Startseite Biochemical effects of lead exposure on oxidative stress and antioxidant status of battery manufacturing workers of Western Maharashtra, India
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Biochemical effects of lead exposure on oxidative stress and antioxidant status of battery manufacturing workers of Western Maharashtra, India

  • Ganesh Haribhau Ghanwat , Arun Jalindar Patil EMAIL logo , Jyotsna A. Patil , Mandakini S. Kshirsagar , Ajit Sontakke und Ram Krishna Ayachit
Veröffentlicht/Copyright: 21. Oktober 2015

Abstract

Background: Lead induces oxidative stress and alters the antioxidant status of population exposed to high lead levels, i.e. battery manufacturing workers. The aim of this study was to know the current scenario of blood lead (PbB) levels and their effect on the oxidative stress parameter, i.e. serum lipid peroxide (LP), and antioxidant parameters, such as red blood cell (RBC)-superoxide dismutase (SOD), RBC-catalase (CAT), plasma ceruloplasmin (CP), and serum nitrite, of battery manufacturing workers.

Methods: Forty-three battery manufacturing workers from Western Maharashtra, India, with ages between 19 and 42 years, were selected as study group and compared with 38 age-matched, healthy male subjects (control group). From both group subjects, 10 mL of blood sample was drawn by puncturing the antecubital vein, and PbB, serum LP, RBC-SOD, RBC-CAT, plasma CP, and serum nitrite were estimated using standard methods.

Results: The PbB levels of the battery manufacturing workers were significantly higher (p<0.001, 1050%) as compared with the control subjects. The serum LP levels were significantly increased (p<0.001, 96.86%); all antioxidant status parameters such as RBC-SOD (p<0.001, –26.32%), RBC-CAT (p<0.001, –51.57%), and plasma CP (p<0.001, –35.13%) were significantly decreased; and serum nitrite levels (p<0.001, 154%) were significantly increased in the battery manufacturing workers as compared with the control subjects.

Conclusions: Despite modern techniques used to reduce lead exposure in battery manufacturing workers, PbB levels remain high, inducing oxidative stress and altering the antioxidant status of battery manufacturing workers.


Corresponding author: Arun Jalindar Patil, Department of Biochemistry, Krishna Institute of Medical Sciences Deemed University, Karad-415539, Dist. Satara, (Maharashtra), India, E-mail:

References

1. Agency for Toxic Substances and Disease Registry (ATSDR). Toxicological profile for lead. US Department of Health and Human Services. Atlanta, GA: US Government Printing, 2005:102–225.Suche in Google Scholar

2. World Health Organization. Biological indices of lead exposure and body burden. In: IPCS, inorganic lead, environmental health criteria 118. Geneva, Switzerland: WHO, 1995;165:114–8.Suche in Google Scholar

3. Patil AJ, Bhagwat VR, Patil JA, Dongre NN, Ambekar JG, Jailkhani R, et al. Effect of lead (Pb) exposure on the activity of superoxide dismutase and catalase in battery manufacturing workers of Western Maharashtra (India) with reference to heme biosynthesis. Int J Environ Res Public Health 2006;3:329–37.10.3390/ijerph2006030041Suche in Google Scholar

4. Sipos P, Szentmihályi K, Fehér E, Abaza M, Szilyági M, Blázovics A. Some effects of lead contamination on liver and gall bladder bile. Acta Biol Szeged 2003;47:139–42.Suche in Google Scholar

5. DeMichele SJ. Nutrition of lead. Comp Biochem Physiol A 1984;78:401–8.10.1016/0300-9629(84)90567-XSuche in Google Scholar

6. Needleman H. Lead poisoning. Annu Rev Med 2004;55:209–22.10.1146/annurev.med.55.091902.103653Suche in Google Scholar

7. Lichtman HC, Feldman F. In-vitro pyrrole and porphyrin synthesis in lead poisoning and iron deficiency. J Clin Invest 1963;42:830–9.10.1172/JCI104775Suche in Google Scholar

8. Jaffe EK, Martin, Li J, Kervinan J, Dunbrack RL, Jr. The molecular mechanism of lead inhibition of human porphobilinogen synthase. J Biol Chem 2001;276:1531–7.10.1074/jbc.M007663200Suche in Google Scholar

9. Warren MJ, Cooper JB, Wood SP, Shoolingin-Jordan PM. X-ray structure of a putative reaction intermediate of 5-aminolaevulinic acid dehydratase. Biochem J 2003;373:733–8.10.1042/bj20030513Suche in Google Scholar

10. Lachant NA, Tomoda A, Tanaka KR. Inhibition of the pentose phosphate shunt by lead: a potential mechanism for hemolysis in lead poisoning. Blood 1984;63:518–24.10.1182/blood.V63.3.518.518Suche in Google Scholar

11. Lamola AA, Joselow M, Yamane T. Zinc protoporphyrin (ZPP): a simple, sensitive, fluorometric screening test for lead poisoning. Clin Chem 1975;21:93–7.10.1093/clinchem/21.1.93Suche in Google Scholar

12. Caìrdenas A, Roels H, Bernard AM, Barbon R, Buchet JP, Lauwerys RR, et al. Markers of early renal changes induced by industrial pollutants. II Application to workers exposed to lead. Br J Ind Med 1993;50:28–36.10.1136/oem.50.1.28Suche in Google Scholar

13. Cramer K, Goyer RA, Jagenburg R, Wilson MH. Renal ultra structure, renal function, and parameters of lead toxicity in workers with different periods of lead exposure. Br J Ind Med 1974;31:113–27.10.1136/oem.31.2.113Suche in Google Scholar

14. Goyer RA. Lead toxicity: a problem in environmental pathology. Am J Pathol 1971;64:167–82.Suche in Google Scholar

15. Mudipalli A. Lead hepatotoxicity & potential health effects. Indian J Med Res 2007;126:518–27.Suche in Google Scholar

16. Fukumoto K, Karai I, Horiguchi S. Effect of lead on erythrocyte membranes. Br J Ind Med 1983;40:220–3.10.1136/oem.40.2.220Suche in Google Scholar

17. Declaration of Helsinki (1964). Amended by World Medical Assembly, Venice, Italy. Br Med J 1996;313:1448–9.10.1136/bmj.313.7070.1448aSuche in Google Scholar

18. Magellan Diagnostics, user’s guide, Lead Care II Blood Lead Testing System. Chelmsford, MA: Magellan Diagnostics: 1–9. Available at: http://www.cliawaived.com/web/items/pdf/ESA_70_3447_LeadCare_II_Analyzer_Manual~1713file3.pdf.Suche in Google Scholar

19. Satoh K. Serum lipid peroxide in cerebrovascular disorders determined by a new colorimetric method. Clin Chim Acta 1978;90:37–43.10.1016/0009-8981(78)90081-5Suche in Google Scholar

20. Marklund S, Marklund G (modified by Nandi). Assay of Sod activity in tissue. J Biochem 1988;13:305–15.10.1007/BF02712155Suche in Google Scholar

21. Aebi H. Catalase methods in enzymatic analysis. In: Bergumeryer HU, editor. Methods of enzymatic analysis, Vol. 3. New York: Academic Press, 1983:276–86.Suche in Google Scholar

22. Ravin HA. An improved colorimetric enzymatic assay of ceruloplasmin. Lab Clin Med 1961;58:161–8.Suche in Google Scholar

23. Henry RJ. Determination of serum ceruloplasmin. In: Clinical chemistry: principles and techniques, 1961:860.Suche in Google Scholar

24. Coras NK, Wakid NW. Determination of inorganic nitrate in serum and urine by a kinetic cadmium reduction method. Clin Chem 1990;36:1440–3.10.1093/clinchem/36.8.1440Suche in Google Scholar

25. Thuppil V, Tannir S. Treating lead toxicity: possibilities beyond synthetic chelation. JKIMSU 2013;2:4–31.Suche in Google Scholar

26. Dongre NN, Suryakar AN, Patil AJ, Rathi DB. Biochemical effects of occupational lead exposure in automobile workers. J Environ Health Res 2010;10:35–44.Suche in Google Scholar

27. Valko M, Rhodes CJ, Moncol J, Izakovic M, Mazur M. Free radicals, metals and antioxidants in oxidative stress-induced cancer. Chem Biol Interact 2006;160:140.10.1016/j.cbi.2005.12.009Suche in Google Scholar

28. Patrick L. Lead toxicity part II – the role of free radical damage and the use of antioxidants in the pathology and treatment of lead toxicity. Altern Med Rev 2006;11:114–27.Suche in Google Scholar

29. Haeger-Arosen B. Studies on urinary excretion of δ-ALA and other haem precursors in lead workers and lead-intoxicated rabbits. Scand J Clin Lab Invest 1960;12:1.Suche in Google Scholar

30. O’Flaherty EJ, Hammond PB, Lerner SI, Hanenson IB, Roda SM. The renal handling of delta-aminolevulinic acid in the rat and in the human. Toxicol Appl Pharmacol 1980;55:423–32.10.1016/0041-008X(80)90044-7Suche in Google Scholar

31. Al-Ubaidy B, Al-Khashali DK, Numan NA. The role of oxidative stress in lead poisoning. Iraqi J Pharm Sci 2006;15:70–5.Suche in Google Scholar

32. Bechara EJ, Medeiros MH, Monteiro HP, Hermes-Lima M, Pereira B, Demasi M, et al. A free radical hypothesis of lead poisoning and inborn porphyrias associated with δ-aminolevulinic acid overload. Quím Nova 1993;16:385–92.Suche in Google Scholar

33. Ahamed M, Siddiqui MK. Low level lead exposure and oxidative stress: current opinions. Clin Chim Acta 2007;383:5764.10.1016/j.cca.2007.04.024Suche in Google Scholar

34. Monteiro HP, Abdalla DS, Augusto O, Bechara EJ. Free radical generation during delta-aminolevulinic acid autoxidation: induction by hemoglobin and connections with porphyrinpathies. Arch Biochem Biophys 1989;271:206–16.10.1016/0003-9861(89)90271-3Suche in Google Scholar

35. Monteiro HP, Bechara EJ, Abdalla DS. Free radicals involvement in neurological porphyrias and lead poisoning. Mol Cell Biochem 1991;103:73–83.10.1007/BF00229595Suche in Google Scholar

36. Hermes-Lima M, Valle VG, Vercesi AE, Bechara EJ. Damage to rat liver mitochondria promoted by d-aminolevulinic acid-generated reactive oxygen species: connections with acute intermittent porphyria and lead-poisoning. Biochim Biophys Acta Amsterdam 1991;1056:57–63.10.1016/S0005-2728(05)80072-6Suche in Google Scholar

37. Donaldson WE, Knowles SO. Is lead toxicosis a reflection of altered fatty acid composition of membranes? Comp Biochem Physiol C 1993;104:377–9.10.1016/0742-8413(93)90003-4Suche in Google Scholar

38. De Silva PE. Determination of lead in plasma and studies on its relationship to lead in erythrocytes. Br J Ind Med 1981;38:209–17.10.1136/oem.38.3.209Suche in Google Scholar

39. Rice-Evans C. Iron-mediated oxidative stress and erythrocytes. In: Harris JR, editor. Blood cell biochemistry, Vol. 1. New York: Plenum, 1990:429–53.10.1007/978-1-4757-9528-8_14Suche in Google Scholar

40. Waldron HA. The anaemia of lead poisoning: a review. Br J Ind Med 1966;23:83–100.10.1136/oem.23.2.83Suche in Google Scholar

41. Bonting SL, Caravaggio LL. Studies on sodium-potassium-activated adenosinetriphosphatase. V. Correlation of enzyme activity with cation flux in six tissues. Arch Biochem Biophys 1963;101:37–46.10.1016/0003-9861(63)90531-9Suche in Google Scholar

42. Hasan J, Vihko V, Hernberg S. Deficient red cell membrane (Na+-K+)-ATPase in lead poisoning. Arch Environ Health 1971;14:313–8.10.1080/00039896.1967.10664738Suche in Google Scholar

43. Raghavan SR, Culver BD, Gonick HC, Erythrocyte lead-binding protein after occupational exposure. II. Influence on lead inhibition of membrane Na+,K+-adenosinetriphosphatase. J Toxicol Environ Health 1981;7:561–8.10.1080/15287398109530001Suche in Google Scholar

44. Fukumoto K, Karai I, Horiguchi S. Effect of lead on erythrocyte membranes. Br J Ind Med 1983;40:220–3.10.1136/oem.40.2.220Suche in Google Scholar

45. Carrell RW, Winterbourn CC, Rachmilewitz EA. Activated oxygen and haemolysis. Br J Haematol 1975;30:259–64.10.1111/j.1365-2141.1975.tb00540.xSuche in Google Scholar

46. Mylroie AA, Collins H, Umbles C, Kyle J. Erythrocyte superoxide dismutase activity and other parameters of copper status in rats ingesting lead acetate. Toxicol Appl Pharmacol 1986;82:512–20.10.1016/0041-008X(86)90286-3Suche in Google Scholar

47. Mylroie AA, Umbles C, Kyle J. Effects of dietary copper supplementation on erythrocyte superoxide dismutase activity, ceruloplasmin and related parameters in rats ingesting lead acetate. In: Hemphill DD, editor. Trace substances in environmental health, Vol. 18. Columbia, MO: University of Missouri Press, 1984:497–504.Suche in Google Scholar

48. Adler AJ, Barth RH, Berlyne GM. Effect of lead on oxygen free radical metabolism: inhibition of SOD activity. Trace Elem Med 1993;10:93–6.Suche in Google Scholar

49. Cadet JL, Brannock C. Free radicals and the pathobiology of brain dopamine systems. Neurochem Int 1998;32:117–31.10.1016/S0197-0186(97)00031-4Suche in Google Scholar

50. Monteiro HP, Abdulla DSP, Aveuri SS, Bechera EJ. Oxygen toxicity related to exposure to lead. Clin Chem 1985;31:1673–6.10.1093/clinchem/31.10.1673Suche in Google Scholar

51. Ito Y, Nijya Y, Kurita H, Shima S, Sarai S. Serum lipid peroxide level and blood SOD activity in workers with occupational exposure to lead. Int Arch Occup Environ Health 1985;56:119–27.10.1007/BF00379383Suche in Google Scholar PubMed

52. Sugawara E, Nakamura K, Miyake T, Fukumura A, Seki Y. Lipid peroxidation and concentration of glutathione in erythrocytes from workers exposed to lead. Br J Ind Med 1991;48:239–42.10.1136/oem.48.4.239Suche in Google Scholar PubMed PubMed Central

53. Chiba M, Shinohara A, Matsushita K, Watanabe H, Inaba Y. Indices of lead-exposure in blood and urine of lead-exposed workers and concentrations of major and trace elements and activities of SOD, GSHPx and catalase in their blood. Tohoku J Exp Med 1996;178:49–62.10.1620/tjem.178.49Suche in Google Scholar PubMed

Received: 2015-3-24
Accepted: 2015-7-30
Published Online: 2015-10-21
Published in Print: 2016-3-1

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