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Zymogram profiling of myeloperoxidase in association with increased risk of infection susceptibility in diabetic foot ulcer

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Abstract

An increase in blood glucose level can lead to altered immunological response of the body and increased infection susceptibility in diabetic condition. This condition along with the variation in the oxidant-antioxidant status can further lead to impaired wound healing. Myeloperoxidase (MPO) is one of the key enzymes involved in oxidative stress and phagocytosis. The main focus of this study was on the prevalence of isozymes of MPO in diabetic foot ulcer condition. Prior to the zymogram studies, the variations in leukocyte MPO activity in diabetic patients with and without foot infection were analysed. The MPO activity in diabetic foot ulcer patients was elevated than that of diabetic patients without foot ulcer complications, but the levels were not up to the MPO levels of the controls. The difference in banding pattern was observed in native PAGE analysis of MPO enzyme isolated from diabetic foot ulcer patients compared to diabetic and non-diabetic control groups. The multiple isozymic bands observed in diabetic foot ulcer condition were unique from that of diabetic patients without complication and normal healthy individuals.

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References

  1. Arnhold J. Properties, functions, and secretion of human myeloperoxidase. Biochemistry Biokhimiia. 2004;69(1):4–9.

    Article  CAS  PubMed  Google Scholar 

  2. Matheson NR, Wong PS, Travis J. Isolation and properties of human neutrophil myeloperoxidase. Biochemistry. 1981;20(2):325–30.

    Article  CAS  PubMed  Google Scholar 

  3. Marchetti C, Patriarca P, Solero GP, Baralle FE, Romano M. Genetic characterization of myeloperoxidase deficiency in Italy. Hum Mutat. 2004;23(5):496–505.

    Article  CAS  PubMed  Google Scholar 

  4. Kutter D, Devaquet P, Vanderstocken G, Paulus JM, Marchal V, Gothot A. Consequences of total and subtotal myeloperoxidase deficiency: risk or benefit? Acta Haematol. 2000;104(1):10–5.

    Article  CAS  PubMed  Google Scholar 

  5. Unubol M, Yavasoglu I, Kacar F, Guney E, Omurlu IK, Ture M, Kadikoylu G, Bolaman Z. Relationship between glycemic control and histochemical myeloperoxidase activity in neutrophils in patients with type 2 diabetes. Diabetol Metab Syndr. 2015;7(1):1–7.

    Article  Google Scholar 

  6. Klebanoff SJ, Kettle AJ, Rosen H, Winterbourn CC, Nauseef WM. Myeloperoxidase: a front-line defender against phagocytosed microorganisms. J Leukoc Biol. 2013;93(2):185–98.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  7. Miller LS, Cho JS. Immunity against Staphylococcus aureus cutaneous infections. Nat Rev Immunol. 2011;11(8):505–18.

    Article  CAS  PubMed  Google Scholar 

  8. Cech P, Stalder H, Widmann JJ, Rohner A, Miescher PA. Leukocyte myeloperoxidase deficiency and diabetes mellitus associated with Candida albicans liver abscess. Am J Med. 1979;66(1):149–53.

    Article  CAS  PubMed  Google Scholar 

  9. Bradley PP, Priebat DA, Christensen RD, Rothstein G. Measurement of cutaneous inflammation: estimation of neutrophil content with an enzyme marker. J Invest Dermatol. 1982;78(3):206–9.

    Article  CAS  PubMed  Google Scholar 

  10. Klebanoff SJ. Myeloperoxidase: friend and foe. J Leukoc Biol. 2005;77(5):598–625.

    Article  CAS  PubMed  Google Scholar 

  11. Pendsey S. Understanding diabetic foot. Int J Diab Dev Ctries. 2010;30(2):75–9.

    Article  Google Scholar 

  12. American Diabetes A. Standards of medical care in diabetes—2014. Diabetes Care. 2014;37(Suppl 1):S14–80.

    Article  Google Scholar 

  13. Taketa K. A tetrazolium method for peroxidase staining: application to the antibody-affinity blotting of α-fetoprotein separated by lectin affinity electrophoresis. Electrophoresis. 1987;8(9):409–14.

    Article  CAS  Google Scholar 

  14. Strauven TA, Armstrong D, James GT, Austin JH. Separation of leukocyte peroxidase isoenzymes by agarose-acrylamide disc electrophoresis. Age. 1978;1(3):111–6.

    Article  CAS  Google Scholar 

  15. Podrez EA, Abu-Soud HM, Hazen SL. Myeloperoxidase-generated oxidants and atherosclerosis. Free Radic Biol Med. 2000;28(12):1717–25.

    Article  CAS  PubMed  Google Scholar 

  16. Park YJ, Park G, Lee SH, Jang SJ, Moon DS, Park CY, Chung CH, Cha JH, Lee BR, Choi YH. Myeloperoxidase (MPO) isozymes of normal neutrophils from normal persons and reactive neutrophils from patients with neutrophilia; using 10 % native PAGE and activity stain for MPO. The Korean Journal of Hematology. 2003;38(1):48–54.

    Google Scholar 

  17. Loria V, Dato I, Graziani F, Biasucci LM. Myeloperoxidase: a new biomarker of inflammation in ischemic heart disease and acute coronary syndromes. Mediat Inflamm. 2008;2008:135625.

    Article  Google Scholar 

  18. Uchimura K, Nagasaka A, Hayashi R, Makino M, Nagata M, Kakizawa H, Kobayashi T, Fujiwara K, Kato T, Iwase K, et al. Changes in superoxide dismutase activities and concentrations and myeloperoxidase activities in leukocytes from patients with diabetes mellitus. J Diabetes Complicat. 1999;13(5–6):264–70.

    Article  CAS  PubMed  Google Scholar 

  19. Suchithra TV, Zuhara KF. Myeloperoxidase activity in infection complicated and uninfected diabetic patients. Ind J Biochem Biophys. 2008;45(3):179–83.

    CAS  Google Scholar 

  20. Paumann-Page M, Furtmuller PG, Hofbauer S, Paton LN, Obinger C, Kettle AJ. Inactivation of human myeloperoxidase by hydrogen peroxide. Arch Biochem Biophys. 2013;539(1):51–62.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  21. Nauseef WM, McCormick SJ, Clark RA. Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase. J Biol Chem. 1995;270(9):4741–7.

    Article  CAS  PubMed  Google Scholar 

  22. Raven E, Dunford B: Chapter 12. Myeloperoxidase: structure and function of the green heme peroxidase of neutrophils. In: Heme Peroxidases. Royal Society of Chemistry; 2015: 272–308.

  23. Otto NM, Schindler R, Lun A, Boenisch O, Frei U, Oppert M. Hyperosmotic stress enhances cytokine production and decreases phagocytosis in vitro. Crit Care. 2008;12(4):R107.

    Article  PubMed  PubMed Central  Google Scholar 

  24. Jafar N, Edriss H, Nugent K. The effect of short-term hyperglycemia on the innate immune system. Am J Med Sci. 2016;351(2):201–11.

    Article  PubMed  Google Scholar 

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Correspondence to T. V. Suchithra.

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Funding

This study was funded by the Faculty research grant of NITC Calicut (Sanction Order No. NITC/Dean (C&SR)/FRG10/0113).

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The authors declare that they have no conflict of interest.

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All procedures performed in studies involving human participants were in accordance with the ethical standards of the institutional and/or national research committee and with the 1964 Helsinki declaration and its later amendments or comparable ethical standards.

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Informed consent was obtained from all individual participants included in the study.

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Mathew, S.M., Suchithra, T.V. Zymogram profiling of myeloperoxidase in association with increased risk of infection susceptibility in diabetic foot ulcer. Int J Diabetes Dev Ctries 37, 459–463 (2017). https://doi.org/10.1007/s13410-016-0518-1

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  • DOI: https://doi.org/10.1007/s13410-016-0518-1

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