Table of Contents Author Guidelines Submit a Manuscript
Oxidative Medicine and Cellular Longevity
Volume 2017, Article ID 6501046, 32 pages
https://doi.org/10.1155/2017/6501046
Review Article

Measurement and Clinical Significance of Biomarkers of Oxidative Stress in Humans

1Department of Biochemical Sciences “A. Rossi Fanelli”, Sapienza University, P.le A. Moro 5, 00185 Rome, Italy
2Center for Food and Nutrition, Council for Agricultural Research and Economics (CREA-AN), Via Ardeatina 546, 00178 Rome, Italy

Correspondence should be addressed to Ilaria Peluso; ti.ilacsit@osulep.i

Received 14 March 2017; Revised 26 April 2017; Accepted 21 May 2017; Published 18 June 2017

Academic Editor: Antonio Ayala

Copyright © 2017 Ilaria Marrocco et al. 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. M. Valko, D. Leibfritz, J. Moncol, M. T. Cronin, M. Mazur, and J. Telser, “Free radicals and antioxidants in normal physiological functions and human disease,” The International Journal of Biochemistry & Cell Biology, vol. 39, no. 1, pp. 44–84, 2007. View at Publisher · View at Google Scholar · View at Scopus
  2. D. R. Bickers and M. Athar, “Oxidative stress in the pathogenesis of skin disease,” The Journal of Investigative Dermatology, vol. 126, no. 12, pp. 2565–2575, 2006. View at Publisher · View at Google Scholar · View at Scopus
  3. R. Franco, R. Sanchez-Olea, E. M. Reyes-Reyes, and M. I. Panayiotidis, “Environmental toxicity, oxidative stress and apoptosis: menage a trois,” Mutation Research, vol. 674, no. 1-2, pp. 3–22, 2009. View at Google Scholar
  4. M. Hodjat, M. A. Rezvanfar, and M. Abdollahi, “A systematic review on the role of environmental toxicants in stem cells aging,” Food and Chemical Toxicology, vol. 86, pp. 298–308, 2015. View at Publisher · View at Google Scholar · View at Scopus
  5. A. Negre-Salvayre, N. Auge, V. Ayala et al., “Pathological aspects of lipid peroxidation,” Free Radical Research, vol. 44, no. 10, pp. 1125–1171, 2010. View at Publisher · View at Google Scholar · View at Scopus
  6. R. A. Roberts, R. A. Smith, S. Safe, C. Szabo, R. B. Tjalkens, and F. M. Robertson, “Toxicological and pathophysiological roles of reactive oxygen and nitrogen species,” Toxicology, vol. 276, no. 2, pp. 85–94, 2010. View at Publisher · View at Google Scholar · View at Scopus
  7. A. Musatov and N. C. Robinson, “Susceptibility of mitochondrial electron-transport complexes to oxidative damage. Focus on cytochrome c oxidase,” Free Radical Research, vol. 46, no. 11, pp. 1313–1326, 2012. View at Publisher · View at Google Scholar · View at Scopus
  8. J. El-Benna, M. Hurtado-Nedelec, V. Marzaioli, J. C. Marie, M. A. Gougerot-Pocidalo, and P. M. Dang, “Priming of the neutrophil respiratory burst: role in host defense and inflammation,” Immunological Reviews, vol. 273, no. 1, pp. 180–193, 2016. View at Publisher · View at Google Scholar · View at Scopus
  9. M. Jaganjac, A. Cipak, R. J. Schaur, and N. Zarkovic, “Pathophysiology of neutrophil-mediated extracellular redox reactions,” Frontiers in Bioscience (Landmark edition), vol. 21, pp. 839–855, 2016. View at Publisher · View at Google Scholar
  10. W. H. Koppenol, P. L. Bounds, T. Nauser, R. Kissner, and H. Ruegger, “Peroxynitrous acid: controversy and consensus surrounding an enigmatic oxidant,” Dalton Transactions, vol. 41, no. 45, pp. 13779–13787, 2012. View at Publisher · View at Google Scholar · View at Scopus
  11. K. Roy, Y. Wu, J. L. Meitzler et al., “NADPH oxidases and cancer,” Clinical Science (London, England), vol. 128, no. 12, pp. 863–875, 2015. View at Publisher · View at Google Scholar · View at Scopus
  12. M. Ushio-Fukai and Y. Nakamura, “Reactive oxygen species and angiogenesis: NADPH oxidase as target for cancer therapy,” Cancer Letters, vol. 266, no. 1, pp. 37–52, 2008. View at Publisher · View at Google Scholar · View at Scopus
  13. P. Chiarugi and T. Fiaschi, “Redox signalling in anchorage-dependent cell growth,” Cellular Signalling, vol. 19, no. 4, pp. 672–682, 2007. View at Publisher · View at Google Scholar · View at Scopus
  14. R. Hu, C. L. Saw, R. Yu, and A. N. Kong, “Regulation of NF-E2-related factor 2 signaling for cancer chemoprevention: antioxidant coupled with antiinflammatory,” Antioxidants & Redox Signaling, vol. 13, no. 11, pp. 1679–1698, 2010. View at Publisher · View at Google Scholar · View at Scopus
  15. D. N. Granger and P. R. Kvietys, “Reperfusion injury and reactive oxygen species: the evolution of a concept,” Redox Biology, vol. 6, pp. 524–551, 2015. View at Publisher · View at Google Scholar · View at Scopus
  16. S. Matsushima, H. Tsutsui, and J. Sadoshima, “Physiological and pathological functions of NADPH oxidases during myocardial ischemia-reperfusion,” Trends in Cardiovascular Medicine, vol. 24, no. 5, pp. 202–5, 2014. View at Publisher · View at Google Scholar · View at Scopus
  17. Y. Sawikr, N. Sastry Yarla, I. Peluso, M. A. Kamal, G. Aliev, and A. Bishayee, “Neuroinflammation in Alzheimer’s disease: the preventive and therapeutic potential of polyphenolic nutraceuticals,” Advances in Protein Chemistry and Structural Biology, vol. 108, pp. 33–57, 2017. View at Publisher · View at Google Scholar
  18. R. S. Ferrari and C. F. Andrade, “Oxidative stress and lung ischemia-reperfusion injury,” Oxidative Medicine and Cellular Longevity, vol. 2015, Article ID 590987, 14 pages, 2015. View at Publisher · View at Google Scholar · View at Scopus
  19. M. Malek and M. Nematbakhsh, “Renal ischemia/reperfusion injury; from pathophysiology to treatment,” Journal of Renal Injury Prevention, vol. 4, no. 2, pp. 20–27, 2015. View at Publisher · View at Google Scholar
  20. S. Rohrbach, C. Troidl, C. Hamm, and R. Schulz, “Ischemia and reperfusion related myocardial inflammation: a network of cells and mediators targeting the cardiomyocyte,” IUBMB Life, vol. 67, no. 2, pp. 110–119, 2015. View at Publisher · View at Google Scholar · View at Scopus
  21. G. A. Kurian, R. Rajagopal, S. Vedantham, and M. Rajesh, “The role of oxidative stress in myocardial ischemia and reperfusion injury and remodeling: revisited,” Oxidative Medicine and Cellular Longevity, vol. 2016, Article ID 1656450, 14 pages, 2016. View at Publisher · View at Google Scholar · View at Scopus
  22. L. Y. Guan, P. Y. Fu, P. D. Li et al., “Mechanisms of hepatic ischemia-reperfusion injury and protective effects of nitric oxide,” World Journal of Gastrointestinal Surgery, vol. 6, no. 7, pp. 122–128, 2014. View at Publisher · View at Google Scholar
  23. T. Zhou, C. C. Chuang, and L. Zuo, “Molecular characterization of reactive oxygen species in myocardial ischemia-reperfusion injury,” BioMed Research International, vol. 2015, Article ID 864946, 9 pages, 2015. View at Publisher · View at Google Scholar · View at Scopus
  24. N. Poulose and R. Raju, “Aging and injury: alterations in cellular energetics and organ function,” Aging and Disease, vol. 5, no. 2, pp. 101–108, 2014. View at Publisher · View at Google Scholar · View at Scopus
  25. P. B. Ham 3rd and R. Raju, “Mitochondrial function in hypoxic ischemic injury and influence of aging,” Progress in Neurobiology, 2016, Epub ahead of print. View at Publisher · View at Google Scholar · View at Scopus
  26. J. Labat-Robert and L. Robert, “Longevity and aging. Role of free radicals and xanthine oxidase. A review,” Pathologie et Biologie, vol. 62, no. 2, pp. 61–66, 2014. View at Publisher · View at Google Scholar · View at Scopus
  27. I. Peluso, G. Morabito, L. Urban, F. Ioannone, and M. Serafini, “Oxidative stress in atherosclerosis development: the central role of LDL and oxidative burst,” Endocrine, Metabolic & Immune Disorders Drug Targets, vol. 12, no. 4, pp. 351–360, 2012. View at Publisher · View at Google Scholar · View at Scopus
  28. D. Pietraforte, R. Vona, A. Marchesi et al., “Redox control of platelet functions in physiology and pathophysiology,” Antioxidants & Redox Signaling, vol. 21, no. 1, pp. 177–193, 2014. View at Publisher · View at Google Scholar · View at Scopus
  29. A. Assinger, F. Koller, W. Schmid, M. Zellner, E. Koller, and I. Volf, “Hypochlorite-oxidized LDL induces intraplatelet ROS formation and surface exposure of CD40L—a prominent role of CD36,” Atherosclerosis, vol. 213, no. 1, pp. 129–134, 2010. View at Publisher · View at Google Scholar · View at Scopus
  30. C. C. Winterbourn, “The challenges of using fluorescent probes to detect and quantify specific reactive oxygen species in living cells,” Biochimica et Biophysica Acta, vol. 1840, no. 2, pp. 730–738, 2014. View at Google Scholar
  31. S. I. Dikalov and D. G. Harrison, “Methods for detection of mitochondrial and cellular reactive oxygen species,” Antioxidants & Redox Signaling, vol. 20, no. 2, pp. 372–382, 2014. View at Publisher · View at Google Scholar · View at Scopus
  32. C. Elbim and G. Lizard, “Flow cytometric investigation of neutrophil oxidative burst and apoptosis in physiological and pathological situations,” Cytometry. Part a, vol. 75, no. 6, pp. 475–481, 2009. View at Publisher · View at Google Scholar · View at Scopus
  33. M. Freitas, J. L. Lima, and E. Fernandes, “Optical probes for detection and quantification of neutrophils’ oxidative burst. A review,” Analytica Chimica Acta, vol. 649, no. 1, pp. 8–23, 2009. View at Publisher · View at Google Scholar · View at Scopus
  34. G. Finak, M. Langweiler, M. Jaimes et al., “Standardizing flow cytometry Immunophenotyping analysis from the Human ImmunoPhenotyping Consortium,” Scientific Reports, vol. 6, p. 20686, 2016. View at Publisher · View at Google Scholar · View at Scopus
  35. B. Rajwa, P. K. Wallace, E. A. Griffiths, and M. Dundar, “Automated assessment of disease progression in acute myeloid leukemia by probabilistic analysis of flow cytometry data,” IEEE Transactions on Biomedical Engineering, vol. 64, no. 5, pp. 1089–1098, 2017. View at Publisher · View at Google Scholar
  36. N. J. Gormley, D. M. Turley, J. S. Dickey et al., “Regulatory perspective on minimal residual disease flow cytometry testing in multiple myeloma,” Cytometry. Part B, Clinical Cytometry, vol. 90, no. 1, pp. 73–80, 2016. View at Publisher · View at Google Scholar
  37. M. M. Sartor and D. J. Gottlieb, “A single tube 10-color flow cytometry assay optimizes detection of minimal residual disease in chronic lymphocytic leukemia,” Cytometry. Part B, Clinical Cytometry, vol. 84, no. 2, pp. 96–103, 2013. View at Publisher · View at Google Scholar · View at Scopus
  38. C. Algrin, J. L. Golmard, M. Michallet et al., “Flow cytometry minimal residual disease after allogeneic transplant for chronic lymphocytic leukemia,” European Journal of Haematology, vol. 98, no. 4, pp. 363–370, 2017. View at Publisher · View at Google Scholar
  39. V. Bordoni, R. Casetti, G. Capuano et al., “A novel 8-color flow cytometry panel to study activation, maturation and senescence of CD4 and CD8 T lymphocytes in HIV-infected individuals at different stages of disease,” International Journal of Immunopathology and Pharmacology, vol. 25, no. 2, pp. 415–424, 2012. View at Publisher · View at Google Scholar
  40. B. B. Nkambule, G. M. Davison, and H. Ipp, “The evaluation of platelet function in HIV infected, asymptomatic treatment-naive individuals using flow cytometry,” Thrombosis Research, vol. 135, no. 6, pp. 1131–1139, 2015. View at Publisher · View at Google Scholar · View at Scopus
  41. L. Whitby, A. Whitby, M. Fletcher, and D. Barnett, “Current laboratory practices in flow cytometry for the enumeration of CD 4+ T-lymphocyte subsets,” Cytometry. Part B, Clinical Cytometry, vol. 88, no. 5, pp. 305–311, 2015. View at Publisher · View at Google Scholar · View at Scopus
  42. R. El Hawary, S. Meshaal, C. Deswarte et al., “Role of flow cytometry in the diagnosis of chronic granulomatous disease: the Egyptian experience,” Journal of Clinical Immunology, vol. 36, no. 6, pp. 610–618, 2016. View at Publisher · View at Google Scholar · View at Scopus
  43. M. G. Macey, J. Sangster, P. A. Veys, and A. C. Newland, “Flow cytometric analysis of the functional ability of neutrophils from patients with autoimmune neutropenia,” Journal of Microscopy, vol. 159, Part 3, pp. 277–283, 1990. View at Google Scholar
  44. G. T. Spear, H. A. Kessler, L. Rothberg, J. Phair, and A. L. Landay, “Decreased oxidative burst activity of monocytes from asymptomatic HIV-infected individuals,” Clinical Immunology and Immunopathology, vol. 54, no. 2, pp. 184–191, 1990. View at Publisher · View at Google Scholar · View at Scopus
  45. A. Gomes, E. Fernandes, and J. L. Lima, “Fluorescence probes used for detection of reactive oxygen species,” Journal of Biochemical and Biophysical Methods, vol. 65, no. 2-3, pp. 45–80, 2005. View at Publisher · View at Google Scholar · View at Scopus
  46. B. Kalyanaraman, V. Darley-Usmar, K. J. Davies et al., “Measuring reactive oxygen and nitrogen species with fluorescent probes: challenges and limitations,” Free Radical Biology & Medicine, vol. 52, no. 1, pp. 1–6, 2012. View at Publisher · View at Google Scholar · View at Scopus
  47. I. Peluso, H. Manafikhi, R. Reggi, and M. Palmery, “Interference of flavonoids with fluorescent intracellular probes: methodological implications in the evaluation of the oxidative burst by flow cytometry,” Cytometry. Part A, vol. 85, no. 8, pp. 663–677, 2014. View at Publisher · View at Google Scholar · View at Scopus
  48. M. Becatti, C. Fiorillo, A. M. Gori et al., “Platelet and leukocyte ROS production and lipoperoxidation are associated with high platelet reactivity in non-ST elevation myocardial infarction (NSTEMI) patients on dual antiplatelet treatment,” Atherosclerosis, vol. 231, no. 2, pp. 392–400, 2013. View at Publisher · View at Google Scholar · View at Scopus
  49. I. Peluso, H. Manafikhi, F. Altieri, C. Zanza, and M. Palmery, “The effect of sample storage on the peroxidation of leukocytes index ratio (PLIR) measure,” Scientific Reports, vol. 4, p. 6539, 2014. View at Publisher · View at Google Scholar · View at Scopus
  50. G. P. Drummen, B. M. Gadella, J. A. Post, and J. F. Brouwers, “Mass spectrometric characterization of the oxidation of the fluorescent lipid peroxidation reporter molecule C11-BODIPY(581/591),” Free Radical Biology & Medicine, vol. 36, no. 12, pp. 1635–1644, 2004. View at Publisher · View at Google Scholar · View at Scopus
  51. G. P. Drummen, L. C. van Liebergen, J. A. Op den Kamp, and J. A. Post, “C11-BODIPY(581/591), an oxidation-sensitive fluorescent lipid peroxidation probe: (micro)spectroscopic characterization and validation of methodology,” Free Radical Biology & Medicine, vol. 33, no. 4, pp. 473–490, 2002. View at Publisher · View at Google Scholar · View at Scopus
  52. A. C. Nicolescu, Q. Li, L. Brown, and G. R. Thatcher, “Nitroxidation, nitration, and oxidation of a BODIPY fluorophore by RNOS and ROS,” Nitric Oxide, vol. 15, no. 2, pp. 163–176, 2006. View at Publisher · View at Google Scholar · View at Scopus
  53. I. Peluso, H. Manafikhi, R. Reggi, Y. Longhitano, C. Zanza, and M. Palmery, “Relationship between the peroxidation of leukocytes index ratio and the improvement of postprandial metabolic stress by a functional food,” Oxidative Medicine and Cellular Longevity, vol. 2016, Article ID 5630985, 10 pages, 2016. View at Publisher · View at Google Scholar · View at Scopus
  54. J. Fernandez, L. Marin, R. Alvarez-Alonso et al., “Biosynthetic modularity rules in the bisintercalator family of antitumor compounds,” Marine Drugs, vol. 12, no. 5, pp. 2668–2699, 2014. View at Publisher · View at Google Scholar · View at Scopus
  55. M. Ciz, P. Denev, M. Kratchanova, O. Vasicek, G. Ambrozova, and A. Lojek, “Flavonoids inhibit the respiratory burst of neutrophils in mammals,” Oxidative Medicine and Cellular Longevity, vol. 2012, Article ID 181295, 6 pages, 2012. View at Publisher · View at Google Scholar · View at Scopus
  56. H. J. Bromme, L. Zuhlke, R. E. Silber, and A. Simm, “DCFH2 interactions with hydroxyl radicals and other oxidants—influence of organic solvents,” Experimental Gerontology, vol. 43, no. 7, pp. 638–644, 2008. View at Publisher · View at Google Scholar · View at Scopus
  57. B. Laupeze, L. Amiot, L. Payen et al., “Multidrug resistance protein (MRP) activity in normal mature leukocytes and CD34-positive hematopoietic cells from peripheral blood,” Life Sciences, vol. 68, no. 11, pp. 1323–1331, 2001. View at Publisher · View at Google Scholar · View at Scopus
  58. J. F. Arthur, J. Qiao, Y. Shen et al., “ITAM receptor-mediated generation of reactive oxygen species in human platelets occurs via Syk-dependent and Syk-independent pathways,” Journal of Thrombosis and Haemostasis, vol. 10, no. 6, pp. 1133–1141, 2012. View at Publisher · View at Google Scholar · View at Scopus
  59. W. Siffert, G. Siffert, P. Scheid, and J. W. Akkerman, “Activation of Na+/H+ exchange and Ca2+ mobilization start simultaneously in thrombin-stimulated platelets. Evidence that platelet shape change disturbs early rises of BCECF fluorescence which causes an underestimation of actual cytosolic alkalinization,” The Biochemical Journal, vol. 258, no. 2, pp. 521–527, 1989. View at Publisher · View at Google Scholar
  60. O. Aharonovitz, H. Fridman, A. A. Livne, and Y. Granot, “The effect of BCECF on intracellular pH of human platelets,” Biochimica et Biophysica Acta, vol. 1284, no. 2, pp. 227–232, 1996. View at Google Scholar
  61. T. Bagrij, A. Klokouzas, S. B. Hladky, and M. A. Barrand, “Influences of glutathione on anionic substrate efflux in tumour cells expressing the multidrug resistance-associated protein, MRP1,” Biochemical Pharmacology, vol. 62, no. 2, pp. 199–206, 2001. View at Publisher · View at Google Scholar · View at Scopus
  62. J. M. Maher, M. Z. Dieter, L. M. Aleksunes et al., “Oxidative and electrophilic stress induces multidrug resistance-associated protein transporters via the nuclear factor-E2-related factor-2 transcriptional pathway,” Hepatology, vol. 46, no. 5, pp. 1597–1610, 2007. View at Publisher · View at Google Scholar · View at Scopus
  63. M. Iwanaga, K. Mori, T. Iida et al., “Nuclear factor kappa B dependent induction of gamma glutamylcysteine synthetase by ionizing radiation in T98G human glioblastoma cells,” Free Radical Biology & Medicine, vol. 24, no. 7-8, pp. 1256–1268, 1998. View at Publisher · View at Google Scholar · View at Scopus
  64. L. Deng, Y. C. Lin-Lee, F. X. Claret, and M. T. Kuo, “2-acetylaminofluorene up-regulates rat mdr1b expression through generating reactive oxygen species that activate NF-kappa B pathway,” The Journal of Biological Chemistry, vol. 276, no. 1, pp. 413–420, 2001. View at Publisher · View at Google Scholar · View at Scopus
  65. F. Thevenod, J. M. Friedmann, A. D. Katsen, and I. A. Hauser, “Up-regulation of multidrug resistance P-glycoprotein via nuclear factor-kappaB activation protects kidney proximal tubule cells from cadmium- and reactive oxygen species-induced apoptosis,” The Journal of Biological Chemistry, vol. 275, no. 3, pp. 1887–1896, 2000. View at Publisher · View at Google Scholar · View at Scopus
  66. Y. Shu and H. Liu, “Reversal of P-glycoprotein-mediated multidrug resistance by cholesterol derived from low density lipoprotein in a vinblastine-resistant human lymphoblastic leukemia cell line,” Biochemistry and Cell Biology, vol. 85, no. 5, pp. 638–646, 2007. View at Publisher · View at Google Scholar · View at Scopus
  67. Y. Kimura, N. Kioka, H. Kato, M. Matsuo, and K. Ueda, “Modulation of drug-stimulated ATPase activity of human MDR1/P-glycoprotein by cholesterol,” The Biochemical Journal, vol. 401, no. 2, pp. 597–605, 2007. View at Publisher · View at Google Scholar · View at Scopus
  68. R. Cermak, “Effect of dietary flavonoids on pathways involved in drug metabolism,” Expert Opinion on Drug Metabolism & Toxicology, vol. 4, no. 1, pp. 17–35, 2008. View at Google Scholar
  69. E. J. Nelson, N. T. Zinkin, and P. M. Hinkle, “Fluorescence methods to assess multidrug resistance in individual cells,” Cancer Chemotherapy and Pharmacology, vol. 42, no. 4, pp. 292–299, 1998. View at Publisher · View at Google Scholar · View at Scopus
  70. N. J. Liptrott, M. Penny, P. G. Bray et al., “The impact of cytokines on the expression of drug transporters, cytochrome P450 enzymes and chemokine receptors in human PBMC,” British Journal of Pharmacology, vol. 156, no. 3, pp. 497–508, 2009. View at Publisher · View at Google Scholar · View at Scopus
  71. A. Kimura, Y. Ishida, T. Hayashi et al., “Interferon-gamma plays protective roles in sodium arsenite-induced renal injury by up-regulating intrarenal multidrug resistance-associated protein 1 expression,” The American Journal of Pathology, vol. 169, no. 4, pp. 1118–1128, 2006. View at Publisher · View at Google Scholar · View at Scopus
  72. S. Tsujimura, K. Saito, S. Nakayamada et al., “Transcriptional regulation of multidrug resistance-1 gene by interleukin-2 in lymphocytes,” Genes to Cells, vol. 9, no. 12, pp. 1265–1273, 2004. View at Publisher · View at Google Scholar · View at Scopus
  73. L. C. Borowski, R. P. Lopes, T. P. Gonzalez et al., “Is steroid resistance related to multidrug resistance-I (MDR-I) in rheumatoid arthritis?” International Immunopharmacology, vol. 7, no. 6, pp. 836–844, 2007. View at Publisher · View at Google Scholar · View at Scopus
  74. S. Liu, P. M. Beringer, L. Hidayat et al., “Probenecid, but not cystic fibrosis, alters the total and renal clearance of fexofenadine,” Journal of Clinical Pharmacology, vol. 48, no. 8, pp. 957–965, 2008. View at Publisher · View at Google Scholar · View at Scopus
  75. W. Malorni, M. B. Lucia, G. Rainaldi et al., “Intracellular expression of P-170 glycoprotein in peripheral blood mononuclear cell subsets from healthy donors and HIV-infected patients,” Haematologica, vol. 83, no. 1, pp. 13–20, 1998. View at Google Scholar
  76. T. Mattiello, R. Guerriero, L. V. Lotti et al., “Aspirin extrusion from human platelets through multidrug resistance protein-4-mediated transport: evidence of a reduced drug action in patients after coronary artery bypass grafting,” Journal of the American College of Cardiology, vol. 58, no. 7, pp. 752–761, 2011. View at Google Scholar
  77. G. Jedlitschky, K. Tirschmann, L. E. Lubenow et al., “The nucleotide transporter MRP4 (ABCC4) is highly expressed in human platelets and present in dense granules, indicating a role in mediator storage,” Blood, vol. 104, no. 12, pp. 3603–3610, 2004. View at Publisher · View at Google Scholar · View at Scopus
  78. I. Massimi, R. Guerriero, L. V. Lotti et al., “Aspirin influences megakaryocytic gene expression leading to up-regulation of multidrug resistance protein-4 in human platelets,” British Journal of Clinical Pharmacology, vol. 78, no. 6, pp. 1343–1353, 2014. View at Publisher · View at Google Scholar · View at Scopus
  79. A. C. Rodrigues, R. Curi, L. R. Britto et al., “Down-regulation of ABCB1 transporter by atorvastatin in a human hepatoma cell line and in human peripheral blood mononuclear cells,” Biochimica et Biophysica Acta, vol. 1760, no. 12, pp. 1866–1873, 2006. View at Google Scholar
  80. M. Egashira, N. Kawamata, K. Sugimoto, T. Kaneko, and K. Oshimi, “P-glycoprotein expression on normal and abnormally expanded natural killer cells and inhibition of P-glycoprotein function by cyclosporin A and its analogue, PSC833,” Blood, vol. 93, no. 2, pp. 599–606, 1999. View at Google Scholar
  81. R. C. Maia, K. Wagner, R. H. Cabral, and V. M. Rumjanek, “Heparin reverses rhodamine 123 extrusion by multidrug resistant cells,” Cancer Letters, vol. 106, no. 1, pp. 101–108, 1996. View at Publisher · View at Google Scholar · View at Scopus
  82. L. M. Lien, Z. C. Chen, C. L. Chung et al., “Multidrug resistance protein 4 (MRP4/ABCC4) regulates thrombus formation in vitro and in vivo,” European Journal of Pharmacology, vol. 737, pp. 159–167, 2014. View at Publisher · View at Google Scholar · View at Scopus
  83. K. Kock, M. Grube, G. Jedlitschky et al., “Expression of adenosine triphosphate-binding cassette (ABC) drug transporters in peripheral blood cells: relevance for physiology and pharmacotherapy,” Clinical Pharmacokinetics, vol. 46, no. 6, pp. 449–470, 2007. View at Publisher · View at Google Scholar · View at Scopus
  84. A. Borgognone and F. M. Pulcinelli, “Reduction of cAMP and cGMP inhibitory effects in human platelets by MRP4-mediated transport,” Thrombosis and Haemostasis, vol. 108, no. 5, pp. 955–962, 2012. View at Publisher · View at Google Scholar · View at Scopus
  85. S. B. Cheepala, A. Pitre, Y. Fukuda et al., “The ABCC4 membrane transporter modulates platelet aggregation,” Blood, vol. 126, no. 20, pp. 2307–2319, 2015. View at Publisher · View at Google Scholar · View at Scopus
  86. M. Sjolinder, S. Tornhamre, H. E. Claesson, J. Hydman, and J. Lindgren, “Characterization of a leukotriene C4 export mechanism in human platelets: possible involvement of multidrug resistance-associated protein 1,” Journal of Lipid Research, vol. 40, no. 3, pp. 439–446, 1999. View at Google Scholar
  87. M. Rius, J. Hummel-Eisenbeiss, and D. Keppler, “ATP-dependent transport of leukotrienes B4 and C4 by the multidrug resistance protein ABCC4 (MRP4),” The Journal of Pharmacology and Experimental Therapeutics, vol. 324, no. 1, pp. 86–94, 2008. View at Publisher · View at Google Scholar · View at Scopus
  88. D. P. Olson, B. J. Taylor, and S. P. Ivy, “Detection of MRP functional activity: calcein AM but not BCECF AM as a multidrug resistance-related protein (MRP1) substrate,” Cytometry, vol. 46, no. 2, pp. 105–113, 2001. View at Publisher · View at Google Scholar · View at Scopus
  89. J. Wang, X. Yi, M. Liu et al., “Correlation between the in vitro functionality of stored platelets and the cytosolic esterase-induced fluorescence intensity with CMFDA,” PLoS One, vol. 10, no. 9, article e0138509, 2015. View at Publisher · View at Google Scholar · View at Scopus
  90. H. Schoenfeld, M. Muhm, U. Doepfmer, A. Exadaktylos, and H. Radtke, “Platelet activity in washed platelet concentrates,” Anesthesia and Analgesia, vol. 99, no. 1, pp. 17–20, 2004. View at Publisher · View at Google Scholar
  91. F. M. Tamimi, S. Montalvo, I. Tresguerres, and L. Blanco Jerez, “A comparative study of 2 methods for obtaining platelet-rich plasma,” Journal of Oral and Maxillofacial Surgery, vol. 65, no. 6, pp. 1084–1093, 2007. View at Publisher · View at Google Scholar · View at Scopus
  92. E. Cecerska-Heryc, A. Jesionowska, S. Klaudyna et al., “Xanthine oxidoreductase reference values in platelet-poor plasma and platelets in healthy volunteers,” Oxidative Medicine and Cellular Longevity, vol. 2015, Article ID 341926, 6 pages, 2015. View at Publisher · View at Google Scholar · View at Scopus
  93. M. H. Ginsberg, F. Kozin, M. O'Malley, and D. J. McCarty, “Release of platelet constituents by monosodium urate crystals,” The Journal of Clinical Investigation, vol. 60, no. 5, pp. 999–1007, 1977. View at Publisher · View at Google Scholar
  94. M. Ginsberg, P. Henson, J. Henson, and F. Kozin, “Mechanisms of platelet response to monosodium urate crystals,” The American Journal of Pathology, vol. 94, no. 3, pp. 549–568, 1979. View at Google Scholar
  95. J. F. Mustard, E. A. Murphy, M. A. Ogryzlo, and H. A. Smythe, “Blood Coagulation and platelet economy in subjects with primary gout,” Canadian Medical Association Journal, vol. 89, pp. 1207–1211, 1963. View at Google Scholar
  96. M. Li, Z. Wang, T. Ma et al., “Enhanced platelet apoptosis in chronic uremic patients,” Renal Failure, vol. 36, no. 6, pp. 847–853, 2014. View at Publisher · View at Google Scholar · View at Scopus
  97. Y. Chen, Y. Xiao, Z. Lin et al., “The role of circulating platelets microparticles and platelet parameters in acute ischemic stroke patients,” Journal of Stroke and Cerebrovascular Diseases, vol. 24, no. 10, pp. 2313–2320, 2015. View at Publisher · View at Google Scholar · View at Scopus
  98. M. George, M. R. Ganesh, A. Sridhar et al., “Evaluation of endothelial and platelet derived Microparticles in patients with acute coronary syndrome,” Journal of Clinical and Diagnostic Research, vol. 9, no. 12, pp. OC09–OC13, 2015. View at Publisher · View at Google Scholar · View at Scopus
  99. G. Giannopoulos, G. Oudatzis, G. Paterakis et al., “Red blood cell and platelet microparticles in myocardial infarction patients treated with primary angioplasty,” International Journal of Cardiology, vol. 176, no. 1, pp. 145–150, 2014. View at Publisher · View at Google Scholar · View at Scopus
  100. R. Suades, T. Padro, R. Alonso, P. Mata, and L. Badimon, “Lipid-lowering therapy with statins reduces microparticle shedding from endothelium, platelets and inflammatory cells,” Thrombosis and Haemostasis, vol. 110, no. 2, pp. 366–377, 2013. View at Publisher · View at Google Scholar · View at Scopus
  101. O. Helal, C. Defoort, S. Robert et al., “Increased levels of microparticles originating from endothelial cells, platelets and erythrocytes in subjects with metabolic syndrome: relationship with oxidative stress,” Nutrition, Metabolism, and Cardiovascular Diseases, vol. 21, no. 9, pp. 665–671, 2011. View at Publisher · View at Google Scholar · View at Scopus
  102. T. Nishizawa, T. Taniura, and S. Nomura, “Effects of febuxostat on platelet-derived microparticles and adiponectin in patients with hyperuricemia,” Blood Coagulation & Fibrinolysis, vol. 26, no. 8, pp. 887–892, 2015. View at Publisher · View at Google Scholar · View at Scopus
  103. S. Robert, P. Poncelet, R. Lacroix et al., “Standardization of platelet-derived microparticle counting using calibrated beads and a Cytomics FC500 routine flow cytometer: a first step towards multicenter studies?” Journal of Thrombosis and Haemostasis, vol. 7, no. 1, pp. 190–197, 2009. View at Publisher · View at Google Scholar · View at Scopus
  104. A. Larsson, T. Lundahl, M. Eriksson, K. Lundkvist, and T. Lindahl, “Endotoxin induced platelet microvesicle formation measured by flow cytometry,” Platelets, vol. 7, no. 3, pp. 153–158, 1996. View at Google Scholar
  105. C. Vors, G. Pineau, J. Drai et al., “Postprandial endotoxemia linked with chylomicrons and lipopolysaccharides handling in obese versus lean men: a lipid dose-effect trial,” The Journal of Clinical Endocrinology and Metabolism, vol. 100, no. 9, pp. 3427–3435, 2015. View at Publisher · View at Google Scholar · View at Scopus
  106. M. I. Lassenius, K. H. Pietilainen, K. Kaartinen et al., “Bacterial endotoxin activity in human serum is associated with dyslipidemia, insulin resistance, obesity, and chronic inflammation,” Diabetes Care, vol. 34, no. 8, pp. 1809–1815, 2011. View at Publisher · View at Google Scholar · View at Scopus
  107. Z. Huang and V. B. Kraus, “Does lipopolysaccharide-mediated inflammation have a role in OA?” Nature Reviews. Rheumatology, vol. 12, no. 2, pp. 123–129, 2016. View at Publisher · View at Google Scholar · View at Scopus
  108. S. Araki, H. Matsuno, M. Haneda et al., “Correlation between albuminuria and spontaneous platelet microaggregate formation in type 2 diabetic patients,” Diabetes Care, vol. 32, no. 11, pp. 2062–2067, 2009. View at Publisher · View at Google Scholar · View at Scopus
  109. S. Suzuki, H. Kudo, and T. Koyama, “Assessment of spontaneous platelet aggregation using laser light scattering in healthy subjects: an attempt to standardize,” International Journal of Laboratory Hematology, vol. 36, no. 6, pp. 676–685, 2014. View at Publisher · View at Google Scholar · View at Scopus
  110. L. Ayers, M. Kohler, P. Harrison et al., “Measurement of circulating cell-derived microparticles by flow cytometry: sources of variability within the assay,” Thrombosis Research, vol. 127, no. 4, pp. 370–377, 2011. View at Publisher · View at Google Scholar · View at Scopus
  111. S. Zeng, X. Zhou, L. Ge et al., “Monocyte subsets and monocyte-platelet aggregates in patients with unstable angina,” Journal of Thrombosis and Thrombolysis, vol. 38, no. 4, pp. 439–446, 2014. View at Publisher · View at Google Scholar · View at Scopus
  112. T. Ishikawa, M. Shimizu, S. Kohara, S. Takizawa, Y. Kitagawa, and S. Takagi, “Appearance of WBC-platelet complex in acute ischemic stroke, predominantly in atherothrombotic infarction,” Journal of Atherosclerosis and Thrombosis, vol. 19, no. 5, pp. 494–501, 2012. View at Publisher · View at Google Scholar · View at Scopus
  113. B. Majumder, J. North, C. Mavroudis, R. Rakhit, and M. W. Lowdell, “Improved accuracy and reproducibility of enumeration of platelet-monocyte complexes through use of doublet-discriminator strategy,” Cytometry. Part B, Clinical Cytometry, vol. 82, no. 6, pp. 353–359, 2012. View at Publisher · View at Google Scholar · View at Scopus
  114. A. Burdess, A. E. Michelsen, F. Brosstad, K. A. Fox, D. E. Newby, and A. F. Nimmo, “Platelet activation in patients with peripheral vascular disease: reproducibility and comparability of platelet markers,” Thrombosis Research, vol. 129, no. 1, pp. 50–55, 2012. View at Publisher · View at Google Scholar · View at Scopus
  115. H. S. Leong, T. J. Podor, B. Manocha, and J. D. Lewis, “Validation of flow cytometric detection of platelet microparticles and liposomes by atomic force microscopy,” Journal of Thrombosis and Haemostasis, vol. 9, no. 12, pp. 2466–2476, 2011. View at Publisher · View at Google Scholar · View at Scopus
  116. W. Jy, L. L. Horstman, H. Park, W. W. Mao, P. Valant, and Y. S. Ahn, “Platelet aggregates as markers of platelet activation: characterization of flow cytometric method suitable for clinical applications,” American Journal of Hematology, vol. 57, no. 1, pp. 33–42, 1998. View at Publisher · View at Google Scholar
  117. S. Hartz, B. Menart, and D. Tschoepe, “Leukocyte apoptosis in whole blood involves platelet-dependent coaggregation,” Cytometry. Part a, vol. 52, no. 2, pp. 117–121, 2003. View at Publisher · View at Google Scholar
  118. I. A. Hagberg and T. Lyberg, “Evaluation of circulating platelet-leukocyte conjugates: a sensitive flow cytometric assay well suited for clinical studies,” Platelets, vol. 11, no. 3, pp. 151–160, 2000. View at Google Scholar
  119. B. Izzi, A. Pampuch, S. Costanzo et al., “Determinants of platelet conjugate formation with polymorphonuclear leukocytes or monocytes in whole blood,” Thrombosis and Haemostasis, vol. 98, no. 6, pp. 1276–1284, 2007. View at Google Scholar
  120. S. J. Vowells, S. Sekhsaria, H. L. Malech, M. Shalit, and T. A. Fleisher, “Flow cytometric analysis of the granulocyte respiratory burst: a comparison study of fluorescent probes,” Journal of Immunological Methods, vol. 178, no. 1, pp. 89–97, 1995. View at Publisher · View at Google Scholar
  121. L. Kobzik, J. J. Godleski, and J. D. Brain, “Oxidative metabolism in the alveolar macrophage: analysis by flow cytometry,” Journal of Leukocyte Biology, vol. 47, no. 4, pp. 295–303, 1990. View at Google Scholar
  122. N. Carrim, J. F. Arthur, J. R. Hamilton et al., “Thrombin-induced reactive oxygen species generation in platelets: a novel role for protease-activated receptor 4 and GPIbalpha,” Redox Biology, vol. 6, pp. 640–647, 2015. View at Publisher · View at Google Scholar · View at Scopus
  123. R. Carnevale, L. Loffredo, C. Nocella et al., “Epicatechin and catechin modulate endothelial activation induced by platelets of patients with peripheral artery disease,” Oxidative Medicine and Cellular Longevity, vol. 2014, Article ID 691015, 9 pages, 2014. View at Publisher · View at Google Scholar · View at Scopus
  124. F. Li, M. Yang, L. Wang et al., “Autofluorescence contributes to false-positive intracellular Foxp3 staining in macrophages: a lesson learned from flow cytometry,” Journal of Immunological Methods, vol. 386, no. 1-2, pp. 101–107, 2012. View at Publisher · View at Google Scholar · View at Scopus
  125. Z. Huczek, K. J. Filipiak, J. Kochman et al., “Baseline platelet size is increased in patients with acute coronary syndromes developing early stent thrombosis and predicts future residual platelet reactivity. A case-control study,” Thrombosis Research, vol. 125, no. 5, pp. 406–412, 2010. View at Publisher · View at Google Scholar · View at Scopus
  126. G. De Luca, M. Verdoia, E. Cassetti et al., “Mean platelet volume is not associated with platelet reactivity and the extent of coronary artery disease in diabetic patients,” Blood Coagulation & Fibrinolysis, vol. 24, no. 6, pp. 619–624, 2013. View at Publisher · View at Google Scholar · View at Scopus
  127. D. I. Won, D. H. Yang, D. H. Kim, S. C. Chae, and J. S. Suh, “Flow cytometric assessment of platelet aspirin resistance using light scattering,” Cytometry. Part B, Clinical Cytometry, vol. 74, no. 2, pp. 110–117, 2008. View at Publisher · View at Google Scholar · View at Scopus
  128. M. Frojmovic and T. Wong, “Dynamic measurements of the platelet membrane glycoprotein IIb-IIIa receptor for fibrinogen by flow cytometry. II. Platelet size-dependent subpopulations,” Biophysical Journal, vol. 59, no. 4, pp. 828–837, 1991. View at Publisher · View at Google Scholar
  129. S. Knasmuller, A. Nersesyan, M. Misik et al., “Use of conventional and -omics based methods for health claims of dietary antioxidants: a critical overview,” The British Journal of Nutrition, vol. 99, E Supplement 1, pp. ES3–E52, 2008. View at Google Scholar
  130. J. K. Juranek, G. K. Daffu, J. Wojtkiewicz, D. Lacomis, J. Kofler, and A. M. Schmidt, “Receptor for advanced glycation end products and its inflammatory ligands are upregulated in amyotrophic lateral sclerosis,” Frontiers in Cellular Neuroscience, vol. 9, p. 485, 2015. View at Publisher · View at Google Scholar · View at Scopus
  131. I. Ozbay, C. Kucur, F. E. Kocak, B. Savran, and F. Oghan, “Advanced oxidation protein product levels as a marker of oxidative stress in paediatric patients with chronic tonsillitis,” Acta Otorhinolaryngologica Italica, vol. 36, no. 5, pp. 381–385, 2016. View at Publisher · View at Google Scholar · View at Scopus
  132. M. Mateu-Jimenez, A. Sanchez-Font, A. Rodriguez-Fuster et al., “Redox imbalance in lung cancer of patients with underlying chronic respiratory conditions,” Molecular Medicine, vol. 22, 2016. View at Publisher · View at Google Scholar · View at Scopus
  133. G. A. Asare, G. Akuffo, D. Doku, B. Asiedu, and S. Santa, “Dynamics of urinary oxidative stress biomarkers: 8-hydroxy-2′-deoxyguanosine and 8-isoprostane in uterine leiomyomas,” Journal of Mid-Life Health, vol. 7, no. 1, pp. 8–14, 2016. View at Publisher · View at Google Scholar
  134. A. Suehiro, K. Uchida, M. Nakanishi, and I. Wakabayashi, “Measurement of urinary advanced glycation end-products (AGEs) using a fluorescence assay for metabolic syndrome-related screening tests,” Diabetes and Metabolic Syndrome: Clinical Research and Reviews, vol. 10, no. 1 Supplement 1, pp. S110–S113, 2016. View at Google Scholar
  135. N. Turk, A. Mornar, V. Mrzljak, and Z. Turk, “Urinary excretion of advanced glycation endproducts in patients with type 2 diabetes and various stages of proteinuria,” Diabetes & Metabolism, vol. 30, no. 2, pp. 187–192, 2004. View at Publisher · View at Google Scholar
  136. J. Kaur, C. Politis, and R. Jacobs, “Salivary 8-hydroxy-2-deoxyguanosine, malondialdehyde, vitamin C, and vitamin E in oral pre-cancer and cancer: diagnostic value and free radical mechanism of action,” Clinical Oral Investigations, vol. 20, no. 2, pp. 315–319, 2016. View at Publisher · View at Google Scholar · View at Scopus
  137. K. Smriti, K. M. Pai, V. Ravindranath, and K. C. Pentapati, “Role of salivary malondialdehyde in assessment of oxidative stress among diabetics,” Journal of Oral Biology and Craniofacial Research, vol. 6, no. 1, pp. 41–44, 2016. View at Publisher · View at Google Scholar · View at Scopus
  138. B. Antus, “Oxidative stress markers in sputum,” Oxidative Medicine and Cellular Longevity, vol. 2016, Article ID 2930434, 12 pages, 2016. View at Publisher · View at Google Scholar · View at Scopus
  139. Z. Yildirim, B. Bozkurt, D. Ozol et al., “Increased exhaled 8-isoprostane and interleukin-6 in patients with Helicobacter pylori infection,” Helicobacter, vol. 21, no. 5, pp. 389–394, 2016. View at Publisher · View at Google Scholar · View at Scopus
  140. E. M. Schumer, M. C. Black, M. Bousamra 2nd et al., “Normalization of exhaled carbonyl compounds after lung cancer resection,” The Annals of Thoracic Surgery, vol. 102, no. 4, pp. 1095–1100, 2016. View at Publisher · View at Google Scholar · View at Scopus
  141. E. M. Schumer, J. R. Trivedi, V. van Berkel et al., “High sensitivity for lung cancer detection using analysis of exhaled carbonyl compounds,” The Journal of Thoracic and Cardiovascular Surgery, vol. 150, no. 6, pp. 1517–1522, 2015, discussion 1522-4. View at Publisher · View at Google Scholar · View at Scopus
  142. B. C. Sousa, A. R. Pitt, and C. M. Spickett, “Chemistry and analysis of HNE and other prominent carbonyl-containing lipid oxidation compounds,” Free Radical Biology & Medicine, 2017, Epub ahead of print. View at Publisher · View at Google Scholar
  143. C. Goldring, A. F. Casini, E. Maellaro, B. Del Bello, and M. Comporti, “Determination of 4-hydroxynonenal by high-performance liquid chromatography with electrochemical detection,” Lipids, vol. 28, no. 2, pp. 141–145, 1993. View at Publisher · View at Google Scholar · View at Scopus
  144. S. Zelzer, H. Mangge, R. Oberreither et al., “Oxidative stress: determination of 4-hydroxy-2-nonenal by gas chromatography/mass spectrometry in human and rat plasma,” Free Radical Research, vol. 49, no. 10, pp. 1233–1238, 2015. View at Publisher · View at Google Scholar · View at Scopus
  145. W. Luczaj, E. Gindzienska-Sieskiewicz, I. Jarocka-Karpowicz et al., “The onset of lipid peroxidation in rheumatoid arthritis: consequences and monitoring,” Free Radical Research, vol. 50, no. 3, pp. 304–313, 2016. View at Publisher · View at Google Scholar · View at Scopus
  146. P. M. Abuja and R. Albertini, “Methods for monitoring oxidative stress, lipid peroxidation and oxidation resistance of lipoproteins,” Clinica Chimica Acta, vol. 306, no. 1-2, pp. 1–17, 2001. View at Publisher · View at Google Scholar · View at Scopus
  147. D. Del Rio, A. J. Stewart, and N. Pellegrini, “A review of recent studies on malondialdehyde as toxic molecule and biological marker of oxidative stress,” Nutrition, Metabolism, and Cardiovascular Diseases, vol. 15, no. 4, pp. 316–328, 2005. View at Publisher · View at Google Scholar · View at Scopus
  148. J. A. Knight, R. K. Pieper, and L. McClellan, “Specificity of the thiobarbituric acid reaction: its use in studies of lipid peroxidation,” Clinical Chemistry, vol. 34, no. 12, pp. 2433–2438, 1988. View at Google Scholar
  149. A. M. Domijan, J. Ralic, S. Radic Brkanac, L. Rumora, and T. Zanic-Grubisic, “Quantification of malondialdehyde by HPLC-FL - application to various biological samples,” Biomedical Chromatography, vol. 29, no. 1, pp. 41–46, 2015. View at Publisher · View at Google Scholar · View at Scopus
  150. D. Grotto, L. D. Santa Maria, S. Boeira et al., “Rapid quantification of malondialdehyde in plasma by high performance liquid chromatography-visible detection,” Journal of Pharmaceutical and Biomedical Analysis, vol. 43, no. 2, pp. 619–624, 2007. View at Publisher · View at Google Scholar · View at Scopus
  151. A. S. Sim, C. Salonikas, D. Naidoo, and D. E. Wilcken, “Improved method for plasma malondialdehyde measurement by high-performance liquid chromatography using methyl malondialdehyde as an internal standard,” Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences, vol. 785, no. 2, pp. 337–344, 2003. View at Google Scholar
  152. K. Natarajan, G. D. Mathialagan, S. Raghavan, and N. Shanmugam, “The advanced Lipoxidation end product precursor malondialdehyde induces IL-17E expression and skews lymphocytes to the th17 subset,” Cellular & Molecular Biology Letters, vol. 20, no. 4, pp. 647–662, 2015. View at Publisher · View at Google Scholar · View at Scopus
  153. A. Ueno, A. Ghosh, D. Hung, J. Li, and H. Jijon, “Th17 plasticity and its changes associated with inflammatory bowel disease,” World Journal of Gastroenterology, vol. 21, no. 43, pp. 12283–12295, 2015. View at Publisher · View at Google Scholar · View at Scopus
  154. U. Dreissigacker, M. T. Suchy, N. Maassen, and D. Tsikas, “Human plasma concentrations of malondialdehyde (MDA) and the F2-isoprostane 15(S)-8-iso-PGF(2alpha) may be markedly compromised by hemolysis: evidence by GC-MS/MS and potential analytical and biological ramifications,” Clinical Biochemistry, vol. 43, no. 1-2, pp. 159–167, 2010. View at Publisher · View at Google Scholar · View at Scopus
  155. J. Proudfoot, A. Barden, T. A. Mori et al., “Measurement of urinary F(2)-isoprostanes as markers of in vivo lipid peroxidation-a comparison of enzyme immunoassay with gas chromatography/mass spectrometry,” Analytical Biochemistry, vol. 272, no. 2, pp. 209–215, 1999. View at Publisher · View at Google Scholar · View at Scopus
  156. K. A. Smith, J. Shepherd, A. Wakil, and E. S. Kilpatrick, “A comparison of methods for the measurement of 8-isoPGF(2alpha): a marker of oxidative stress,” Annals of Clinical Biochemistry, vol. 48, no. Pt 2, pp. 147–154, 2011. View at Publisher · View at Google Scholar · View at Scopus
  157. D. Il'yasova, J. D. Morrow, A. Ivanova, and L. E. Wagenknecht, “Epidemiological marker for oxidant status: comparison of the ELISA and the gas chromatography/mass spectrometry assay for urine 2,3-dinor-5,6-dihydro-15-F2t-isoprostane,” Annals of Epidemiology, vol. 14, no. 10, pp. 793–797, 2004. View at Publisher · View at Google Scholar · View at Scopus
  158. M. A. Lam, G. J. Maghzal, M. Khademi et al., “Absence of systemic oxidative stress and increased CSF prostaglandin F2alpha in progressive MS,” Neurology® Neuroimmunology & Neuroinflammation, vol. 3, no. 4, p. e256, 2016. View at Publisher · View at Google Scholar
  159. N. Wang, R. Dai, W. Wang, Y. Peng, X. Zhao, and K. Bi, “Simultaneous profiling of eicosanoid metabolome in plasma by UPLC-MS/MS method: application to identify potential makers for rheumatoid arthritis,” Talanta, vol. 161, pp. 157–164, 2016. View at Publisher · View at Google Scholar · View at Scopus
  160. N. Wang, X. Zhao, W. Wang, Y. Peng, K. Bi, and R. Dai, “Targeted profiling of arachidonic acid and eicosanoids in rat tissue by UFLC-MS/MS: application to identify potential markers for rheumatoid arthritis,” Talanta, vol. 162, pp. 479–487, 2017. View at Publisher · View at Google Scholar
  161. H. Wiseman and B. Halliwell, “Damage to DNA by reactive oxygen and nitrogen species: role in inflammatory disease and progression to cancer,” The Biochemical Journal, vol. 313, Part 1, pp. 17–29, 1996. View at Publisher · View at Google Scholar
  162. M. Dizdaroglu, P. Jaruga, M. Birincioglu, and H. Rodriguez, “Free radical-induced damage to DNA: mechanisms and measurement,” Free Radical Biology & Medicine, vol. 32, no. 11, pp. 1102–1115, 2002. View at Publisher · View at Google Scholar · View at Scopus
  163. J. Cadet, T. Douki, D. Gasparutto, and J. L. Ravanat, “Oxidative damage to DNA: formation, measurement and biochemical features,” Mutation Research, vol. 531, no. 1-2, pp. 5–23, 2003. View at Google Scholar
  164. A. M. Knaapen, N. Gungor, R. P. Schins, P. J. Borm, and F. J. Van Schooten, “Neutrophils and respiratory tract DNA damage and mutagenesis: a review,” Mutagenesis, vol. 21, no. 4, pp. 225–236, 2006. View at Publisher · View at Google Scholar · View at Scopus
  165. H. Li, S. Cui, S. Wang et al., “Ultrasensitive UPLC-MS/MS method for analysis of etheno-DNA adducts in human white blood cells,” Free Radical Research, vol. 49, no. 9, pp. 1049–1054, 2015. View at Publisher · View at Google Scholar · View at Scopus
  166. H. Bartsch and J. Nair, “Accumulation of lipid peroxidation-derived DNA lesions: potential lead markers for chemoprevention of inflammation-driven malignancies,” Mutation Research, vol. 591, no. 1-2, pp. 34–44, 2005. View at Google Scholar
  167. J. Nair, F. Gansauge, H. Beger, P. Dolara, G. Winde, and H. Bartsch, “Increased etheno-DNA adducts in affected tissues of patients suffering from Crohn's disease, ulcerative colitis, and chronic pancreatitis,” Antioxidants & Redox Signaling, vol. 8, no. 5-6, pp. 1003–1010, 2006. View at Publisher · View at Google Scholar · View at Scopus
  168. P. Bin, M. Shen, H. Li et al., “Increased levels of urinary biomarkers of lipid peroxidation products among workers occupationally exposed to diesel engine exhaust,” Free Radical Research, vol. 50, no. 8, pp. 820–830, 2016. View at Publisher · View at Google Scholar · View at Scopus
  169. S. Cui, H. Li, S. Wang et al., “Ultrasensitive UPLC-MS-MS method for the quantitation of etheno-DNA adducts in human urine,” International Journal of Environmental Research and Public Health, vol. 11, no. 10, pp. 10902–10914, 2014. View at Publisher · View at Google Scholar · View at Scopus
  170. J. Cadet and J. R. Wagner, “Oxidatively generated base damage to cellular DNA by hydroxyl radical and one-electron oxidants: similarities and differences,” Archives of Biochemistry and Biophysics, vol. 557, pp. 47–54, 2014. View at Publisher · View at Google Scholar · View at Scopus
  171. M. Dizdaroglu and P. Jaruga, “Mechanisms of free radical-induced damage to DNA,” Free Radical Research, vol. 46, no. 4, pp. 382–419, 2012. View at Publisher · View at Google Scholar · View at Scopus
  172. J. L. Ravanat, J. Cadet, and T. Douki, “Oxidatively generated DNA lesions as potential biomarkers of in vivo oxidative stress,” Current Molecular Medicine, vol. 12, no. 6, pp. 655–671, 2012. View at Publisher · View at Google Scholar · View at Scopus
  173. C. M. Gedik, A. Collins, and Escodd, “Establishing the background level of base oxidation in human lymphocyte DNA: results of an interlaboratory validation study,” The FASEB Journal, vol. 19, no. 1, pp. 82–84, 2005. View at Publisher · View at Google Scholar · View at Scopus
  174. European Standards Committee on Urinary Lesion, AM. D. Evans, R. Olinski, S. Loft, and M. S. Cooke, “Toward consensus in the analysis of urinary 8-oxo-7,8-dihydro-2′-deoxyguanosine as a noninvasive biomarker of oxidative stress,” The FASEB Journal, vol. 24, no. 4, pp. 1249–1260, 2010. View at Publisher · View at Google Scholar · View at Scopus
  175. M. S. Cooke, R. Olinski, S. Loft, and A. European Standards, “Committee on urinary lesion, measurement and meaning of oxidatively modified DNA lesions in urine,” Cancer Epidemiology, Biomarkers & Prevention, vol. 17, no. 1, pp. 3–14, 2008. View at Publisher · View at Google Scholar · View at Scopus
  176. H. Sova, A. Jukkola-Vuorinen, U. Puistola, S. Kauppila, and P. Karihtala, “8-Hydroxydeoxyguanosine: a new potential independent prognostic factor in breast cancer,” British Journal of Cancer, vol. 102, no. 6, pp. 1018–1023, 2010. View at Publisher · View at Google Scholar · View at Scopus
  177. S. Loft, P. Svoboda, H. Kasai et al., “Prospective study of 8-oxo-7,8-dihydro-2′-deoxyguanosine excretion and the risk of lung cancer,” Carcinogenesis, vol. 27, no. 6, pp. 1245–1250, 2006. View at Publisher · View at Google Scholar · View at Scopus
  178. L. L. Wu, C. C. Chiou, P. Y. Chang, and J. T. Wu, “Urinary 8-OHdG: a marker of oxidative stress to DNA and a risk factor for cancer, atherosclerosis and diabetics,” Clinica Chimica Acta, vol. 339, no. 1-2, pp. 1–9, 2004. View at Publisher · View at Google Scholar · View at Scopus
  179. M. Kant, M. Akis, M. Calan et al., “Elevated urinary levels of 8-oxo-2′-deoxyguanosine, (5'R)- and (5′S)-8,5′-cyclo-2′-deoxyadenosines, and 8-iso-prostaglandin F2alpha as potential biomarkers of oxidative stress in patients with prediabetes,” DNA Repair (Amst), vol. 48, pp. 1–7, 2016. View at Publisher · View at Google Scholar · View at Scopus
  180. K. Broedbaek, V. Siersma, T. Henriksen et al., “Urinary markers of nucleic acid oxidation and cancer in type 2 diabetes,” Redox Biology, vol. 4, pp. 34–39, 2015. View at Publisher · View at Google Scholar · View at Scopus
  181. E. R. Stadtman, “Protein oxidation and aging,” Free Radical Research, vol. 40, no. 12, pp. 1250–1258, 2006. View at Google Scholar
  182. M. J. Davies, “Protein oxidation and peroxidation,” The Biochemical Journal, vol. 473, no. 7, pp. 805–825, 2016. View at Publisher · View at Google Scholar · View at Scopus
  183. C. Ott and T. Grune, “Protein oxidation and proteolytic signalling in aging,” Current Pharmaceutical Design, vol. 20, no. 18, pp. 3040–3051, 2014. View at Publisher · View at Google Scholar · View at Scopus
  184. A. Hohn, T. Jung, and T. Grune, “Pathophysiological importance of aggregated damaged proteins,” Free Radical Biology & Medicine, vol. 71, pp. 70–89, 2014. View at Publisher · View at Google Scholar · View at Scopus
  185. E. R. Stadtman, “Oxidation of proteins by mixed-function oxidation systems: implication in protein turnover, aging and neutrophil function,” Trends in Biochemical Sciences, vol. 11, no. 1, pp. 11-12, 1986. View at Publisher · View at Google Scholar · View at Scopus
  186. B. S. Berlett and E. R. Stadtman, “Protein oxidation in aging, disease, and oxidative stress,” The Journal of Biological Chemistry, vol. 272, no. 33, pp. 20313–20316, 1997. View at Publisher · View at Google Scholar · View at Scopus
  187. J. C. Monboisse and J. P. Borel, “Oxidative damage to collagen,” EXS, vol. 62, pp. 323–327, 1992. View at Google Scholar
  188. V. Vanhooren, A. Navarrete Santos, K. Voutetakis et al., “Protein modification and maintenance systems as biomarkers of ageing,” Mechanisms of Ageing and Development, vol. 151, pp. 71–84, 2015. View at Publisher · View at Google Scholar · View at Scopus
  189. D. A. Butterfield, L. Gu, F. Di Domenico, and R. A. Robinson, “Mass spectrometry and redox proteomics: applications in disease,” Mass Spectrometry Reviews, vol. 33, no. 4, pp. 277–301, 2014. View at Publisher · View at Google Scholar · View at Scopus
  190. A. Hohn, J. Konig, and T. Grune, “Protein oxidation in aging and the removal of oxidized proteins,” Journal of Proteomics, vol. 92, pp. 132–159, 2013. View at Publisher · View at Google Scholar · View at Scopus
  191. N. Breusing and T. Grune, “Biomarkers of protein oxidation from a chemical, biological and medical point of view,” Experimental Gerontology, vol. 45, no. 10, pp. 733–737, 2010. View at Publisher · View at Google Scholar · View at Scopus
  192. C. L. Hawkins, P. E. Morgan, and M. J. Davies, “Quantification of protein modification by oxidants,” Free Radical Biology & Medicine, vol. 46, no. 8, pp. 965–988, 2009. View at Publisher · View at Google Scholar · View at Scopus
  193. E. R. Stadtman and R. L. Levine, “Free radical-mediated oxidation of free amino acids and amino acid residues in proteins,” Amino Acids, vol. 25, no. 3-4, pp. 207–218, 2003. View at Publisher · View at Google Scholar · View at Scopus
  194. M. Chevion, E. Berenshtein, and E. R. Stadtman, “Human studies related to protein oxidation: protein carbonyl content as a marker of damage,” Free Radical Research, Supplement 33, pp. S99–108, 2000. View at Google Scholar
  195. L. Gil, W. Siems, B. Mazurek et al., “Age-associated analysis of oxidative stress parameters in human plasma and erythrocytes,” Free Radical Research, vol. 40, no. 5, pp. 495–505, 2006. View at Google Scholar
  196. R. Sultana, M. Perluigi, and D. A. Butterfield, “Protein oxidation and lipid peroxidation in brain of subjects with Alzheimer’s disease: insights into mechanism of neurodegeneration from redox proteomics,” Antioxidants & Redox Signaling, vol. 8, no. 11-12, pp. 2021–2037, 2006. View at Publisher · View at Google Scholar
  197. A. Z. Reznick and L. Packer, “Oxidative damage to proteins: spectrophotometric method for carbonyl assay,” Methods in Enzymology, vol. 233, pp. 357–363, 1994. View at Google Scholar
  198. R. L. Levine, J. A. Williams, E. R. Stadtman, and E. Shacter, “Carbonyl assays for determination of oxidatively modified proteins,” Methods in Enzymology, vol. 233, pp. 346–357, 1994. View at Google Scholar
  199. H. Buss, T. P. Chan, K. B. Sluis, N. M. Domigan, and C. C. Winterbourn, “Protein carbonyl measurement by a sensitive ELISA method,” Free Radical Biology & Medicine, vol. 23, no. 3, pp. 361–366, 1997. View at Publisher · View at Google Scholar · View at Scopus
  200. C. Delgado-Andrade, “Carboxymethyl-lysine: thirty years of investigation in the field of AGE formation,” Food & Function, vol. 7, no. 1, pp. 46–57, 2016. View at Publisher · View at Google Scholar · View at Scopus
  201. G. Vistoli, D. De Maddis, A. Cipak, N. Zarkovic, M. Carini, and G. Aldini, “Advanced glycoxidation and lipoxidation end products (AGEs and ALEs): an overview of their mechanisms of formation,” Free Radical Research, vol. 47, Supplement 1, pp. 3–27, 2013. View at Publisher · View at Google Scholar · View at Scopus
  202. P. A. Grimsrud, H. Xie, T. J. Griffin, and D. A. Bernlohr, “Oxidative stress and covalent modification of protein with bioactive aldehydes,” The Journal of Biological Chemistry, vol. 283, no. 32, pp. 21837–21841, 2008. View at Publisher · View at Google Scholar · View at Scopus
  203. M. Perluigi, R. Coccia, and D. A. Butterfield, “4-Hydroxy-2-nonenal, a reactive product of lipid peroxidation, and neurodegenerative diseases: a toxic combination illuminated by redox proteomics studies,” Antioxidants & Redox Signaling, vol. 17, no. 11, pp. 1590–1609, 2012. View at Publisher · View at Google Scholar · View at Scopus
  204. J. Anguizola, R. Matsuda, O. S. Barnaby et al., “Review: glycation of human serum albumin,” Clinica Chimica Acta, vol. 425, pp. 64–76, 2013. View at Publisher · View at Google Scholar · View at Scopus
  205. V. M. Monnier and D. R. Sell, “Prevention and repair of protein damage by the Maillard reaction in vivo,” Rejuvenation Research, vol. 9, no. 2, pp. 264–273, 2006. View at Publisher · View at Google Scholar · View at Scopus
  206. M. X. Fu, J. R. Requena, A. J. Jenkins, T. J. Lyons, J. W. Baynes, and S. R. Thorpe, “The advanced glycation end product, Nepsilon-(carboxymethyl)lysine, is a product of both lipid peroxidation and glycoxidation reactions,” The Journal of Biological Chemistry, vol. 271, no. 17, pp. 9982–9986, 1996. View at Google Scholar
  207. S. J. Loomis, Y. Chen, D. B. Sacks et al., “Cross-sectional analysis of AGE-CML, sRAGE, and esRAGE with diabetes and Cardiometabolic risk factors in a community-based cohort,” Clinical Chemistry, vol. 63, no. 5, pp. 980–989, 2017. View at Publisher · View at Google Scholar
  208. E. Sanchez, A. Betriu, D. Arroyo et al., “Skin autofluorescence and subclinical atherosclerosis in mild to moderate chronic kidney disease: a case-control study,” PloS One, vol. 12, no. 1, article e0170778, 2017. View at Publisher · View at Google Scholar
  209. E. Lohou, N. A. Sasaki, A. Boullier, and P. Sonnet, “Multifunctional diamine AGE/ALE inhibitors with potential therapeutical properties against Alzheimer’s disease,” European Journal of Medicinal Chemistry, vol. 122, pp. 702–722, 2016. View at Publisher · View at Google Scholar · View at Scopus
  210. M. Colzani, G. Aldini, and M. Carini, “Mass spectrometric approaches for the identification and quantification of reactive carbonyl species protein adducts,” Journal of Proteomics, vol. 92, pp. 28–50, 2013. View at Publisher · View at Google Scholar · View at Scopus
  211. F. Di Domenico, G. Pupo, A. Tramutola et al., “Redox proteomics analysis of HNE-modified proteins in Down syndrome brain: clues for understanding the development of Alzheimer disease,” Free Radical Biology & Medicine, vol. 71, pp. 270–280, 2014. View at Publisher · View at Google Scholar · View at Scopus
  212. J. M. Ashraf, S. Ahmad, I. Choi et al., “Recent advances in detection of AGEs: immunochemical, bioanalytical and biochemical approaches,” IUBMB Life, vol. 67, no. 12, pp. 897–913, 2015. View at Publisher · View at Google Scholar · View at Scopus
  213. C. Da Moura Semedo, M. Webb, H. Waller, K. Khunti, and M. Davies, “Skin autofluorescence, a non-invasive marker of advanced glycation end products: clinical relevance and limitations,” Postgraduate Medical Journal, vol. 93, no. 1099, pp. 289–294, 2017. View at Publisher · View at Google Scholar
  214. C. Y. Liu, Q. F. Huang, Y. B. Cheng et al., “A comparative study on skin and plasma advanced glycation end products and their associations with arterial stiffness,” Pulse (Basel, Switzerland), vol. 4, no. 4, pp. 208–218, 2017. View at Google Scholar
  215. S. Osawa, N. Katakami, A. Kuroda et al., “Skin Autofluorescence is associated with early-stage atherosclerosis in patients with type 1 diabetes,” Journal of Atherosclerosis and Thrombosis, vol. 24, no. 3, pp. 312–326, 2017. View at Publisher · View at Google Scholar
  216. J. P. J. Lobo, C. P. Brescansin, I. C. Santos-Weiss et al., “Serum fluorescent advanced glycation end (F-AGE) products in gestational diabetes patients,” Archives of endocrinology and metabolism, vol. 13, p. 0, 2017. View at Publisher · View at Google Scholar
  217. Q. Liu, M. A. Smith, J. Avila et al., “Alzheimer-specific epitopes of tau represent lipid peroxidation-induced conformations,” Free Radical Biology & Medicine, vol. 38, no. 6, pp. 746–754, 2005. View at Publisher · View at Google Scholar · View at Scopus
  218. R. N. Johnson, P. A. Metcalf, and J. R. Baker, “Fructosamine: a new approach to the estimation of serum glycosylprotein. An index of diabetic control,” Clinica Chimica Acta, vol. 127, no. 1, pp. 87–95, 1983. View at Publisher · View at Google Scholar · View at Scopus
  219. E. Schleicher and O. H. Wieland, “Specific quantitation by HPLC of protein (lysine) bound glucose in human serum albumin and other glycosylated proteins,” Journal of Clinical Chemistry and Clinical Biochemistry, vol. 19, no. 2, pp. 81–87, 1981. View at Google Scholar
  220. X. B. Xu, F. Ma, S. J. Yu, and Y. G. Guan, “Simultaneous analysis of Nepsilon-(carboxymethyl)lysine, reducing sugars, and lysine during the dairy thermal process,” Journal of Dairy Science, vol. 96, no. 9, pp. 5487–5493, 2013. View at Publisher · View at Google Scholar · View at Scopus
  221. J. L. Scheijen, M. P. van de Waarenburg, C. D. Stehouwer, and C. G. Schalkwijk, “Measurement of pentosidine in human plasma protein by a single-column high-performance liquid chromatography method with fluorescence detection,” Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences, vol. 877, no. 7, pp. 610–614, 2009. View at Google Scholar
  222. W. Gu, Z. Xu, F. Qi, Z. Sang, C. Wang, and F. Li, “Plasma levels of soluble receptor for advanced glycation end products in patients with acute respiratory distress syndrome,” International Journal of Clinical and Experimental Medicine, vol. 7, no. 12, pp. 5558–5562, 2014. View at Google Scholar
  223. Z. Turk, M. Sesto, J. Skodlar et al., “Products of advanced glycation in patients with type 2 diabetes and vascular disease,” Annals of Clinical Biochemistry, vol. 40, Part 5, pp. 552–559, 2003. View at Publisher · View at Google Scholar · View at Scopus
  224. S. Ahmad, S. Habib, Moinuddin, and A. Ali, “Preferential recognition of epitopes on AGE-IgG by the autoantibodies in rheumatoid arthritis patients,” Human Immunology, vol. 74, no. 1, pp. 23–27, 2013. View at Publisher · View at Google Scholar · View at Scopus
  225. S. Bartesaghi, G. Ferrer-Sueta, G. Peluffo et al., “Protein tyrosine nitration in hydrophilic and hydrophobic environments,” Amino Acids, vol. 32, no. 4, pp. 501–515, 2007. View at Publisher · View at Google Scholar · View at Scopus
  226. F. J. Schopfer, P. R. Baker, and B. A. Freeman, “NO-dependent protein nitration: a cell signaling event or an oxidative inflammatory response?” Trends in Biochemical Sciences, vol. 28, no. 12, pp. 646–654, 2003. View at Publisher · View at Google Scholar · View at Scopus
  227. J. M. Souza, G. Peluffo, and R. Radi, “Protein tyrosine nitration—functional alteration or just a biomarker?” Free Radical Biology & Medicine, vol. 45, no. 4, pp. 357–366, 2008. View at Publisher · View at Google Scholar · View at Scopus
  228. D. Tsikas and M. W. Duncan, “Mass spectrometry and 3-nitrotyrosine: strategies, controversies, and our current perspective,” Mass Spectrometry Reviews, vol. 33, no. 4, pp. 237–276, 2014. View at Publisher · View at Google Scholar · View at Scopus
  229. Y. Kamisaki, K. Wada, K. Nakamoto, Y. Kishimoto, M. Kitano, and T. Itoh, “Sensitive determination of nitrotyrosine in human plasma by isocratic high-performance liquid chromatography,” Journal of Chromatography. B, Biomedical Applications, vol. 685, no. 2, pp. 343–347, 1996. View at Publisher · View at Google Scholar · View at Scopus
  230. N. Rabbani and P. J. Thornalley, “Assay of 3-nitrotyrosine in tissues and body fluids by liquid chromatography with tandem mass spectrometric detection,” Methods in Enzymology, vol. 440, pp. 337–359, 2008. View at Google Scholar
  231. 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 Google Scholar
  232. S. Xu, J. Ying, B. Jiang et al., “Detection of sequence-specific tyrosine nitration of manganese SOD and SERCA in cardiovascular disease and aging,” American Journal of Physiology. Heart and Circulatory Physiology, vol. 290, no. 6, pp. H2220–H2227, 2006. View at Google Scholar
  233. J. Khan, D. M. Brennand, N. Bradley, B. Gao, R. Bruckdorfer, and M. Jacobs, “3-Nitrotyrosine in the proteins of human plasma determined by an ELISA method,” The Biochemical Journal, vol. 332, Part 3, pp. 807-808, 1998. View at Google Scholar
  234. C. Herce-Pagliai, S. Kotecha, and D. E. Shuker, “Analytical methods for 3-nitrotyrosine as a marker of exposure to reactive nitrogen species: a review,” Nitric Oxide, vol. 2, no. 5, pp. 324–336, 1998. View at Publisher · View at Google Scholar · View at Scopus
  235. S. Meredith, G. Parekh, J. Towler et al., “Mapping nitro-tyrosine modifications in fibrinogen by mass spectrometry as a biomarker for inflammatory disease,” Free Radical Biology & Medicine, vol. 75, Supplement 1, p. S50, 2014. View at Publisher · View at Google Scholar
  236. G. Peluffo and R. Radi, “Biochemistry of protein tyrosine nitration in cardiovascular pathology,” Cardiovascular Research, vol. 75, no. 2, pp. 291–302, 2007. View at Publisher · View at Google Scholar · View at Scopus
  237. N. R. Jayakumari, A. C. Reghuvaran, R. S. Rajendran et al., “Are nitric oxide-mediated protein modifications of functional significance in diabetic heart? ye'S, -NO', wh'Y-NO't?” Nitric Oxide, vol. 43, pp. 35–44, 2014. View at Publisher · View at Google Scholar · View at Scopus
  238. W. S. Yeo, Y. J. Kim, M. H. Kabir, J. W. Kang, M. Ahsan-Ul-Bari, and K. P. Kim, “Mass spectrometric analysis of protein tyrosine nitration in aging and neurodegenerative diseases,” Mass Spectrometry Reviews, vol. 34, no. 2, pp. 166–183, 2015. View at Publisher · View at Google Scholar · View at Scopus
  239. R. Sultana, H. F. Poon, J. Cai et al., “Identification of nitrated proteins in Alzheimer’s disease brain using a redox proteomics approach,” Neurobiology of Disease, vol. 22, no. 1, pp. 76–87, 2006. View at Publisher · View at Google Scholar · View at Scopus
  240. V. Witko-Sarsat, M. Friedlander, T. Nguyen Khoa et al., “Advanced oxidation protein products as novel mediators of inflammation and monocyte activation in chronic renal failure,” Journal of Immunology, vol. 161, no. 5, pp. 2524–2532, 1998. View at Google Scholar
  241. W. Cao, F. F. Hou, and J. Nie, “AOPPs and the progression of kidney disease,” Kidney International, vol. 4, Supplement 2011, no. 1, pp. 102–106, 2014. View at Google Scholar
  242. M. Cristani, A. Speciale, A. Saija, S. Gangemi, P. L. Minciullo, and F. Cimino, “Circulating advanced oxidation protein products as oxidative stress biomarkers and progression mediators in pathological conditions related to inflammation and immune dysregulation,” Current Medicinal Chemistry, vol. 23, no. 34, pp. 3862–3882, 2016. View at Publisher · View at Google Scholar · View at Scopus
  243. M. Kalousova, J. Skrha, and T. Zima, “Advanced glycation end-products and advanced oxidation protein products in patients with diabetes mellitus,” Physiological Research, vol. 51, no. 6, pp. 597–604, 2002. View at Google Scholar
  244. S. L. Du, X. Z. Zeng, J. W. Tian, J. Ai, J. Wan, and J. X. He, “Advanced oxidation protein products in predicting acute kidney injury following cardiac surgery,” Biomarkers, vol. 20, no. 3, pp. 206–211, 2015. View at Publisher · View at Google Scholar · View at Scopus
  245. E. L. Taylor, K. R. Armstrong, D. Perrett, A. T. Hattersley, and P. G. Winyard, “Optimisation of an advanced oxidation protein products assay: its application to studies of oxidative stress in diabetes mellitus,” Oxidative Medicine and Cellular Longevity, vol. 2015, Article ID 496271, 10 pages, 2015. View at Publisher · View at Google Scholar · View at Scopus
  246. S. L. Hazen, J. R. Crowley, D. M. Mueller, and J. W. Heinecke, “Mass spectrometric quantification of 3-chlorotyrosine in human tissues with attomole sensitivity: a sensitive and specific marker for myeloperoxidase-catalyzed chlorination at sites of inflammation,” Free Radical Biology & Medicine, vol. 23, no. 6, pp. 909–916, 1997. View at Publisher · View at Google Scholar · View at Scopus
  247. S. L. Hazen and J. W. Heinecke, “3-Chlorotyrosine, a specific marker of myeloperoxidase-catalyzed oxidation, is markedly elevated in low density lipoprotein isolated from human atherosclerotic intima,” The Journal of Clinical Investigation, vol. 99, no. 9, pp. 2075–2081, 1997. View at Publisher · View at Google Scholar
  248. S. M. Wu and S. V. Pizzo, “α2-Macroglobulin from rheumatoid arthritis synovial fluid: functional analysis defines a role for oxidation in inflammation,” Archives of Biochemistry and Biophysics, vol. 391, no. 1, pp. 119–126, 2001. View at Publisher · View at Google Scholar · View at Scopus
  249. A. J. Kettle, T. Chan, I. Osberg et al., “Myeloperoxidase and protein oxidation in the airways of young children with cystic fibrosis,” American Journal of Respiratory and Critical Care Medicine, vol. 170, no. 12, pp. 1317–1323, 2004. View at Publisher · View at Google Scholar · View at Scopus
  250. I. H. Buss, R. Senthilmohan, B. A. Darlow, N. Mogridge, A. J. Kettle, and C. C. Winterbourn, “3-Chlorotyrosine as a marker of protein damage by myeloperoxidase in tracheal aspirates from preterm infants: association with adverse respiratory outcome,” Pediatric Research, vol. 53, no. 3, pp. 455–462, 2003. View at Publisher · View at Google Scholar · View at Scopus
  251. E. Verhoye, M. R. Langlois, and I. Asklepios, “Circulating oxidized low-density lipoprotein: a biomarker of atherosclerosis and cardiovascular risk?” Clinical Chemistry and Laboratory Medicine, vol. 47, no. 2, pp. 128–137, 2009. View at Publisher · View at Google Scholar · View at Scopus
  252. P. Holvoet, D. De Keyzer, and D. R. Jacobs Jr., “Oxidized LDL and the metabolic syndrome,” Future Lipidology, vol. 3, no. 6, pp. 637–649, 2008. View at Publisher · View at Google Scholar · View at Scopus
  253. G. Maiolino, G. Rossitto, P. Caielli, V. Bisogni, G. P. Rossi, and L. A. Calo, “The role of oxidized low-density lipoproteins in atherosclerosis: the myths and the facts,” Mediators of Inflammation, vol. 2013, Article ID 714653, 13 pages, 2013. View at Publisher · View at Google Scholar · View at Scopus
  254. J. Frijhoff, P. G. Winyard, N. Zarkovic et al., “Clinical relevance of biomarkers of oxidative stress,” Antioxidants & Redox Signaling, vol. 23, no. 14, pp. 1144–1170, 2015. View at Publisher · View at Google Scholar · View at Scopus
  255. S. Al Kasab, C. Cassarly, N. A. Le et al., “Postprandial clearance of oxidized low-density lipoprotein in patients with stroke due to atherosclerosis,” Journal of Stroke and Cerebrovascular Diseases, vol. 26, no. 3, pp. 488–493, 2017. View at Publisher · View at Google Scholar
  256. F. L. Balderas, M. Quezada-Larios, E. A. Garcia Latorre, and J. D. Mendez, “Increased uptake of oxidized LDL by macrophages from type 2 diabetics is inhibited by polyamines,” Biomedicine & Pharmacotherapy, vol. 77, pp. 59–64, 2016. View at Publisher · View at Google Scholar · View at Scopus
  257. A. T. Babakr, O. M. Elsheikh, A. A. Almarzouki et al., “Relationship between oxidized low-density lipoprotein antibodies and obesity in different glycemic situations,” Diabetes, Metabolic Syndrome and Obesity, vol. 7, pp. 513–520, 2014. View at Publisher · View at Google Scholar · View at Scopus
  258. A. A. Rahsepar, A. Mirzaee, F. Moodi et al., “Malondialdehyde-modified LDL IgG antibody levels and indices of cardiac function in valvular heart and coronary artery disease patients,” Medical Principles and Practice, vol. 24, no. 5, pp. 424–431, 2015. View at Publisher · View at Google Scholar · View at Scopus
  259. G. Marx and M. Chevion, “Site-specific modification of albumin by free radicals. Reaction with copper(II) and ascorbate,” The Biochemical Journal, vol. 236, no. 2, pp. 397–400, 1986. View at Publisher · View at Google Scholar
  260. D. Roy, J. Quiles, D. C. Gaze, P. Collinson, J. C. Kaski, and G. F. Baxter, “Role of reactive oxygen species on the formation of the novel diagnostic marker ischaemia modified albumin,” Heart, vol. 92, no. 1, pp. 113-114, 2006. View at Publisher · View at Google Scholar · View at Scopus
  261. D. Bar-Or, G. Curtis, N. Rao, N. Bampos, and E. Lau, “Characterization of the Co2+ and Ni2+ binding amino-acid residues of the N-terminus of human albumin. An insight into the mechanism of a new assay for myocardial ischemia,” European Journal of Biochemistry, vol. 268, no. 1, pp. 42–47, 2001. View at Publisher · View at Google Scholar · View at Scopus
  262. R. H. Christenson, S. H. Duh, W. R. Sanhai et al., “Characteristics of an albumin cobalt binding test for assessment of acute coronary syndrome patients: a multicenter study,” Clinical Chemistry, vol. 47, no. 3, pp. 464–470, 2001. View at Google Scholar
  263. D. C. Gaze, “Ischemia modified albumin: a novel biomarker for the detection of cardiac ischemia,” Drug Metabolism and Pharmacokinetics, vol. 24, no. 4, pp. 333–341, 2009. View at Publisher · View at Google Scholar · View at Scopus
  264. E. Mothes and P. Faller, “Evidence that the principal CoII-binding site in human serum albumin is not at the N-terminus: implication on the albumin cobalt binding test for detecting myocardial ischemia,” Biochemistry, vol. 46, no. 8, pp. 2267–2274, 2007. View at Publisher · View at Google Scholar · View at Scopus
  265. D. Bar-Or, E. Lau, and J. V. Winkler, “A novel assay for cobalt-albumin binding and its potential as a marker for myocardial ischemia-a preliminary report,” The Journal of Emergency Medicine, vol. 19, no. 4, pp. 311–315, 2000. View at Publisher · View at Google Scholar · View at Scopus
  266. S. G. Ma, Y. Jin, W. Hu, F. Bai, W. Xu, and W. N. Yu, “Evaluation of ischemia-modified albumin and C-reactive protein in type 2 diabetics with and without ketosis,” Biomarker Insights, vol. 7, pp. 19–26, 2012. View at Publisher · View at Google Scholar · View at Scopus
  267. A. Gunduz, S. Turedi, A. Mentese et al., “Ischemia-modified albumin levels in cerebrovascular accidents,” The American Journal of Emergency Medicine, vol. 26, no. 8, pp. 874–8, 2008. View at Publisher · View at Google Scholar · View at Scopus
  268. E. Altunoglu, G. Guntas, F. Erdenen et al., “Ischemia-modified albumin and advanced oxidation protein products as potential biomarkers of protein oxidation in Alzheimer’s disease,” Geriatrics & Gerontology International, vol. 15, no. 7, pp. 872–880, 2015. View at Publisher · View at Google Scholar · View at Scopus
  269. A. Kumar, “Ischemia-modified albumin: its diagnostic implications and shortfalls,” Journal of Biomedical Science, vol. 1, pp. 2–4, 2012. View at Google Scholar
  270. E. Sbarouni, P. Georgiadou, and V. Voudris, “Ischemia modified albumin changes - review and clinical implications,” Clinical Chemistry and Laboratory Medicine, vol. 49, no. 2, pp. 177–184, 2011. View at Publisher · View at Google Scholar · View at Scopus
  271. P. O. Collinson and D. C. Gaze, “Ischaemia-modified albumin: clinical utility and pitfalls in measurement,” Journal of Clinical Pathology, vol. 61, no. 9, pp. 1025–1028, 2008. View at Publisher · View at Google Scholar · View at Scopus
  272. A. G. Madian, A. D. Myracle, N. Diaz-Maldonado, N. S. Rochelle, E. M. Janle, and F. E. Regnier, “Differential carbonylation of proteins as a function of in vivo oxidative stress,” Journal of Proteome Research, vol. 10, no. 9, pp. 3959–3972, 2011. View at Publisher · View at Google Scholar · View at Scopus
  273. A. Bachi, I. Dalle-Donne, and A. Scaloni, “Redox proteomics: chemical principles, methodological approaches and biological/biomedical promises,” Chemical Reviews, vol. 113, no. 1, pp. 596–698, 2013. View at Publisher · View at Google Scholar · View at Scopus
  274. S. Boronat, S. Garcia-Santamarina, and E. Hidalgo, “Gel-free proteomic methodologies to study reversible cysteine oxidation and irreversible protein carbonyl formation,” Free Radical Research, vol. 49, no. 5, pp. 494–510, 2015. View at Publisher · View at Google Scholar · View at Scopus
  275. L. J. Yan, “Protein redox modification as a cellular defense mechanism against tissue ischemic injury,” Oxidative Medicine and Cellular Longevity, vol. 2014, Article ID 343154, 12 pages, 2014. View at Publisher · View at Google Scholar · View at Scopus
  276. M. Fedorova, R. C. Bollineni, and R. Hoffmann, “Protein carbonylation as a major hallmark of oxidative damage: update of analytical strategies,” Mass Spectrometry Reviews, vol. 33, no. 2, pp. 79–97, 2014. View at Publisher · View at Google Scholar · View at Scopus
  277. M. A. Baraibar, R. Ladouce, and B. Friguet, “Proteomic quantification and identification of carbonylated proteins upon oxidative stress and during cellular aging,” Journal of Proteomics, vol. 92, pp. 63–70, 2013. View at Publisher · View at Google Scholar · View at Scopus
  278. M. Serafini, D. Villano, G. Spera, and N. Pellegrini, “Redox molecules and cancer prevention: the importance of understanding the role of the antioxidant network,” Nutrition and Cancer, vol. 56, no. 2, pp. 232–240, 2006. View at Publisher · View at Google Scholar · View at Scopus
  279. C. C. Winterbourn and M. B. Hampton, “Thiol chemistry and specificity in redox signaling,” Free Radical Biology & Medicine, vol. 45, no. 5, pp. 549–561, 2008. View at Publisher · View at Google Scholar · View at Scopus
  280. Y. Wang, J. Yang, and J. Yi, “Redox sensing by proteins: oxidative modifications on cysteines and the consequent events,” Antioxidants & Redox Signaling, vol. 16, no. 7, pp. 649–657, 2012. View at Publisher · View at Google Scholar · View at Scopus
  281. L. B. Poole, “The basics of thiols and cysteines in redox biology and chemistry,” Free Radical Biology & Medicine, vol. 80, pp. 148–157, 2015. View at Publisher · View at Google Scholar · View at Scopus
  282. M. Trujillo, B. Alvarez, and R. Radi, “One- and two-electron oxidation of thiols: mechanisms, kinetics and biological fates,” Free Radical Research, vol. 50, no. 2, pp. 150–171, 2016. View at Publisher · View at Google Scholar · View at Scopus
  283. B. C. Smith and M. A. Marletta, “Mechanisms of S-nitrosothiol formation and selectivity in nitric oxide signaling,” Current Opinion in Chemical Biology, vol. 16, no. 5-6, pp. 498–506, 2012. View at Publisher · View at Google Scholar · View at Scopus
  284. F. R. Laurindo, L. A. Pescatore, and C. Fernandes Dde, “Protein disulfide isomerase in redox cell signaling and homeostasis,” Free Radical Biology & Medicine, vol. 52, no. 9, pp. 1954–1969, 2012. View at Publisher · View at Google Scholar · View at Scopus
  285. E. M. Hanschmann, J. R. Godoy, C. Berndt, C. Hudemann, and C. H. Lillig, “Thioredoxins, glutaredoxins, and peroxiredoxins—molecular mechanisms and health significance: from cofactors to antioxidants to redox signaling,” Antioxidants & Redox Signaling, vol. 19, no. 13, pp. 1539–1605, 2013. View at Publisher · View at Google Scholar · View at Scopus
  286. J. Lu and A. Holmgren, “The thioredoxin antioxidant system,” Free Radical Biology & Medicine, vol. 66, pp. 75–87, 2014. View at Publisher · View at Google Scholar · View at Scopus
  287. M. Pajares, N. Jimenez-Moreno, I. H. Dias et al., “Redox control of protein degradation,” Redox Biology, vol. 6, pp. 409–420, 2015. View at Publisher · View at Google Scholar · View at Scopus
  288. 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
  289. J. Tyedmers, A. Mogk, and B. Bukau, “Cellular strategies for controlling protein aggregation,” Nature Reviews. Molecular Cell Biology, vol. 11, no. 11, pp. 777–788, 2010. View at Publisher · View at Google Scholar · View at Scopus
  290. M. A. Comini, “Measurement and meaning of cellular thiol:disufhide redox status,” Free Radical Research, vol. 50, no. 2, pp. 246–271, 2016. View at Publisher · View at Google Scholar · View at Scopus
  291. Y. M. Go and D. P. Jones, “Thiol/disulfide redox states in signaling and sensing,” Critical Reviews in Biochemistry and Molecular Biology, vol. 48, no. 2, pp. 173–181, 2013. View at Google Scholar
  292. C. Klomsiri, P. A. Karplus, and L. B. Poole, “Cysteine-based redox switches in enzymes,” Antioxidants & Redox Signaling, vol. 14, no. 6, pp. 1065–1077, 2011. View at Publisher · View at Google Scholar · View at Scopus
  293. S. B. Wall, J. Y. Oh, A. R. Diers, and A. Landar, “Oxidative modification of proteins: an emerging mechanism of cell signaling,” Frontiers in Physiology, vol. 3, p. 369, 2012. View at Publisher · View at Google Scholar · View at Scopus
  294. M. D. Shelton, P. B. Chock, and J. J. Mieyal, “Glutaredoxin: role in reversible protein s-glutathionylation and regulation of redox signal transduction and protein translocation,” Antioxidants & Redox Signaling, vol. 7, no. 3-4, pp. 348–366, 2005. View at Publisher · View at Google Scholar · View at Scopus
  295. P. Ghezzi, “Protein glutathionylation in health and disease,” Biochimica et Biophysica Acta, vol. 1830, no. 5, pp. 3165–3172, 2013. View at Google Scholar
  296. S. L. Ullevig, H. S. Kim, J. D. Short et al., “Protein S-glutathionylation mediates macrophage responses to metabolic cues from the extracellular environment,” Antioxidants & Redox Signaling, vol. 25, no. 15, pp. 836–851, 2016. View at Publisher · View at Google Scholar · View at Scopus
  297. R. Rossi, I. Dalle-Donne, A. Milzani, and D. Giustarini, “Oxidized forms of glutathione in peripheral blood as biomarkers of oxidative stress,” Clinical Chemistry, vol. 52, no. 7, pp. 1406–1414, 2006. View at Publisher · View at Google Scholar · View at Scopus
  298. S. E. Bursell and G. L. King, “The potential use of glutathionyl hemoglobin as a clinical marker of oxidative stress,” Clinical Chemistry, vol. 46, no. 2, pp. 145-146, 2000. View at Google Scholar
  299. T. Niwa, C. Naito, A. H. Mawjood, and K. Imai, “Increased glutathionyl hemoglobin in diabetes mellitus and hyperlipidemia demonstrated by liquid chromatography/electrospray ionization-mass spectrometry,” Clinical Chemistry, vol. 46, no. 1, pp. 82–88, 2000. View at Google Scholar
  300. M. Johansson and M. Lundberg, “Glutathionylation of beta-actin via a cysteinyl sulfenic acid intermediary,” BMC Biochemistry, vol. 8, p. 26, 2007. View at Publisher · View at Google Scholar · View at Scopus
  301. G. A. Figtree, C. C. Liu, S. Bibert et al., “Reversible oxidative modification: a key mechanism of Na+-K+ pump regulation,” Circulation Research, vol. 105, no. 2, pp. 185–193, 2009. View at Publisher · View at Google Scholar · View at Scopus
  302. C. C. Liu, N. Fry, K. K. Galougahi, H. H. Rasmussen, and G. A. Figtree, “Glutathionylation of erythrocyte Na–K pump in heart failure: a novel biomarker that reflects a key oxidative abnormality in the heart,” Circulation, vol. 126, 2012. View at Google Scholar
  303. G. Wu, Y. Z. Fang, S. Yang, J. R. Lupton, and N. D. Turner, “Glutathione metabolism and its implications for health,” The Journal of Nutrition, vol. 134, no. 3, pp. 489–492, 2004. View at Google Scholar
  304. S. C. Lu, “Regulation of glutathione synthesis,” Molecular Aspects of Medicine, vol. 30, no. 1-2, pp. 42–59, 2009. View at Publisher · View at Google Scholar · View at Scopus
  305. F. Q. Schafer and G. R. Buettner, “Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple,” Free Radical Biology & Medicine, vol. 30, no. 11, pp. 1191–1212, 2001. View at Publisher · View at Google Scholar · View at Scopus
  306. R. A. Blanco, T. R. Ziegler, B. A. Carlson et al., “Diurnal variation in glutathione and cysteine redox states in human plasma,” The American Journal of Clinical Nutrition, vol. 86, no. 4, pp. 1016–1023, 2007. View at Google Scholar
  307. A. Pastore, G. Federici, E. Bertini, and F. Piemonte, “Analysis of glutathione: implication in redox and detoxification,” Clinica Chimica Acta, vol. 333, no. 1, pp. 19–39, 2003. View at Publisher · View at Google Scholar · View at Scopus
  308. R. Rossi, A. Milzani, I. Dalle-Donne et al., “Blood glutathione disulfide: in vivo factor or in vitro artifact?” Clinical Chemistry, vol. 48, no. 5, pp. 742–753, 2002. View at Google Scholar
  309. J. M. Lee and J. A. Johnson, “An important role of Nrf2-ARE pathway in the cellular defense mechanism,” Journal of Biochemistry and Molecular Biology, vol. 37, no. 2, pp. 139–143, 2004. View at Google Scholar
  310. R. Zhang, M. Xu, Y. Wang, F. Xie, G. Zhang, and X. Qin, “Nrf2-a promising therapeutic target for defensing against oxidative stress in stroke,” Molecular Neurobiology, 2016, Epub ahead of print. View at Publisher · View at Google Scholar · View at Scopus
  311. I. Ganan-Gomez, Y. Wei, H. Yang, M. C. Boyano-Adanez, and G. Garcia-Manero, “Oncogenic functions of the transcription factor Nrf2,” Free Radical Biology & Medicine, vol. 65, pp. 750–764, 2013. View at Publisher · View at Google Scholar · View at Scopus
  312. F. Polito, M. Cicciu, M. Aguennouz et al., “Prognostic value of HMGB1 and oxidative stress markers in multiple trauma patients: a single-centre prospective study,” International Journal of Immunopathology and Pharmacology, vol. 29, no. 3, pp. 504–509, 2016. View at Publisher · View at Google Scholar · View at Scopus
  313. N. L. Reynaert, A. van der Vliet, A. S. Guala et al., “Dynamic redox control of NF-kappaB through glutaredoxin-regulated S-glutathionylation of inhibitory kappaB kinase beta,” Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 35, pp. 13086–13091, 2006. View at Google Scholar
  314. P. S. Son, S. A. Park, H. K. Na, D. M. Jue, S. Kim, and Y. J. Surh, “Piceatannol, a catechol-type polyphenol, inhibits phorbol ester-induced NF-{kappa}B activation and cyclooxygenase-2 expression in human breast epithelial cells: cysteine 179 of IKK{beta} as a potential target,” Carcinogenesis, vol. 31, no. 8, pp. 1442–1449, 2010. View at Publisher · View at Google Scholar · View at Scopus
  315. K. Heyninck, M. Lahtela-Kakkonen, P. Van der Veken, G. Haegeman, and W. Vanden Berghe, “Withaferin A inhibits NF-kappaB activation by targeting cysteine 179 in IKKbeta,” Biochemical Pharmacology, vol. 91, no. 4, pp. 501–509, 2014. View at Publisher · View at Google Scholar · View at Scopus
  316. T. Ishii, M. Ishikawa, N. Miyoshi et al., “Catechol type polyphenol is a potential modifier of protein sulfhydryls: development and application of a new probe for understanding the dietary polyphenol actions,” Chemical Research in Toxicology, vol. 22, no. 10, pp. 1689–1698, 2009. View at Publisher · View at Google Scholar · View at Scopus
  317. R. Sirota, D. Gibson, and R. Kohen, “The role of the catecholic and the electrophilic moieties of caffeic acid in Nrf2/Keap1 pathway activation in ovarian carcinoma cell lines,” Redox Biology, vol. 4, pp. 48–59, 2015. View at Publisher · View at Google Scholar · View at Scopus
  318. P. Higgins, J. Dawson, K. R. Lees, K. McArthur, T. J. Quinn, and M. R. Walters, “Xanthine oxidase inhibition for the treatment of cardiovascular disease: a systematic review and meta-analysis,” Cardiovascular Therapeutics, vol. 30, no. 4, pp. 217–226, 2012. View at Publisher · View at Google Scholar · View at Scopus
  319. G. R. Drummond, S. Selemidis, K. K. Griendling, and C. G. Sobey, “Combating oxidative stress in vascular disease: NADPH oxidases as therapeutic targets,” Nature Reviews. Drug Discovery, vol. 10, no. 6, pp. 453–471, 2011. View at Publisher · View at Google Scholar · View at Scopus
  320. S. Sahoo, D. N. Meijles, and P. J. Pagano, “NADPH oxidases: key modulators in aging and age-related cardiovascular diseases?” Clinical Science (London, England), vol. 130, no. 5, pp. 317–335, 2016. View at Publisher · View at Google Scholar · View at Scopus
  321. H. Scharnagl, M. E. Kleber, B. Genser et al., “Association of myeloperoxidase with total and cardiovascular mortality in individuals undergoing coronary angiography—the LURIC study,” International Journal of Cardiology, vol. 174, no. 1, pp. 96–105, 2014. View at Publisher · View at Google Scholar · View at Scopus
  322. J. D. Morrow, W. Qiu, D. Chhabra et al., “Identifying a gene expression signature of frequent COPD exacerbations in peripheral blood using network methods,” BMC Medical Genomics, vol. 8, p. 1, 2015. View at Google Scholar
  323. 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
  324. A. J. Kettle, A. M. Albrett, A. L. Chapman et al., “Measuring chlorine bleach in biology and medicine,” Biochimica et Biophysica Acta, vol. 1840, no. 2, pp. 781–793, 2014. View at Google Scholar
  325. B. Ibrahim and P. J. Stoward, “The histochemical localization of xanthine oxidase,” The Histochemical Journal, vol. 10, no. 5, pp. 615–617, 1978. View at Publisher · View at Google Scholar · View at Scopus
  326. T. P. Cappola, D. A. Kass, G. S. Nelson et al., “Allopurinol improves myocardial efficiency in patients with idiopathic dilated cardiomyopathy,” Circulation, vol. 104, no. 20, pp. 2407–2411, 2001. View at Publisher · View at Google Scholar
  327. S. D. Anker, W. Doehner, M. Rauchhaus et al., “Uric acid and survival in chronic heart failure: validation and application in metabolic, functional, and hemodynamic staging,” Circulation, vol. 107, no. 15, pp. 1991–1997, 2003. View at Publisher · View at Google Scholar · View at Scopus
  328. S. Kojima, T. Sakamoto, M. Ishihara et al., “Coronary syndrome study, prognostic usefulness of serum uric acid after acute myocardial infarction (the Japanese Acute Coronary Syndrome Study),” The American Journal of Cardiology, vol. 96, no. 4, pp. 489–495, 2005. View at Publisher · View at Google Scholar · View at Scopus
  329. F. J. Nieto, C. Iribarren, M. D. Gross, G. W. Comstock, and R. G. Cutler, “Uric acid and serum antioxidant capacity: a reaction to atherosclerosis?” Atherosclerosis, vol. 148, no. 1, pp. 131–139, 2000. View at Publisher · View at Google Scholar · View at Scopus
  330. A. Sarnesto, N. Linder, and K. O. Raivio, “Organ distribution and molecular forms of human xanthine dehydrogenase/xanthine oxidase protein,” Laboratory Investigation, vol. 74, no. 1, pp. 48–56, 1996. View at Google Scholar
  331. F. Stirpe and E. Della Corte, “The regulation of rat liver xanthine oxidase. Conversion in vitro of the enzyme activity from dehydrogenase (type D) to oxidase (type O),” The Journal of Biological Chemistry, vol. 244, no. 14, pp. 3855–3863, 1969. View at Google Scholar
  332. T. Nishino, K. Okamoto, B. T. Eger, E. F. Pai, and T. Nishino, “Mammalian xanthine oxidoreductase - mechanism of transition from xanthine dehydrogenase to xanthine oxidase,” The FEBS Journal, vol. 275, no. 13, pp. 3278–3289, 2008. View at Publisher · View at Google Scholar · View at Scopus
  333. R. Harrison, “Structure and function of xanthine oxidoreductase: where are we now?” Free Radical Biology & Medicine, vol. 33, no. 6, pp. 774–797, 2002. View at Publisher · View at Google Scholar · View at Scopus
  334. N. Cantu-Medellin and E. E. Kelley, “Xanthine oxidoreductase-catalyzed reactive species generation: a process in critical need of reevaluation,” Redox Biology, vol. 1, pp. 353–358, 2013. View at Publisher · View at Google Scholar · View at Scopus
  335. S. Baldus, R. Koster, P. Chumley et al., “Oxypurinol improves coronary and peripheral endothelial function in patients with coronary artery disease,” Free Radical Biology & Medicine, vol. 39, no. 9, pp. 1184–1190, 2005. View at Publisher · View at Google Scholar · View at Scopus
  336. P. Ghezzi, M. Bianchi, A. Mantovani, F. Spreafico, and M. Salmona, “Enhanced xanthine oxidase activity in mice treated with interferon and interferon inducers,” Biochemical and Biophysical Research Communications, vol. 119, no. 1, pp. 144–149, 1984. View at Publisher · View at Google Scholar · View at Scopus
  337. J. M. McCord, “Oxygen-derived free radicals in postischemic tissue injury,” The New England Journal of Medicine, vol. 312, no. 3, pp. 159–163, 1985. View at Publisher · View at Google Scholar
  338. Y. Lytvyn, B. A. Perkins, and D. Z. Cherney, “Uric acid as a biomarker and a therapeutic target in diabetes,” Canadian Journal of Diabetes, vol. 39, no. 3, pp. 239–246, 2015. View at Publisher · View at Google Scholar · View at Scopus
  339. M. Kaufman and M. Guglin, “Uric acid in heart failure: a biomarker or therapeutic target?” Heart Failure Reviews, vol. 18, no. 2, pp. 177–186, 2013. View at Publisher · View at Google Scholar · View at Scopus
  340. V. Filiopoulos, D. Hadjiyannakos, and D. Vlassopoulos, “New insights into uric acid effects on the progression and prognosis of chronic kidney disease,” Renal Failure, vol. 34, no. 4, pp. 510–520, 2012. View at Publisher · View at Google Scholar · View at Scopus
  341. B. Halliwell and M. Whiteman, “Measuring reactive species and oxidative damage in vivo and in cell culture: how should you do it and what do the results mean?” British Journal of Pharmacology, vol. 142, no. 2, pp. 231–255, 2004. View at Publisher · View at Google Scholar · View at Scopus
  342. B. N. Ames, R. Cathcart, E. Schwiers, and P. Hochstein, “Uric acid provides an antioxidant defense in humans against oxidant- and radical-caused aging and cancer: a hypothesis,” Proceedings of the National Academy of Sciences of the United States of America, vol. 78, no. 11, pp. 6858–6862, 1981. View at Google Scholar
  343. R. Kand'ar, P. Zakova, and V. Muzakova, “Monitoring of antioxidant properties of uric acid in humans for a consideration measuring of levels of allantoin in plasma by liquid chromatography,” Clinica Chimica Acta, vol. 365, no. 1-2, pp. 249–256, 2006. View at Publisher · View at Google Scholar · View at Scopus
  344. D. Il'yasova, P. Scarbrough, and I. Spasojevic, “Urinary biomarkers of oxidative status,” Clinica Chimica Acta, vol. 413, no. 19-20, pp. 1446–1453, 2012. View at Publisher · View at Google Scholar · View at Scopus
  345. M. Czerska, K. Mikolajewska, M. Zielinski, J. Gromadzinska, and W. Wasowicz, “Today's oxidative stress markers,” Medycyna Pracy, vol. 66, no. 3, pp. 393–405, 2015. View at Publisher · View at Google Scholar · View at Scopus
  346. R. Kandar, “The ratio of oxidized and reduced forms of selected antioxidants as a possible marker of oxidative stress in humans,” Biomedical Chromatography, vol. 30, no. 1, pp. 13–28, 2016. View at Publisher · View at Google Scholar · View at Scopus
  347. I. N. Zelko, T. J. Mariani, and R. J. Folz, “Superoxide dismutase multigene family: a comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression,” Free Radical Biology & Medicine, vol. 33, no. 3, pp. 337–349, 2002. View at Publisher · View at Google Scholar · View at Scopus
  348. A. V. Peskin and C. C. Winterbourn, “Assay of superoxide dismutase activity in a plate assay using WST-1,” Free Radical Biology & Medicine, vol. 103, pp. 188–191, 2017. View at Publisher · View at Google Scholar
  349. C. Vives-Bauza, A. Starkov, and E. Garcia-Arumi, “Measurements of the antioxidant enzyme activities of superoxide dismutase, catalase, and glutathione peroxidase,” Methods in Cell Biology, vol. 80, pp. 379–393, 2007. View at Google Scholar
  350. M. R. Slaughter and P. J. O'Brien, “Fully-automated spectrophotometric method for measurement of antioxidant activity of catalase,” Clinical Biochemistry, vol. 33, no. 7, pp. 525–534, 2000. View at Publisher · View at Google Scholar · View at Scopus
  351. J. M. Harlan, J. D. Levine, K. S. Callahan, B. R. Schwartz, and L. A. Harker, “Glutathione redox cycle protects cultured endothelial cells against lysis by extracellularly generated hydrogen peroxide,” The Journal of Clinical Investigation, vol. 73, no. 3, pp. 706–713, 1984. View at Publisher · View at Google Scholar
  352. L. Flohe and W. A. Gunzler, “Assays of glutathione peroxidase,” Methods in Enzymology, vol. 105, pp. 114–121, 1984. View at Google Scholar
  353. D. M. Goldberg and R. J. Spooner, “Assay of glutathione reductase,” in Methods of Enzymatic Analysis, H. V. Bergmeyer, Ed., pp. 258–265, Verlag Chemie, Weinheim, Germany, 1983. View at Google Scholar
  354. M. Banerjee and P. Vats, “Reactive metabolites and antioxidant gene polymorphisms in type 2 diabetes mellitus,” Redox Biology, vol. 2, pp. 170–177, 2014. View at Publisher · View at Google Scholar · View at Scopus
  355. S. Eslami and A. Sahebkar, “Glutathione-S-transferase M1 and T1 null genotypes are associated with hypertension risk: a systematic review and meta-analysis of 12 studies,” Current Hypertension Reports, vol. 16, no. 6, p. 432, 2014. View at Google Scholar
  356. J. Rybka, D. Kupczyk, K. Kedziora-Kornatowska et al., “Age-related changes in an antioxidant defense system in elderly patients with essential hypertension compared with healthy controls,” Redox Report, vol. 16, no. 2, pp. 71–77, 2011. View at Google Scholar
  357. D. V. Simic, J. Mimic-Oka, M. Pljesa-Ercegovac et al., “Byproducts of oxidative protein damage and antioxidant enzyme activities in plasma of patients with different degrees of essential hypertension,” Journal of Human Hypertension, vol. 20, no. 2, pp. 149–155, 2006. View at Google Scholar
  358. M. Kumawat, T. K. Sharma, I. Singh et al., “Antioxidant enzymes and lipid peroxidation in type 2 diabetes mellitus patients with and without nephropathy,” North American Journal of Medical Sciences, vol. 5, no. 3, pp. 213–219, 2013. View at Publisher · View at Google Scholar · View at Scopus
  359. M. Kumawat, T. K. Sharma, N. Singh et al., “Study of changes in antioxidant enzymes status in diabetic post menopausal group of women suffering from cardiovascular complications,” Clinical Laboratory, vol. 58, no. 3-4, pp. 203–207, 2012. View at Google Scholar
  360. S. M. Bandeira, G. S. Guedes, L. J. da Fonseca et al., “Characterization of blood oxidative stress in type 2 diabetes mellitus patients: increase in lipid peroxidation and SOD activity,” Oxidative Medicine and Cellular Longevity, vol. 2012, Article ID 819310, 13 pages, 2012. View at Publisher · View at Google Scholar · View at Scopus
  361. H. M. Turk, A. Sevinc, C. Camci et al., “Plasma lipid peroxidation products and antioxidant enzyme activities in patients with type 2 diabetes mellitus,” Acta Diabetologica, vol. 39, no. 3, pp. 117–122, 2002. View at Publisher · View at Google Scholar · View at Scopus
  362. T. Atli, K. Keven, A. Avci et al., “Oxidative stress and antioxidant status in elderly diabetes mellitus and glucose intolerance patients,” Archives of Gerontology and Geriatrics, vol. 39, no. 3, pp. 269–275, 2004. View at Publisher · View at Google Scholar · View at Scopus
  363. F. N. Ahmed, F. N. Naqvi, and F. Shafiq, “Lipid peroxidation and serum antioxidant enzymes in patients with type 2 diabetes mellitus,” Annals of the New York Academy of Sciences, vol. 1084, pp. 481–489, 2006. View at Google Scholar
  364. N. Kurtul, E. Bakan, H. Aksoy, and O. Baykal, “Leukocyte lipid peroxidation, superoxide dismutase and catalase activities of type 2 diabetic patients with retinopathy,” Acta Medica (Hradec Králové), vol. 48, no. 1, pp. 35–38, 2005. View at Google Scholar
  365. F. J. Tinahones, M. Murri-Pierri, L. Garrido-Sanchez et al., “Oxidative stress in severely obese persons is greater in those with insulin resistance,” Obesity (Silver Spring), vol. 17, no. 2, pp. 240–246, 2009. View at Publisher · View at Google Scholar · View at Scopus
  366. A. K. Arya, D. Pokharia, and K. Tripathi, “Relationship between oxidative stress and apoptotic markers in lymphocytes of diabetic patients with chronic non healing wound,” Diabetes Research and Clinical Practice, vol. 94, no. 3, pp. 377–384, 2011. View at Publisher · View at Google Scholar · View at Scopus
  367. K. Gawlik, J. W. Naskalski, D. Fedak et al., “Markers of antioxidant defense in patients with type 2 diabetes,” Oxidative Medicine and Cellular Longevity, vol. 2016, Article ID 2352361, 6 pages, 2016. View at Publisher · View at Google Scholar · View at Scopus
  368. A. Likidlilid, N. Patchanans, T. Peerapatdit, and C. Sriratanasathavorn, “Lipid peroxidation and antioxidant enzyme activities in erythrocytes of type 2 diabetic patients,” Journal of the Medical Association of Thailand, vol. 93, no. 6, pp. 682–693, 2010. View at Google Scholar
  369. B. J. Lee, Y. C. Lin, Y. C. Huang, Y. W. Ko, S. Hsia, and P. T. Lin, “The relationship between coenzyme Q10, oxidative stress, and antioxidant enzymes activities and coronary artery disease,” Scientific World Journal, vol. 2012, no. article 792756, 2012. View at Publisher · View at Google Scholar · View at Scopus
  370. M. Murri, M. Luque-Ramirez, M. Insenser, M. Ojeda-Ojeda, and H. F. Escobar-Morreale, “Circulating markers of oxidative stress and polycystic ovary syndrome (PCOS): a systematic review and meta-analysis,” Human Reproduction Update, vol. 19, no. 3, pp. 268–288, 2013. View at Publisher · View at Google Scholar · View at Scopus
  371. M. Iborra, I. Moret, F. Rausell et al., “Role of oxidative stress and antioxidant enzymes in Crohn’s disease,” Biochemical Society Transactions, vol. 39, no. 4, pp. 1102–1106, 2011. View at Publisher · View at Google Scholar · View at Scopus
  372. N. Karaouzene, H. Merzouk, M. Aribi et al., “Effects of the association of aging and obesity on lipids, lipoproteins and oxidative stress biomarkers: a comparison of older with young men,” Nutrition, Metabolism, and Cardiovascular Diseases, vol. 21, no. 10, pp. 792–799, 2011. View at Publisher · View at Google Scholar · View at Scopus
  373. S. Qin and D. X. Hou, “Multiple regulations of Keap1/Nrf2 system by dietary phytochemicals,” Molecular Nutrition & Food Research, vol. 60, no. 8, pp. 1731–1755, 2016. View at Publisher · View at Google Scholar · View at Scopus
  374. F. S. Tonin, L. M. Steimbach, A. Wiens, C. M. Perlin, and R. Pontarolo, “Impact of natural juice consumption on plasma antioxidant status: a systematic review and meta-analysis,” Molecules, vol. 20, no. 12, pp. 22146–22156, 2015. View at Publisher · View at Google Scholar · View at Scopus
  375. Q. Zhou, L. Zhu, D. Zhang et al., “Oxidative stress-related biomarkers in postmenopausal osteoporosis: a systematic review and meta-analyses,” Disease Markers, vol. 2016, Article ID 7067984, 12 pages, 2016. View at Publisher · View at Google Scholar · View at Scopus
  376. J. Yang, N. Diaz, J. Adelsberger et al., “The effects of storage temperature on PBMC gene expression,” BMC Immunology, vol. 17, p. 6, 2016. View at Google Scholar
  377. M. G. Barnes, A. A. Grom, T. A. Griffin, R. A. Colbert, and S. D. Thompson, “Gene expression profiles from peripheral blood mononuclear cells are sensitive to short processing delays,” Biopreservation and Biobanking, vol. 8, no. 3, pp. 153–162, 2010. View at Publisher · View at Google Scholar · View at Scopus
  378. A. Ambayya, A. T. Su, N. H. Osman et al., “Haematological reference intervals in a multiethnic population,” PLoS One, vol. 9, no. 3, article e91968, 2014. View at Publisher · View at Google Scholar · View at Scopus
  379. C. B. Chiwakata, C. J. Hemmer, and M. Dietrich, “High levels of inducible nitric oxide synthase mRNA are associated with increased monocyte counts in blood and have a beneficial role in plasmodium falciparum malaria,” Infection and Immunity, vol. 68, no. 1, pp. 394–399, 2000. View at Publisher · View at Google Scholar
  380. S. S. Okada, E. M. de Oliveira, T. H. de Araujo et al., “Myeloperoxidase in human peripheral blood lymphocytes: production and subcellular localization,” Cellular Immunology, vol. 300, pp. 18–25, 2016. View at Publisher · View at Google Scholar · View at Scopus
  381. P. Pietarinen-Runtti, E. Lakari, K. O. Raivio, and V. L. Kinnula, “Expression of antioxidant enzymes in human inflammatory cells,” American Journal of Physiology. Cell Physiology, vol. 278, no. 1, pp. C118–C125, 2000. View at Google Scholar
  382. X. Yin, Y. Xiao, F. Li, S. Qi, Z. Yin, and J. Gao, “Prognostic role of neutrophil-to-lymphocyte ratio in prostate cancer: a systematic review and meta-analysis,” Medicine (Baltimore), vol. 95, no. 3, article e2544, 2016. View at Publisher · View at Google Scholar · View at Scopus
  383. H. Yodying, A. Matsuda, M. Miyashita et al., “Prognostic significance of neutrophil-to-lymphocyte ratio and platelet-to-lymphocyte ratio in oncologic outcomes of esophageal cancer: a systematic review and meta-analysis,” Annals of Surgical Oncology, vol. 23, no. 2, pp. 646–654, 2016. View at Publisher · View at Google Scholar · View at Scopus
  384. J. Sun, X. Chen, P. Gao et al., “Can the neutrophil to lymphocyte ratio be used to determine gastric cancer treatment outcomes? A Systematic Review and Meta-Analysis,” Disease Markers, vol. 2016, Article ID 7862469, 10 pages, 2016. View at Publisher · View at Google Scholar · View at Scopus
  385. Y. Luo, D. L. She, H. Xiong, S. J. Fu, and L. Yang, “Pretreatment neutrophil to lymphocyte ratio as a prognostic predictor of urologic tumors: a systematic review and meta-analysis,” Medicine (Baltimore), vol. 94, no. 40, article e1670, 2015. View at Publisher · View at Google Scholar · View at Scopus
  386. J. J. Yang, Z. G. Hu, W. X. Shi, T. Deng, S. Q. He, and S. G. Yuan, “Prognostic significance of neutrophil to lymphocyte ratio in pancreatic cancer: a meta-analysis,” World Journal of Gastroenterology, vol. 21, no. 9, pp. 2807–2815, 2015. View at Publisher · View at Google Scholar · View at Scopus
  387. A. J. Templeton, M. G. McNamara, B. Seruga et al., “Prognostic role of neutrophil-to-lymphocyte ratio in solid tumors: a systematic review and meta-analysis,” Journal of the National Cancer Institute, vol. 106, no. 6, p. dju124, 2014. View at Publisher · View at Google Scholar · View at Scopus
  388. T. F. Nishijima, H. B. Muss, S. S. Shachar, K. Tamura, and Y. Takamatsu, “Prognostic value of lymphocyte-to-monocyte ratio in patients with solid tumors: a systematic review and meta-analysis,” Cancer Treatment Reviews, vol. 41, no. 10, pp. 971–978, 2015. View at Publisher · View at Google Scholar · View at Scopus
  389. J. J. Teng, J. Zhang, T. Y. Zhang, S. Zhang, and B. S. Li, “Prognostic value of peripheral blood lymphocyte-to-monocyte ratio in patients with solid tumors: a meta-analysis,” OncoTargets and therapy, vol. 9, pp. 37–47, 2016. View at Publisher · View at Google Scholar · View at Scopus
  390. N. G. Kounis, G. D. Soufras, G. Tsigkas, and G. Hahalis, “White blood cell counts, leukocyte ratios, and eosinophils as inflammatory markers in patients with coronary artery disease,” Clinical and Applied Thrombosis/Hemostasis, vol. 21, no. 2, pp. 139–143, 2015. View at Publisher · View at Google Scholar · View at Scopus
  391. N. D. Vaziri, M. V. Pahl, A. Crum, and K. Norris, “Effect of uremia on structure and function of immune system,” Journal of Renal Nutrition, vol. 22, no. 1, pp. 149–156, 2012. View at Publisher · View at Google Scholar · View at Scopus
  392. S. Mocellin, M. Provenzano, C. R. Rossi, P. Pilati, D. Nitti, and M. Lise, “Use of quantitative real-time PCR to determine immune cell density and cytokine gene profile in the tumor microenvironment,” Journal of Immunological Methods, vol. 280, no. 1-2, pp. 1–11, 2003. View at Publisher · View at Google Scholar · View at Scopus
  393. P. Kar, H. Chawla, S. Saha, N. Tandon, and R. Goswami, “Identification of reference housekeeping-genes for mRNA expression studies in patients with type 1 diabetes,” Molecular and Cellular Biochemistry, vol. 417, no. 1-2, pp. 49–56, 2016. View at Publisher · View at Google Scholar · View at Scopus
  394. D. Lettieri-Barbato, F. Tomei, A. Sancini, G. Morabito, and M. Serafini, “Effect of plant foods and beverages on plasma non-enzymatic antioxidant capacity in human subjects: a meta-analysis,” The British Journal of Nutrition, vol. 109, no. 9, pp. 1544–1556, 2013. View at Google Scholar
  395. I. Peluso and A. Raguzzini, “Salivary and urinary Total antioxidant capacity as biomarkers of oxidative stress in humans,” Pathology Research International, vol. 2016, Article ID 5480267, 14 pages, 2016. View at Publisher · View at Google Scholar · View at Scopus
  396. I. Peluso, A. Cavaliere, and M. Palmery, “Plasma total antioxidant capacity and peroxidation biomarkers in psoriasis,” Journal of Biomedical Science, vol. 23, no. 1, p. 52, 2016. View at Google Scholar
  397. S. Z. Bathaie, A. Shams, and F. Moghadas Zadeh, “Kermani, Crocin bleaching assay using purified di-gentiobiosyl Crocin (-crocin) from Iranian saffron,” Iranian Journal of Basic Medical Sciences, vol. 14, no. 5, pp. 399–406, 2011. View at Google Scholar
  398. R. Apak, K. Guclu, M. Ozyurek, B. Bektasoglu, and M. Bener, “Cupric ion reducing antioxidant capacity assay for antioxidants in human serum and for hydroxyl radical scavengers,” Methods in Molecular Biology, vol. 594, pp. 215–239, 2010. View at Google Scholar
  399. O. Erel, “A new automated colorimetric method for measuring total oxidant status,” Clinical Biochemistry, vol. 38, no. 12, pp. 1103–1111, 2005. View at Publisher · View at Google Scholar · View at Scopus
  400. G. Beretta, G. Aldini, R. M. Facino, R. M. Russell, N. I. Krinsky, and K. J. Yeum, “Total antioxidant performance: a validated fluorescence assay for the measurement of plasma oxidizability,” Analytical Biochemistry, vol. 354, no. 2, pp. 290–298, 2006. View at Publisher · View at Google Scholar · View at Scopus
  401. G. Aldini, K. J. Yeum, R. M. Russell, and N. I. Krinsky, “A method to measure the oxidizability of both the aqueous and lipid compartments of plasma,” Free Radical Biology & Medicine, vol. 31, no. 9, pp. 1043–1050, 2001. View at Publisher · View at Google Scholar · View at Scopus
  402. M. Takashima, M. Horie, M. Shichiri, Y. Hagihara, Y. Yoshida, and E. Niki, “Assessment of antioxidant capacity for scavenging free radicals in vitro: a rational basis and practical application,” Free Radical Biology & Medicine, vol. 52, no. 7, pp. 1242–1252, 2012. View at Publisher · View at Google Scholar · View at Scopus
  403. R. Amorati and L. Valgimigli, “Advantages and limitations of common testing methods for antioxidants,” Free Radical Research, vol. 49, no. 5, pp. 633–649, 2015. View at Publisher · View at Google Scholar · View at Scopus
  404. I. Pinchuk, H. Shoval, Y. Dotan, and D. Lichtenberg, “Evaluation of antioxidants: scope, limitations and relevance of assays,” Chemistry and Physics of Lipids, vol. 165, no. 6, pp. 638–647, 2012. View at Publisher · View at Google Scholar · View at Scopus
  405. C. G. Fraga, P. I. Oteiza, and M. Galleano, “In vitro measurements and interpretation of total antioxidant capacity,” Biochimica et Biophysica Acta, vol. 1840, no. 2, pp. 931–934, 2014. View at Google Scholar
  406. P. C. Hollman, A. Cassidy, B. Comte et al., “The biological relevance of direct antioxidant effects of polyphenols for cardiovascular health in humans is not established,” The Journal of Nutrition, vol. 141, no. 5, pp. 989S–1009S, 2011. View at Publisher · View at Google Scholar · View at Scopus
  407. G. Bartosz, “Non-enzymatic antioxidant capacity assays: limitations of use in biomedicine,” Free Radical Research, vol. 44, no. 7, pp. 711–720, 2010. View at Publisher · View at Google Scholar · View at Scopus
  408. D. Huang, B. Ou, and R. L. Prior, “The chemistry behind antioxidant capacity assays,” Journal of Agricultural and Food Chemistry, vol. 53, no. 6, pp. 1841–1856, 2005. View at Publisher · View at Google Scholar · View at Scopus
  409. L. M. Magalhaes, M. A. Segundo, S. Reis, and J. L. Lima, “Methodological aspects about in vitro evaluation of antioxidant properties,” Analytica Chimica Acta, vol. 613, no. 1, pp. 1–19, 2008. View at Publisher · View at Google Scholar · View at Scopus
  410. E. Niki, “Assessment of antioxidant capacity in vitro and in vivo,” Free Radical Biology & Medicine, vol. 49, no. 4, pp. 503–515, 2010. View at Publisher · View at Google Scholar · View at Scopus
  411. C. Lopez-Alarcon and A. Denicola, “Evaluating the antioxidant capacity of natural products: a review on chemical and cellular-based assays,” Analytica Chimica Acta, vol. 763, pp. 1–10, 2013. View at Publisher · View at Google Scholar · View at Scopus
  412. A. R. Collins, “Assays for oxidative stress and antioxidant status: applications to research into the biological effectiveness of polyphenols,” The American Journal of Clinical Nutrition, vol. 81, no. 1 Supplement, pp. 261S–267S, 2005. View at Google Scholar
  413. T. Petrosino and M. Serafini, “Antioxidant modulation of F2-isoprostanes in humans: a systematic review,” Critical Reviews in Food Science and Nutrition, vol. 54, no. 9, pp. 1202–1221, 2014. View at Publisher · View at Google Scholar · View at Scopus
  414. C. J. Carrión-García, E. J. Guerra-Hernandez, B. Garcia-Villanova, and E. Molina-Montes, “Non-enzymatic antioxidant capacity (NEAC) estimated by two different dietary assessment methods and its relationship with NEAC plasma levels,” European Journal of Nutrition, 2016, Epub ahead of print. View at Publisher · View at Google Scholar · View at Scopus
  415. K. S. De Bona, L. P. Belle, P. E. Bittencourt et al., “Erythrocytic enzymes and antioxidant status in people with type 2 diabetes: beneficial effect of Syzygium cumini leaf extract in vitro,” Diabetes Research and Clinical Practice, vol. 94, no. 1, pp. 84–90, 2011. View at Publisher · View at Google Scholar · View at Scopus
  416. S. Bhatia, R. Shukla, S. Venkata Madhu, J. Kaur Gambhir, and K. Madhava Prabhu, “Antioxidant status, lipid peroxidation and nitric oxide end products in patients of type 2 diabetes mellitus with nephropathy,” Clinical Biochemistry, vol. 36, no. 7, pp. 557–562, 2003. View at Publisher · View at Google Scholar · View at Scopus
  417. J. Kasznicki, M. Kosmalski, A. Sliwinska et al., “Evaluation of oxidative stress markers in pathogenesis of diabetic neuropathy,” Molecular Biology Reports, vol. 39, no. 9, pp. 8669–8678, 2012. View at Publisher · View at Google Scholar · View at Scopus
  418. V. Ramakrishna and R. Jailkhani, “Oxidative stress in non-insulin-dependent diabetes mellitus (NIDDM) patients,” Acta Diabetologica, vol. 45, no. 1, pp. 41–46, 2008. View at Publisher · View at Google Scholar · View at Scopus
  419. S. Merzouk, A. Hichami, S. Madani et al., “Antioxidant status and levels of different vitamins determined by high performance liquid chromatography in diabetic subjects with multiple complications,” General Physiology and Biophysics, vol. 22, no. 1, pp. 15–27, 2003. View at Google Scholar
  420. K. Kaviarasan, M. M. Arjunan, and K. V. Pugalendi, “Lipid profile, oxidant-antioxidant status and glycoprotein components in hyperlipidemic patients with/without diabetes,” Clinica Chimica Acta, vol. 362, no. 1-2, pp. 49–56, 2005. View at Publisher · View at Google Scholar · View at Scopus
  421. M. Jandric-Balen, V. Bozikov, D. Bistrovic et al., “Antioxidant enzymes activity in patients with peripheral vascular disease, with and without presence of diabetes mellitus,” Collegium Antropologicum, vol. 27, no. 2, pp. 735–743, 2003. View at Google Scholar
  422. K. Komosinska-Vassev, K. Olczyk, P. Olczyk, and K. Winsz-Szczotka, “Effects of metabolic control and vascular complications on indices of oxidative stress in type 2 diabetic patients,” Diabetes Research and Clinical Practice, vol. 68, no. 3, pp. 207–216, 2005. View at Publisher · View at Google Scholar · View at Scopus
  423. T. S. Chen, S. Y. Liou, and Y. L. Chang, “Supplementation of Emblica officinalis (Amla) extract reduces oxidative stress in uremic patients,” The American Journal of Chinese Medicine, vol. 37, no. 1, pp. 19–25, 2009. View at Google Scholar
  424. J. Maiuolo, F. Oppedisano, S. Gratteri, C. Muscoli, and V. Mollace, “Regulation of uric acid metabolism and excretion,” International Journal of Cardiology, vol. 213, pp. 8–14, 2016. View at Publisher · View at Google Scholar · View at Scopus
  425. W. Doehner, E. A. Jankowska, J. Springer, M. Lainscak, and S. D. Anker, “Uric acid and xanthine oxidase in heart failure - emerging data and therapeutic implications,” International Journal of Cardiology, vol. 213, pp. 15–19, 2016. View at Publisher · View at Google Scholar · View at Scopus
  426. M. Gliozzi, N. Malara, S. Muscoli, and V. Mollace, “The treatment of hyperuricemia,” International Journal of Cardiology, vol. 213, pp. 23–27, 2016. View at Publisher · View at Google Scholar · View at Scopus
  427. H. Benkhai, S. Lemanski, H. Below et al., “Can physical stress be measured in urine using the parameter antioxidative potential?” GMS Krankenhaushygiene interdisziplinär, vol. 5, no. 2, 2010. View at Publisher · View at Google Scholar
  428. N. Malliaraki, D. Mpliamplias, M. Kampa, K. Perakis, A. N. Margioris, and E. Castanas, “Total and corrected antioxidant capacity in hemodialyzed patients,” BMC Nephrology, vol. 4, p. 4, 2003. View at Google Scholar
  429. C. Campos, R. Guzman, E. Lopez-Fernandez, and A. Casado, “Urinary uric acid and antioxidant capacity in children and adults with Down syndrome,” Clinical Biochemistry, vol. 43, no. 3, pp. 228–233, 2010. View at Publisher · View at Google Scholar · View at Scopus
  430. D. Duplancic, L. Kukoc-Modun, D. Modun, and N. Radic, “Simple and rapid method for the determination of uric acid-independent antioxidant capacity,” Molecules, vol. 16, no. 8, pp. 7058–7068, 2011. View at Publisher · View at Google Scholar · View at Scopus
  431. A. Prymont-Przyminska, A. Zwolinska, A. Sarniak et al., “Consumption of strawberries on a daily basis increases the non-urate 2,2-diphenyl-1-picryl-hydrazyl (DPPH) radical scavenging activity of fasting plasma in healthy subjects,” Journal of Clinical Biochemistry and Nutrition, vol. 55, no. 1, pp. 48–55, 2014. View at Publisher · View at Google Scholar · View at Scopus
  432. T. Atsumi, S. Fujisawa, Y. Nakabayashi, T. Kawarai, T. Yasui, and K. Tonosaki, “Pleasant feeling from watching a comical video enhances free radical-scavenging capacity in human whole saliva,” Journal of Psychosomatic Research, vol. 56, no. 3, pp. 377–379, 2004. View at Publisher · View at Google Scholar · View at Scopus
  433. A. Vidovic, M. Grubisic-Ilic, D. Kozaric-Kovacic et al., “Exaggerated platelet reactivity to physiological agonists in war veterans with posttraumatic stress disorder,” Psychoneuroendocrinology, vol. 36, no. 2, pp. 161–172, 2011. View at Publisher · View at Google Scholar · View at Scopus
  434. A. Ghiselli, M. Serafini, F. Natella, and C. Scaccini, “Total antioxidant capacity as a tool to assess redox status: critical view and experimental data,” Free Radical Biology & Medicine, vol. 29, no. 11, pp. 1106–1114, 2000. View at Publisher · View at Google Scholar · View at Scopus
  435. W. Ammerlaan, J. P. Trezzi, P. Lescuyer, C. Mathay, K. Hiller, and F. Betsou, “Method validation for preparing serum and plasma samples from human blood for downstream proteomic, metabolomic, and circulating nucleic acid-based applications,” Biopreservation and Biobanking, vol. 12, no. 4, pp. 269–280, 2014. View at Publisher · View at Google Scholar · View at Scopus
  436. D. A. Granger, D. Cicchetti, F. A. Rogosch, L. C. Hibel, M. Teisl, and E. Flores, “Blood contamination in children's saliva: prevalence, stability, and impact on the measurement of salivary cortisol, testosterone, and dehydroepiandrosterone,” Psychoneuroendocrinology, vol. 32, no. 6, pp. 724–733, 2007. View at Publisher · View at Google Scholar · View at Scopus
  437. F. Veglia, G. Cighetti, M. De Franceschi et al., “Age- and gender-related oxidative status determined in healthy subjects by means of OXY-SCORE, a potential new comprehensive index,” Biomarkers, vol. 11, no. 6, pp. 562–573, 2006. View at Google Scholar
  438. C. Vassalle, “An easy and reliable automated method to estimate oxidative stress in the clinical setting,” Methods in Molecular Biology, vol. 477, pp. 31–39, 2008. View at Google Scholar
  439. C. Vassalle, C. Novembrino, S. Maffei et al., “Determinants of oxidative stress related to gender: relevance of age and smoking habit,” Clinical Chemistry and Laboratory Medicine, vol. 49, no. 9, pp. 1509–1513, 2011. View at Publisher · View at Google Scholar · View at Scopus
  440. C. Vassalle, R. Sciarrino, S. Bianchi, D. Battaglia, A. Mercuri, and S. Maffei, “Sex-related differences in association of oxidative stress status with coronary artery disease,” Fertility and Sterility, vol. 97, no. 2, pp. 414–419, 2012. View at Publisher · View at Google Scholar · View at Scopus
  441. F. Veglia, V. Cavalca, and E. Tremoli, “OXY-SCORE: a global index to improve evaluation of oxidative stress by combining pro- and antioxidant markers,” Methods in Molecular Biology, vol. 594, pp. 197–213, 2010. View at Google Scholar
  442. F. Veglia, J. P. Werba, E. Tremoli et al., “Assessment of oxidative stress in coronary artery bypass surgery: comparison between the global index OXY-SCORE and individual biomarkers,” Biomarkers, vol. 14, no. 7, pp. 465–472, 2009. View at Publisher · View at Google Scholar · View at Scopus
  443. M. Nishimura, A. Takaki, N. Tamaki et al., “Serum oxidative-anti-oxidative stress balance is dysregulated in patients with hepatitis C virus-related hepatocellular carcinoma,” Hepatology Research, vol. 43, no. 10, pp. 1078–1092, 2013. View at Publisher · View at Google Scholar · View at Scopus
  444. M. Terao, A. Takaki, T. Maruyama et al., “Serum oxidative/anti-oxidative stress balance is dysregulated in potentially pulmonary hypertensive patients with liver cirrhosis: a case control study,” Internal Medicine, vol. 54, no. 22, pp. 2815–2826, 2015. View at Publisher · View at Google Scholar · View at Scopus
  445. Y. Shimomura, A. Takaki, N. Wada et al., “The serum oxidative/anti-oxidative stress balance becomes dysregulated in patients with non-alcoholic steatohepatitis associated with hepatocellular carcinoma,” Internal Medicine, vol. 56, no. 3, pp. 243–251, 2017. View at Publisher · View at Google Scholar
  446. C. Novembrino, G. Cighetti, R. De Giuseppe et al., “Effects of encapsulated fruit and vegetable juice powder concentrates on oxidative status in heavy smokers,” Journal of the American College of Nutrition, vol. 30, no. 1, pp. 49–56, 2011. View at Google Scholar
  447. C. Vassalle, P. Piaggi, N. Weltman et al., “Innovative approach to interpret the variability of biomarkers after ultra-endurance exercise: the multifactorial analysis,” Biomarkers in Medicine, vol. 8, no. 6, pp. 881–891, 2014. View at Publisher · View at Google Scholar · View at Scopus
  448. L. Condezo-Hoyos, M. Rubio, S. M. Arribas et al., “A plasma oxidative stress global index in early stages of chronic venous insufficiency,” Journal of Vascular Surgery, vol. 57, no. 1, pp. 205–213, 2013. View at Publisher · View at Google Scholar · View at Scopus