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Licensed Unlicensed Requires Authentication Published by De Gruyter April 18, 2016

One more health benefit of blood donation: reduces acute-phase reactants, oxidants and increases antioxidant capacity

  • Muharrem Yunce EMAIL logo , Husamettin Erdamar , Nezihe Asli Bayram and Sumeyye Gok



One of the most important problems in finding blood donors is the inadequacy of volunteer number. To overcome this problem, one of the solutions we suggest is innovating new health benefits of blood donation. The aim of the present study is to investigate the effects of blood donation on oxidative status markers and acute-phase reactants.


A total of 96 healthy volunteers were recruited into the study. Blood samples were withdrawn 5 min before and 24 h after the blood donation. Serum nitric oxide, malondialdehyde levels, and activity of superoxide dismutase and myeloperoxidase were measured spectrophotometrically. Serum levels of high-sensitive C-reactive protein and pentraxin-3 as acute-phase reactants were measured by enzyme-linked immunosorbent assay kits.


We found statistically significant lower pentraxin-3 and high-sensitive C-reactive protein levels and higher superoxide dismutase activity and nitric oxide level 24 h after blood donation in serum of blood donor when compared with before blood donation.


These findings suggest that blood donation affected oxidative status and acute-phase reactants in donors. Blood donation removes oxidants and decreases oxidative stress by elevating antioxidant enzyme such as superoxide dismutase. This is one more health benefit or reason why we should donate blood. Further large-scale studies should evaluate this mechanism and compare the same effect of wet cupping therapy.

  1. Author contributions: All the authors have accepted responsibility for the entire content of this submitted manuscript and approved submission.

  2. Research funding: This work is supported by the Scientific Research Fund of Turgut Ozal University under project number 2013-04-003.

  3. Employment or leadership: None declared.

  4. Honorarium: None declared.

  5. Competing interests: The funding organization(s) played no role in the study design; in the collection, analysis, and interpretation of data; in the writing of the report; or in the decision to submit the report for publication.


1. Salonen JT, Tuomainen TP, Salonen R, Lakka TA, Nyyssonen K. Donation of blood is associated with reduced risk of myocardial infarction. The Kuopio Ischaemic Heart Disease Risk Factor Study. Am J Epidemiol 1998;148:445–51.10.1093/oxfordjournals.aje.a009669Search in Google Scholar PubMed

2. Zacharski LR, Chow BK, Howes PS, Shamayeva G, Baron JA, Dalman RL, et al. Decreased cancer risk after iron reduction in patients with peripheral arterial disease: results from a randomized trial. J Natl Cancer Inst 2008;100:996–1002.10.1093/jnci/djn209Search in Google Scholar PubMed

3. Houschyar KS, Ludtke R, Dobos GJ, Kalus U, Broecker-Preuss M, Rampp T, et al. Effects of phlebotomy-induced reduction of body iron stores on metabolic syndrome: results from a randomized clinical trial. BMC Med 2012;10:54.10.1186/1741-7015-10-54Search in Google Scholar PubMed PubMed Central

4. Tagil SM, Celik HT, Ciftci S, Kazanci FH, Arslan M, Erdamar N, et al. Wet-cupping removes oxidants and decreases oxidative stress. Complement Ther Med 2014;22:1032–6.10.1016/j.ctim.2014.10.008Search in Google Scholar PubMed

5. Miranda KM, Espey MG, Wink DA. A rapid, simple spectrophotometric method for simultaneous detection of nitrate and nitrite. Nitric Oxide-Biol Ch 2001;5:62–71.10.1006/niox.2000.0319Search in Google Scholar PubMed

6. Hashem MA, Mohamed MH. Haemato-biochemical and pathological studies on aflatoxicosis and treatment of broiler chicks in Egypt. Veterinaria Ital 2009;45:323–37.Search in Google Scholar

7. Stevens RG, Davis S, Thomas DB, Anderson LE, Wilson BW. Electric-power, pineal function, and the risk of breast-cancer. FASEB J 1992;6:853–60.10.1096/fasebj.6.3.1740235Search in Google Scholar PubMed

8. Kroupova J, Bartova E, Fojt L, Strasak L, Kozubek S, Vetterl V. Low-frequency magnetic field effect on cytoskeleton and chromatin. Bioelectrochemistry 2007;70:96–100.10.1016/j.bioelechem.2006.03.034Search in Google Scholar PubMed

9. Salem A, Hafedh A, Rached A, Mohsen S, Khemais BR. Zinc prevents hematological and biochemical alterations induced by static magnetic field in rats. Pharmacol Rep 2005;57:616–22.Search in Google Scholar

10. West IC. Radicals and oxidative stress in diabetes. Diab Med 2000;17.3:171–80.10.1046/j.1464-5491.2000.00259.xSearch in Google Scholar PubMed

11. Jenner P. Oxidative stress in Parkinson’s disease and other neurodegenerative disorders. Pathol Biol 1996;44:57–64.Search in Google Scholar

12. Duda D, Grzesik J, Pawlicki K. Changes in liver and kidney concentration of copper, manganese, cobalt and iron in rats exposed to static and low-frequency (50 Hz) magnetic-fields. J Trace Elem Elect H 1991;5:181–6.Search in Google Scholar

13. Sobczak A, Kula B, Danch A. Effects of electromagnetic field on free-radical processes in steelworkers. Part II: magnetic field influence on vitamin A, E and selenium concentrations in plasma. J Occup Health 2002;44:230–3.10.1539/joh.44.230Search in Google Scholar

14. Jain, Sachin, Vidhi Gautam, and Sania Naseem. Acute-phase proteins: As diagnostic tool. Journal of Pharmacy and Bioallied Sciences 2011;3:118.10.4103/0975-7406.76489Search in Google Scholar PubMed PubMed Central

15. Guevara, Ibeth, et al. Determination of nitrite/nitrate in human biological material by the simple Griess reaction. Clinica Chimica Acta 1998;274:177–88.10.1016/S0009-8981(98)00060-6Search in Google Scholar

16. Mihara M, Uchiyama M. Determination of malonaldehyde precursor in tissues by thiobarbituric acid test. Anal Biochem 1978;86:271–8.10.1016/0003-2697(78)90342-1Search in Google Scholar

17. Sun Y, Oberley LW, Li Y. A simple method for clinical assay of superoxide dismutase. Clin Chem 1988;34:497–500.10.1093/clinchem/34.3.497Search in Google Scholar

18. Nowak D. Hydrogen peroxide release from human polymorphonuclear leukocytes measured with horseradish peroxidase and o-dianisidine. Effect of various stimulators and cytochalasin B. Biomedica biochimica acta 1989;49:353–362.Search in Google Scholar

19. SPSS Inc. SPSS 16.0 for Windows. 2007.Search in Google Scholar

20. Jensen LE, Whitehead AS. Regulation of serum amyloid A protein expression during the acute-phase response. Biochem J 1998;334:489–503. International Federation of Red Cross and Red Crescent Societies. 201510.1042/bj3340489Search in Google Scholar PubMed PubMed Central

21. Garlanda C, Bottazzi B, Bastone A, Mantovani A. Pentraxins at the crossroads between innate immunity, inflammation, matrix deposition, and female fertility. Annu Rev Immunol 2005;23:337–66.10.1146/annurev.immunol.23.021704.115756Search in Google Scholar PubMed

22. Basile A, Sica A, dAniello E, Breviario F, Garrido G, Castellano M, et al. Characterization of the promoter for the human long pentraxin PTX3 – role of NF-kappa B in tumor necrosis factor-alpha and interleukin-1 beta regulation. J Biol Chem 1997;272:8172–8.10.1074/jbc.272.13.8172Search in Google Scholar PubMed

23. Bottazzi B, Vouret-Craviari V, Bastone A, De Gioia L, Matteucci C, Peri G, et al. Multimer formation and ligand recognition by the long pentraxin PTX3 – Similarities and differences with the short pentraxins C-reactive protein and serum amyloid P component. J Biol Chem 1997;272:32817–23.10.1074/jbc.272.52.32817Search in Google Scholar PubMed

24. Amrein K, Valentin A, Lanzer G, Drexler C. Adverse events and safety issues in blood donation–a comprehensive review. Blood Rev 2012;26:33–42.10.1016/j.blre.2011.09.003Search in Google Scholar PubMed

25. Kim DK, Jeong JH, Lee JM, Kim KS, Park SH, Kim YD, et al. Inverse agonist of estrogen-related receptor gamma controls Salmonella typhimurium infection by modulating host iron homeostasis. Nat Med 2014;20:419–24.10.1038/nm.3483Search in Google Scholar PubMed

26. Gaut JP, Byun J, Tran HD, Lauber WM, Carroll JA, Hotchkiss RS, et al. Myeloperoxidase produces nitrating oxidants in vivo. J Clin Invest 2002;109:1311–9.10.1172/JCI0215021Search in Google Scholar

27. Ergenekon E, Bozkaya D, Goktas T, Erbas D, Yucel A, Turan O, et al. Are serum nitric oxide and vascular endothelial growth factor levels affected by packed red blood cell transfusions? Hematology 2010;15:170–3.10.1179/102453309X12583347113456Search in Google Scholar PubMed

28. Beckman JS, Ye YZ, Chen J, Conger KA. The interactions of nitric oxide with oxygen radicals and scavengers in cerebral ischemic injury. Adv Neurol 1996;71:339–54.Search in Google Scholar

29. Wink DA, Miranda KM, Espey MG, Pluta RM, Hewett SJ, Colton C, et al. Mechanisms of the antioxidant effects of nitric oxide. Antioxid Redox Sign 2001;3:203–13.10.1089/152308601300185179Search in Google Scholar PubMed

30. Larsen FJ, Ekblom B, Sahlin K, Lundberg JO, Weitzberg E. Effects of dietary nitrate on blood pressure in healthy volunteers. N Engl J Med 2006;355:2792–3.10.1056/NEJMc062800Search in Google Scholar PubMed

31. Azarov I, He X, Jeffers A, Basu S, Ucer B, Hantgan RR, et al. Rate of nitric oxide scavenging by hemoglobin bound to haptoglobin. NOBC J Nitric Oxide Soc 2008;18:296–302.10.1016/j.niox.2008.02.006Search in Google Scholar PubMed PubMed Central

Received: 2015-9-16
Accepted: 2016-2-26
Published Online: 2016-4-18
Published in Print: 2016-11-1

©2016 Walter de Gruyter GmbH, Berlin/Boston

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