Indian Journal of Clinical Biochemistry

, Volume 26, Issue 1, pp 28–31 | Cite as

Myeloperoxidase in Chronic Kidney Disease

  • A. Madhusudhana Rao
  • Usha Anand
  • C. V. Anand
Original Article


Numerous lines of evidence implicate a role of myeloperoxidase (MPO) in the pathogenesis of cardiovascular disease (CVD). It is a well accepted fact that patients with chronic kidney disease (CKD) are at an increased risk for CVD. MPO is a pro-oxidant enzyme which could be involved in the increased susceptibility of these patients to CVD. Hence, the levels of plasma MPO was determined in healthy controls as well as in patients with CKD [stratified with the level of their kidney failure as CKD stages II–V (end stage renal disease)]. Plasma MPO was assayed by a spectrophotometric method. Serum urea and creatinine were estimated on a clinical chemistry analyzer using standard laboratory procedures. The mean plasma MPO levels were significantly lower with advancing stages of renal failure (P < 0.001). There was a positive correlation between MPO and GFR (r = +0.89, P < 0.001) and a negative correlation with urea (r = −0.85, P < 0.001) and creatinine (r = −0.82, P < 0.001). While an inverse association was observed between plasma MPO and urea in CKD patients, such an association was not observed in control subjects (P = 0.43). In conclusion, the decline in plasma MPO levels may be due to the inhibitory effect of uraemic toxins on the enzyme.


Chronic kidney disease MPO-hydrogen peroxide–chloride system Oxidative stress Uraemic toxins Cardiovascular disease 


  1. 1.
    Hampton MB, Kettle AJ, Winterbourn CC. Inside the neutrophil phagosome: oxidants, myeloperoxidase, and bacterial killing. Blood. 1998;92:3007–17.PubMedGoogle Scholar
  2. 2.
    Podrez EA, Abu-soud HM, Hazen SL. Myeloperoxidase generated oxidants and atherosclerosis. Free Radic Biol Med. 2000;28:1717–25.CrossRefPubMedGoogle Scholar
  3. 3.
    Brown KE, Brunt EM, Heinecke JW. Immunohistochemical detection of myeloperoxidase and its oxidation products in Kupffer cells of human liver. Am J Pathol. 2001;159:2081–8.CrossRefPubMedGoogle Scholar
  4. 4.
    Winterbourn CC, Kettle AJ. Biomarkers of myeloperoxidase derived hypo chlorous acid. Free Radic Biol Med. 2000;29:403–9.CrossRefPubMedGoogle Scholar
  5. 5.
    Heinecke JW. Mechanisms of oxidative damage by myeloperoxidase in atherosclerosis and other inflammatory disorders. J Lab Clin Med. 1999;133:321–5.CrossRefPubMedGoogle Scholar
  6. 6.
    Vita JA, Brennan ML, Gokce N, Mann SA, Goormastic M, Shishehbor MH, et al. Serum myeloperoxidase levels independently predict endothelial dysfunction in humans. Circulation. 2004;110:1134–9.CrossRefPubMedGoogle Scholar
  7. 7.
    Brennan ML, Penn MS, Vn Lente FV, Nambi V, Shishehbor MH, Aviles RJ. Prognostic value of myeloperoxidase in patients with chest pain. N Engl J Med. 2003;349:1595–604.CrossRefPubMedGoogle Scholar
  8. 8.
    Levey AS, Coresh J, Balk E, Kausz AT, Levin A, Steffes MW, et al. National Kidney Foundation practice guidelines for chronic kidney disease: evaluation, classification, and stratification. Ann Intern Med. 2003;139:137–47.PubMedGoogle Scholar
  9. 9.
    Levey AS, Coresh J, Greene T et al. Expressing the MDRD study equation for estimating GFR with IDMS traceable (gold standard) serum creatinine values. J Am Soc Nephrol 2005;16:69A.Google Scholar
  10. 10.
    Krueger AJ, Yang JJ, Roy TA, Robbins DJ, Mackerer CR. An automated myeloperoxidase assay. Clin Chem. 1990;36:158.PubMedGoogle Scholar
  11. 11.
    Arsenault BJ, Stroes ES, Boekholdt SM. Is myeloperoxidase a useful marker to predict the risk of cardiovascular events? Curr Cardiovasc Risk Rep. 2009;3:137–43.CrossRefGoogle Scholar
  12. 12.
    Weiner DE, Tighiourat H, Amin MG, Stark PC, Macleod B, Griffith JL, et al. Chronic kidney disease as a risk factor for cardiovascular disease and all-cause mortality: a pooled analysis of community-based studies. J Am Soc Nephrol. 2004;15:1307–15.CrossRefPubMedGoogle Scholar
  13. 13.
    Malle E, Buch T, Grone HJ. Myeloperoxidase in kidney disease. Kidney Int. 2003;64:1956–67.CrossRefPubMedGoogle Scholar
  14. 14.
    Maruyama Y, Lindholm B, Stenvinkel P. Inflammation and oxidative stress in ESRD—the role of myeloperoxidase. J Nephrol. 2004;17(Suppl 8):72–6.Google Scholar
  15. 15.
    Capeillere BC, Gausson V, Nguyen AT, Descamps LB, Drueke T, Witko SV. Respective role of uraemic toxins and myeloperoxidase in the uraemic state. Nephrol Dial Transplant. 2006;21:1555–63.CrossRefGoogle Scholar
  16. 16.
    Slungaard A, Mahoney JR. Thiocyanate is the major substrate for eosinophil peroxidase in physiologic fluids. J Biol Chem. 1991;266:4903–10.PubMedGoogle Scholar
  17. 17.
    Dirnhuber P, Schutz F. The isomeric transformation of urea into ammonium cyanate in aqueous solutions. Biochem J. 1948;42:628–32.Google Scholar
  18. 18.
    Mingwei Q, John WE, Simon PW. Cyanate-mediated inhibition of neutrophil myeloperoxidase activity. Biochem J. 1997;326:159–66.Google Scholar

Copyright information

© Association of Clinical Biochemists of India 2010

Authors and Affiliations

  1. 1.Department of BiochemistryPSG Institute of Medical Sciences and ResearchCoimbatoreIndia

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