Table of Contents Author Guidelines Submit a Manuscript
Table of Contents Alerts

To receive news and publication updates for Journal of Immunology Research, enter your email address in the box below.

Journal of Immunology Research
Volume 2019, Article ID 4783018, 10 pages
https://doi.org/10.1155/2019/4783018
Research Article

Myeloperoxidase and Eosinophil Peroxidase Inhibit Endotoxin Activity and Increase Mouse Survival in a Lipopolysaccharide Lethal Dose 90% Model

Robert C. Allen,1 Mary L. Henery,2 John C. Allen,2 Roger J. Hawks,3 and Jackson T. Stephens Jr.2

1Department of Pathology, Creighton University School of Medicine, Omaha, NE 68124, USA
2Exoxemis, Inc., Omaha, NE 68110, USA
3Concord Biosciences, LLC, Concord, OH 44077, USA

Correspondence should be addressed to Robert C. Allen; ude.nothgierc@nellatrebor

Received 25 February 2019; Revised 21 July 2019; Accepted 20 August 2019; Published 30 September 2019

Academic Editor: Douglas C. Hooper

Copyright © 2019 Robert C. Allen 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. K. Agner, “Studies of myeloperoxidase activity,” Acta Chemica Scandinavica, vol. 17, pp. S332–S338, 1963. View at Google Scholar
  2. M. Zederbauer, P. G. Furtmuller, S. Brogioni, C. Jakopitsch, G. Smulevich, and C. Obinger, “Heme to protein linkages in mammalian peroxidases: impact on spectroscopic, redox and catalytic properties,” Natural Product Reports, vol. 24, no. 3, pp. 571–584, 2007. View at Publisher · View at Google Scholar · View at Scopus
  3. M. G. Carlson, C. G. Peterson, and P. Venge, “Human eosinophil peroxidase: purification and characterization,” Journal of Immunology, vol. 134, no. 3, pp. 1875–1879, 1985. View at Google Scholar
  4. K. Sakamaki, M. Tomonaga, K. Tsukui, and S. Nagata, “Molecular cloning and characterization of a chromosomal gene for human eosinophil peroxidase,” The Journal of Biological Chemistry, vol. 264, no. 28, pp. 16828–16836, 1989. View at Google Scholar
  5. R. L. Olsen and C. Little, “Purification and some properties of myeloperoxidase and eosinophil peroxidase from human blood,” The Biochemical Journal, vol. 209, no. 3, pp. 781–787, 1983. View at Publisher · View at Google Scholar · View at Scopus
  6. B. G. J. M. Bolscher, H. Plat, and R. Wever, “Some properties of human eosinophil peroxidase, a comparison with other peroxidases,” Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, vol. 784, no. 2-3, pp. 177–186, 1984. View at Publisher · View at Google Scholar · View at Scopus
  7. S. J. Klebanoff, “Myeloperoxidase-halide-hydrogen peroxide antibacterial system,” Journal of Bacteriology, vol. 95, no. 6, pp. 2131–2138, 1968. View at Google Scholar
  8. E. C. Jong, W. R. Henderson, and S. J. Klebanoff, “Bactericidal activity of eosinophil peroxidase,” Journal of Immunology, vol. 124, no. 3, pp. 1378–1382, 1980. View at Google Scholar
  9. J. Schultz and K. Kaminker, “Myeloperoxidase of the leucocyte of normal human blood. I. Content and localization,” Archives of Biochemistry and Biophysics, vol. 96, no. 3, pp. 465–467, 1962. View at Publisher · View at Google Scholar · View at Scopus
  10. R. C. Allen, P. R. Stevens, T. H. Price, G. S. Chatta, and D. C. Dale, “In Vivo Effects of Recombinant Human Granulocyte Colony-Stimulating Factor on Neutrophil Oxidative Functions in Normal Human Volunteers,” The Journal of Infectious Diseases, vol. 175, no. 5, pp. 1184–1192, 1997. View at Publisher · View at Google Scholar · View at Scopus
  11. K. Agner, “Detoxicating effect of verdoperoxidase on toxins,” Nature, vol. 159, no. 4034, pp. 271-272, 1947. View at Publisher · View at Google Scholar · View at Scopus
  12. W. Ooi, H. G. Levine, J. T. LaMont, and R. A. Clark, “Inactivation of Clostridium difficile cytotoxin by the neutrophil myeloperoxidase system,” The Journal of Infectious Diseases, vol. 149, no. 2, pp. 215–219, 1984. View at Publisher · View at Google Scholar · View at Scopus
  13. K. Agner, “Studies on peroxidative detoxification of purified diphtheria toxin,” The Journal of Experimental Medicine, vol. 92, no. 4, pp. 337–347, 1950. View at Publisher · View at Google Scholar · View at Scopus
  14. C. Galanos, E. T. Rietschel, O. Luderitz, O. Westphal, Y. B. Kim, and D. W. Watson, “Biological activities of lipid A complexed with bovine-serum albumin,” European Journal of Biochemistry, vol. 31, no. 2, pp. 230–233, 1972. View at Publisher · View at Google Scholar · View at Scopus
  15. R. C. Allen and J. T. Stephens Jr., “Myeloperoxidase selectively binds and selectively kills microbes,” Infection and Immunity, vol. 79, no. 1, pp. 474–485, 2011. View at Publisher · View at Google Scholar · View at Scopus
  16. C. R. Raetz, R. J. Ulevitch, S. D. Wright, C. H. Sibley, A. Ding, and C. F. Nathan, “Gram-negative endotoxin: an extraordinary lipid with profound effects on eukaryotic signal transduction,” The FASEB Journal, vol. 5, no. 12, pp. 2652–2660, 1991. View at Publisher · View at Google Scholar
  17. M. Luchi and D. C. Morrison, “Comparable endotoxic properties of lipopolysaccharides are manifest in diverse clinical isolates of Gram-negative bacteria,” Infection and Immunity, vol. 68, no. 4, pp. 1899–1904, 2000. View at Publisher · View at Google Scholar · View at Scopus
  18. X. Wang and P. J. Quinn, “Endotoxins: lipopolysaccharides of Gram-negative bacteria,” Sub-Cellular Biochemistry, vol. 53, pp. 3–25, 2010. View at Publisher · View at Google Scholar · View at Scopus
  19. J. P. Gaut, G. C. Yeh, H. D. Tran et al., “Neutrophils employ the myeloperoxidase system to generate antimicrobial brominating and chlorinating oxidants during sepsis,” Proceedings of the National Academy of Sciences of the United States of America, vol. 98, no. 21, pp. 11961–11966, 2001. View at Publisher · View at Google Scholar · View at Scopus
  20. L. L. Reber, C. M. Gillis, P. Starkl et al., “Neutrophil myeloperoxidase diminishes the toxic effects and mortality induced by lipopolysaccharide,” The Journal of Experimental Medicine, vol. 214, no. 5, pp. 1249–1258, 2017. View at Publisher · View at Google Scholar · View at Scopus
  21. S. J. Klebanoff, A. M. Waltersdorph, and H. Rosen, “[52] Antimicrobial activity of myeloperoxidase,” in Methods in Enzymology, vol. 105, Elsevier, 1984. View at Publisher · View at Google Scholar · View at Scopus
  22. H. U. Bergmeyer and K. Gawehn, Methods of enzymatic analysis, vol. 1, Academic press, 1974.
  23. J. C. Hurley, “Endotoxemia: methods of detection and clinical correlates,” Clinical Microbiology Reviews, vol. 8, no. 2, pp. 268–292, 1995. View at Publisher · View at Google Scholar
  24. N. O. Solum, “The coagulogen of Limulus polyphemus hemocytes. A comparison of the clotted and non-clotted forms of the molecule,” Thrombosis Research, vol. 2, no. 1, pp. 55–69, 1973. View at Publisher · View at Google Scholar · View at Scopus
  25. P. A. Tomasulo, J. Levin, P. A. Murphy, and J. A. Winkelstein, “Biological activities of tritiated endotoxins: correlation of the Limulus lysate assay with rabbit pyrogen and complement-activation assays for endotoxin,” Translational Research, vol. 89, no. 2, pp. 308–315, 1977. View at Google Scholar
  26. J. Neter and W. Wasserman, Applied Linear Statistical Models: Regression, Analysis of Variance, and Experimental Designs, Richard D. Irwin. Inc., Homewood, IL, USA, 1974.
  27. N. Mantel, “Evaluation of survival data and two new rank order statistics arising in its consideration,” Cancer Chemotherapy Reports, vol. 50, no. 3, pp. 163–170, 1966. View at Google Scholar
  28. N. Breslow, “A generalized Kruskal-Wallis test for comparing K samples subject to unequal patterns of censorship,” Biometrika, vol. 57, no. 3, pp. 579–594, 1970. View at Publisher · View at Google Scholar · View at Scopus
  29. R. E. Tarone and J. Ware, “On distribution-free tests for equality of survival distributions,” Biometrika, vol. 64, no. 1, pp. 156–160, 1977. View at Publisher · View at Google Scholar · View at Scopus
  30. G. A. Denys, P. Grover, P. O'Hanley, and J. T. Stephens Jr., “In vitro antibacterial activity of E-101 solution, a novel myeloperoxidase-mediated antimicrobial, against Gram-positive and Gram-negative pathogens,” The Journal of Antimicrobial Chemotherapy, vol. 66, no. 2, pp. 335–342, 2011. View at Publisher · View at Google Scholar · View at Scopus
  31. G. A. Denys, N. C. Devoe, P. Gudis, M. May, R. C. Allen, and J. T. Stephens Jr., “Mechanism of Microbicidal Action of E-101 Solution, a Myeloperoxidase-Mediated Antimicrobial, and Its Oxidative Products,” Infection and Immunity, vol. 87, no. 7, 2019. View at Publisher · View at Google Scholar
  32. R. C. Allen and J. T. Stephens Jr., “Role of lactic acid bacteria-myeloperoxidase synergy in establishing and maintaining the normal flora in man,” Food and Nutrition Sciences, vol. 04, no. 11, pp. 67–72, 2013. View at Publisher · View at Google Scholar
  33. R. C. Allen and J. T. Stephens Jr., “Reduced-oxidized difference spectral analysis and chemiluminescence-based Scatchard analysis demonstrate selective binding of myeloperoxidase to microbes,” Luminescence, vol. 26, no. 3, pp. 208–213, 2011. View at Publisher · View at Google Scholar · View at Scopus
  34. R. C. Allen and J. T. Stephens Jr., “Phagocyte and extra-phagocyte myeloperoxidase-mediated microbicidal action,” in Science Against Microbial Pathogens: Communicating Current Research and Technological Advances, M.-V. A. Badajoz, Ed., Formatex Res. Ctr., 2011. View at Google Scholar