Table of Contents
ISRN Inflammation
Volume 2012, Article ID 260453, 7 pages
http://dx.doi.org/10.5402/2012/260453
Research Article

The Importance of Myeloperoxidase in Apocynin-Mediated NADPH Oxidase Inhibition

1Departamento de Química, Faculdade de Ciências, Universidade Estadual Paulista UNESP, CEP 17033-360, Bauru, SP, Brazil
2Centro de Investigação em Pediatria (CIPED), Faculdade de Ciências Médicas, Universidade Estadual de Campinas, CEP 13083-887, Campinas, SP, Brazil
3Instituto de Ciências Biomédicas, Universidade de São Paulo, CEP 05508-000, São Paulo, SP, Brazil

Received 30 January 2012; Accepted 28 February 2012

Academic Editors: E. Kurutas and B. Ryffel

Copyright © 2012 Ana Carolina de Almeida 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. K. Cathcart, “Regulation of superoxide anion production by NADPH oxidase in monocytes/macrophages: contributions to atherosclerosis,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 24, no. 1, pp. 23–28, 2004. View at Publisher · View at Google Scholar · View at Scopus
  2. Y. Groemping and K. Rittinger, “Activation and assembly of the NADPH oxidase: a structural perspective,” Biochemical Journal, vol. 386, no. 3, pp. 401–416, 2005. View at Publisher · View at Google Scholar · View at Scopus
  3. M. Ushio-Fukai, “Compartmentalization of redox signaling through NaDPH oxidase-derived rOS,” Antioxidants and Redox Signaling, vol. 11, no. 6, pp. 1289–1299, 2009. View at Publisher · View at Google Scholar · View at Scopus
  4. G. Y. Lam, J. Huang, and J. H. Brumell, “The many roles of NOX2 NADPH oxidase-derived ROS in immunity,” Seminars in Immunopathology, pp. 1–16, 2010. View at Publisher · View at Google Scholar · View at Scopus
  5. 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
  6. J. Stolk, T. J. Hiltermann, J. H. Dijkman, and A. J. Verhoeven, “Characteristics of the inhibition of NADPH oxidase activation in neutrophils by apocynin, a methoxy-substituted catechol,” American Journal of Respiratory Cell and Molecular Biology, vol. 11, no. 1, pp. 95–102, 1994. View at Google Scholar · View at Scopus
  7. F. P. J. G. Lafeber, C. J. Beukelman, E. Van Den Worm et al., “Apocynin, a plant-derived, cartilage-saving drug, might be useful in the treatment of rheumatoid arthritis,” Rheumatology, vol. 38, no. 11, pp. 1088–1093, 1999. View at Google Scholar · View at Scopus
  8. Y. Zhang, M. M. K. Chan, M. C. Andrews et al., “Apocynin but not allopurinol prevents and reverses adrenocorticotropic hormone-induced hypertension in the rat,” American Journal of Hypertension, vol. 18, no. 7, pp. 910–916, 2005. View at Publisher · View at Google Scholar · View at Scopus
  9. D. K. Johnson, K. J. Schillinger, D. M. Kwait et al., “Inhibition of NADPH oxidase activation in endothelial cells by ortho-methoxy-substituted catechols,” Endothelium, vol. 9, no. 3, pp. 191–203, 2002. View at Publisher · View at Google Scholar · View at Scopus
  10. M. Vejrazka, R. Micek, and S. Stipek, “Apocynin inhibits NADPH oxidase in phagocytes but stimulates ROS production in non-phagocytic cells,” Biochimica et Biophysica Acta, vol. 1722, no. 2, pp. 143–147, 2005. View at Publisher · View at Google Scholar
  11. C. Riganti, C. Costamagna, A. Bosia, and D. Ghigo, “The NADPH oxidase inhibitor apocynin (acetovanillone) induces oxidative stress,” Toxicology and Applied Pharmacology, vol. 212, no. 3, pp. 179–187, 2006. View at Publisher · View at Google Scholar · View at Scopus
  12. S. Heumüller, S. Wind, E. Barbosa-Sicard et al., “Apocynin is not an inhibitor of vascular NADPH oxidases but an antioxidant,” Hypertension, vol. 51, no. 2, pp. 211–217, 2008. View at Publisher · View at Google Scholar · View at Scopus
  13. Y. Steffen, C. Gruber, T. Schewe, and H. Sies, “Mono-O-methylated flavanols and other flavonoids as inhibitors of endothelial NADPH oxidase,” Archives of Biochemistry and Biophysics, vol. 469, no. 2, pp. 209–219, 2008. View at Publisher · View at Google Scholar · View at Scopus
  14. S. S. Barbieri, V. Cavalca, S. Eligini et al., “Apocynin prevents cyclooxygenase 2 expression in human monocytes through NADPH oxidase and glutathione redox-dependent mechanisms,” Free Radical Biology and Medicine, vol. 37, no. 2, pp. 156–165, 2004. View at Publisher · View at Google Scholar · View at Scopus
  15. F. Engels, B. F. Renirie, B. A. 'T Hart, R. P. Labadie, and F. P. Nijkamp, “Effects of apocynin, a drug isolated from the roots of Picrorhiza kurroa, on arachidonic acid metabolism,” FEBS Letters, vol. 305, no. 3, pp. 254–256, 1992. View at Publisher · View at Google Scholar · View at Scopus
  16. A. C. De Almeida, O. C. Marques, C. Arslanian, A. Condino-Neto, and V. F. Ximenes, “4-Fluoro-2-methoxyphenol, an apocynin analog with enhanced inhibitory effect on leukocyte oxidant production and phagocytosis,” European Journal of Pharmacology, vol. 660, no. 2-3, pp. 445–453, 2011. View at Publisher · View at Google Scholar
  17. R. Mazor, O. Itzhaki, S. Sela et al., “Tumor necrosis factor-α: a possible priming agent for the polymorphonuclear leukocyte-reduced nicotinamide-adenine dinucleotide phosphate oxidase in hypertension,” Hypertension, vol. 55, no. 2, pp. 353–362, 2010. View at Publisher · View at Google Scholar · View at Scopus
  18. V. F. Ximenes, M. P. P. Kanegae, S. R. Rissato, and M. S. Galhiane, “The oxidation of apocynin catalyzed by myeloperoxidase: proposal for NADPH oxidase inhibition,” Archives of Biochemistry and Biophysics, vol. 457, no. 2, pp. 134–141, 2007. View at Publisher · View at Google Scholar · View at Scopus
  19. C. Brochetta, M. G. Perrotta, A. Jeromin et al., “Identification and Subcellular Localization of Neuronal Calcium Sensor-1 (NCS-1) in Human Neutrophils and HL-60 Cells,” Inflammation, vol. 27, no. 6, pp. 361–372, 2003. View at Publisher · View at Google Scholar · View at Scopus
  20. H. Oh, B. Siano, and S. Diamond, “Neutrophil isolation protocol,” Journal of Visualized Experiments, no. 17, 2008. View at Google Scholar · View at Scopus
  21. R. E. Aldridge, T. Chan, C. J. Van Dalen et al., “Eosinophil peroxidase produces hypobromous acid in the airways of stable asthmatics,” Free Radical Biology and Medicine, vol. 33, no. 6, pp. 847–856, 2002. View at Publisher · View at Google Scholar · View at Scopus
  22. T. MUnzel, I. B. Afanas'ev, A. L. Kleschyov, and D. G. Harrison, “Detection of superoxide in vascular tissue,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 22, no. 11, pp. 1761–1768, 2002. View at Publisher · View at Google Scholar · View at Scopus
  23. D. Montgomery, Design and Analysis of Experiments, John Wiley & Sons, New York, NY, USA, 1991.
  24. J. P. Uetrecht, “Myeloperoxidase as a generator of drug free radicals.,” Biochemical Society symposium, vol. 61, pp. 163–170, 1995. View at Google Scholar · View at Scopus
  25. B. S. van der Veen, M. P. J. de Winther, and P. Heeringa, “Myeloperoxidase: Molecular mechanisms of action and their relevance to human health and disease,” Antioxidants and Redox Signaling, vol. 11, no. 11, pp. 2899–2937, 2009. View at Publisher · View at Google Scholar · View at Scopus
  26. M. J. Davies, “Myeloperoxidase-derived oxidation: mechanisms of biological damage and its prevention,” Journal of Clinical Biochemistry and Nutrition, vol. 48, no. 1, pp. 8–19, 2011. View at Publisher · View at Google Scholar
  27. L. R. G. Castor, K. A. Locatelli, and V. F. Ximenes, “Pro-oxidant activity of apocynin radical,” Free Radical Biology and Medicine, vol. 48, no. 12, pp. 1636–1643, 2010. View at Publisher · View at Google Scholar · View at Scopus
  28. M. Mora-Pale, M. Weïwer, J. Yu, R. J. Linhardt, and J. S. Dordick, “Inhibition of human vascular NADPH oxidase by apocynin derived oligophenols,” Bioorganic and Medicinal Chemistry, vol. 17, no. 14, pp. 5146–5152, 2009. View at Publisher · View at Google Scholar · View at Scopus
  29. C. Panousis, A. J. Kettle, and D. R. Phillips, “Myeloperoxidase oxidizes mitoxantrone to metabolites which bind covalently to DNA and RNA,” Anti-Cancer Drug Design, vol. 10, no. 8, pp. 593–605, 1995. View at Google Scholar · View at Scopus
  30. A. Davalos, G. de La Peña, C. C. Sánchez-Martín, M. Teresa Guerra, B. Bartolom, and M. A. Lasunción, “Effects of red grape juice polyphenols in NADPH oxidase subunit expression in human neutrophils and mononuclear blood cells,” British Journal of Nutrition, vol. 102, no. 8, pp. 1125–1135, 2009. View at Publisher · View at Google Scholar · View at Scopus
  31. M. Yang, M. D. Chordia, F. Li, T. Huang, J. Linden, and T. L. MacDonald, “Neutrophil- and myeloperoxidase-mediated metabolism of reduced nimesulide: Evidence for bioactivation,” Chemical Research in Toxicology, vol. 23, no. 11, pp. 1691–1700, 2010. View at Publisher · View at Google Scholar · View at Scopus
  32. K. J. Reszka, B. A. Wagner, L. M. Teesch, B. E. Britigan, D. R. Spitz, and C. P. Burns, “Inactivation of anthracyclines by cellular peroxidase,” Cancer Research, vol. 65, no. 14, pp. 6346–6353, 2005. View at Publisher · View at Google Scholar · View at Scopus
  33. N. K. Dutta, P. H. Marker, and N. R. Rao, “Berberine in toxin-induced experimental cholera,” British Journal of Pharmacology, vol. 44, no. 1, pp. 153–159, 1972. View at Google Scholar · View at Scopus
  34. M. P. Kanegae, A. Condino-Neto, L. A. Pedroza et al., “Diapocynin versus apocynin as pretranscriptional inhibitors of NADPH oxidase and cytokine production by peripheral blood mononuclear cells,” Biochemical and Biophysical Research Communications, vol. 393, no. 3, pp. 551–554, 2010. View at Google Scholar
  35. P. A. R. Juliet, T. Hayashi, S. Daigo et al., “Combined effect of testosterone and apocynin on nitric oxide and superoxide production in PMA-differentiated THP-1 cells,” Biochimica et Biophysica Acta, vol. 1693, no. 3, pp. 185–191, 2004. View at Publisher · View at Google Scholar · View at Scopus