. 6, article 6271, 9 pages, 2015. View at Publisher · View at Google Scholar · View at Scopus
  225. N. M. Domigan, A. C. Carr, J. G. Lewis, P. A. Elder, and C. C. Winterbourn, “A monoclonal antibody recognizing the chlorohydrin derivatives of oleic acid for probing hypochlorous acid involvement in tissue injury,” Redox Report, vol. 3, no. 2, pp. 111–117, 1997. View at Publisher · View at Google Scholar · View at Scopus