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2012 | 17 | 4 |

Tytuł artykułu

Effects of lead chloride on human erythrocyte membranes and on kinetic anion sulphate and glutathione concentrations

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
Our study concerns the effects of exposure to lead chloride on the morphology, K+ efflux, SO4 − influx and GSH levels of the human erythrocyte. Blood was collected in heparinized tubes and washed three times. The cells were suspended at 3% hematocrit and incubated for 1 h at 25°C in a medium containing increasing concentrations of lead chloride (0, 0.3, 0.5 and 1 μM). After incubation, the suspensions were centrifuged and the erythrocyte pellets were divided into three aliquots for testing. The results show: an increase in the permeability of erythrocytes treated with lead chloride with consequent damage and cellular death, especially in the presence of high concentrations; an increase in potassium ion efflux; alterations in the morphology and membrane structure of the red blood cells; and a decrease in sulphate uptake, due either to the oxidative effect of this compound on the band 3 protein, which loses its biological valence as a carrier of sulphate ions, or to a decrease in the ATP erythrocyte concentration. In conclusion, the exposure of erythrocytes to Pb2+ ions leads to a reduction in the average lifetime of the erythrocytes and the subsequent development of anemia. These data are discussed in terms of the possible effect of lead on the reduction-oxidation systems of the cell. Oxidant agents, such as lead, are known to cross-link integral membrane proteins, leading to K/Cl-cotransport. The increased K+ efflux affects the altered redox state.

Wydawca

-

Rocznik

Tom

17

Numer

4

Opis fizyczny

p.586-597,fig.,ref.

Twórcy

autor
  • Dipartimento di Scienze della Vita "M.
autor
autor
autor
autor
autor

Bibliografia

  • 1. Lockitch, G. Perspectives on lead toxicity. Clin. Biochem. 26 (1993) 371-381.
  • 2. Giuliani, R., Bettoni, F., Leali, D., Morandini, F., Apostoli, P., Grigolato, P., Cesana, B.M. and Aleo, M.F. Focal adhesion molecule as potential target of lead toxicity in NRK-52E cell line. FEBS Lett. 579 (2005) 6251-6258.
  • 3. Zamzami, N., Maisse, C., Métivier, D. and Kroemer, G. Measurement of membrane permeability and permeability transition of mitochondria. Methods Cell Biol. 165 (2001) 147-158.
  • 4. Stohs, S.J. and Bagchi, D. Oxidative mechanisms in the toxicity of metal ions. Free Radic. Biol. Med. 18 (1995) 321-336.
  • 5. Martinou, J.C. and Green, D.R. Breaking the mitochondrial barrier. Nat. Rev. Mol. Cell. Biol. 2 (2001) 63-67.
  • 6. Simons, T.J. Passive transport and binding of lead by human red blood cells. J. Physiol. 378 (1986) 267-286.
  • 7. Hamasaki, N. and Okubo, K. Band 3 protein: physiology, function and structure. Cell. Mol. Biol. 42 (1996) 1025-1039.
  • 8. Casey, J.R. and Kopito, R.R. The role of cysteine residues in the erythrocyte plasma membrane anion exchange protein. J. Biol. Chem. 270 (1995) 8521- 8527.
  • 9. Galtieri, A., Tellone, E., Romano, L., Misiti, F., Bellocco, E., Ficarra, S., Russo, A., Di Rosa, D., Castagnola, M., Giardina, B. and Messana, I. Band 3 protein function in human erythrocytes: effect of oxygenationdeoxigenation. Biochem. Biophys. Acta 1564 (2002) 214-218.
  • 10. Blackman, S.M., Hustedt, E.J., Cobb, C.E. and Beth, A.H. Flexibility of the cytoplasmic domain of the anion exchange protein, band 3, in human erythrocytes. Biophys. J. 81 (2001) 3363-3376.
  • 11. Poole, J. Red cell antigens on band 3 and glycophorin A. Blood Rev. 14 (2000) 31-43.
  • 12. Yannoukakos, D., Vasseur, C., Piau, J.P., Wajcman, H. and Bursaux, E. Phosphorilation sites in human erythrocyte band 3 protein. Biochim. Biophys. Acta 1061 (1991) 253-266.
  • 13. Barbul, A., Zipser, Y., Nachles, A. and Korenstein, R. Deoxygenation and elevation of intracellular magnesium induce tyrosine phosphorilation of band 3 in human erythrocytes. FEBS Lett. 455 (1999) 87-91.
  • 14. Romano, L., Scuteri, A., Gugliotta, T., Romano, P., De Luca, G., Sidoti, A. and Amato, A. Sulphate influx in the erythrocytes of normal, diabetic and hypertensive patients. Cell Biol. Int. 26 (2002) 421-426.
  • 15. De Luca, G., Gugliotta, T., Scuteri, A., Romano, P., Rinaldi, C., Sidoti, A., Amato, A. and Romano, L. The interaction of haemoglobin, magnesium, organic phosphates and the Band 3 protein in nucleated and anucleated erythrocytes. Cell Biochem. Funct. 22 (2004) 179-186.
  • 16. Pastore, A., Federici, G., Bertini, E. and Piemonte, F. Analysis of glutathione. Implication in redox and detoxication. Clin. Chim. Acta 333 (2003) 19-39.
  • 17. Counter, S.A., Buchanam, L.H., Ortega, F. and Rifai, N. Blood lead and hemoglobin levels in Andean children with chronic lead intoxication. Neurotoxicology 21 (2000) 301-308.
  • 18. Hernàndez-Serrato, M.I., Mendoza-Alvarado, L.R., Rojas-Martinez, R., Gonzàlez-Garza, C., Hulme, J.M. and Olaiz-Fernàndez, G. Factors associated with lead exposure in Oaxaca, Mexico. J. Expo. Anal. Environ. Epidemiol. 13 (2003) 341-347.
  • 19. Stober, T., Stelte, W. and Kunze, K. Lead concentrations in blood, plasma, erythrocytes, and cerebrospinal fluid in amyotrophic lateral sclerosis. J. Neurol. Sci. 61 (1983) 21-26.
  • 20. Simons, T.J. Cellular interactions between lead and calcium. Br. Med. Bull. 42 (1986) 431-434.
  • 21. Roy, S.S., Sen, G. and Biswas, T. Role of sulfhydryl groups in band 3 in the inhibition of phosphate transport across erythrocyte membrane in visceral leishmaniasis. Arch. Biochem. Biophys. 436 (2005) 121-127.
  • 22. De Luca, G., Gugliotta, T., Parisi, G., Romano, P., Geraci, A., Romano, O., Scuteri, A. and Romano, L. Effects of nickel on human and fish red blood cells. Biosci. Rep. 27 (2007) 265-273.
  • 23. Teti, D., Crupi, M., Busà, M., Valenti, A., Loddo, S., Mondello, M. and Romano, L. Chemical and pathological oxidative influences on band 3 protein anion-exchanger. Cell Physiol. Biochem. 16 (2005) 77-86.
  • 24. Huber, S.M., Gamper, N. and Lang, F. Chloride conductance and volumeregulatory non selective cation conductance in human red blood cell ghosts. Pflùgers Arch. 441 (2001) 551-558.
  • 25. Donaldson, W.E. and Knowles, S.O. Is lead toxicosis a reflection of altered fatty acid composition of membranes? Comp. Biochem. Physiol. 104C (1999) 377-379.
  • 26. Yücebilgic, G., Bilgin, R., Tamer, L. and Tükel, S. Effects of lead on Na+ -K+ ATPase and Ca2+ATPase activities and lipid peroxidation in blood of workers. Int. J. Toxicol. 22 (2003) 95-97.
  • 27. Sivaprasad, R., Nagaraj, M. and Varalakshmi, P. Combined efficacies of lipoic acid and meso-2,3-dimercaptosuccinic acid on lead-induced erythrocyte membrane lipid peroxidation and antioxidant status in rats. Hum. Exp. Toxicol. 22 (2003) 182-192.
  • 28. Mota de Freitas, D., Amari, L., Scrinivason, C., Rong, Q., Romosomy, R., Abraha, A., Geraldes, C.F.G.C. and Boyd, M.K. Competition between Li+ and Mg2+ for the phosphate groups in the human erythrocyte membrane and ATP. An NMR and fluorescence study. Biochemistry 33 (1994) 4101-4110.
  • 29. Baranowska-Bosiacka, I. and Hlynczak, A.J. The effect of lead ions on the energy metabolism of human erythrocytes in vitro. Comp. Biochem. Physiol. C Toxicol. Pharmacol. 134 (2003) 403-416.
  • 30. Grabowska, M. and Gumińska, M. The effect of lead on lactate formation, ATP level and membrane ATPase activities in human erythrocytes in vitro. Int. J. Occup. Med. Environ. Health 9 (1996) 265-274.
  • 31. Kempe, D.S., Lang, P.A., Eisele, K., Klarl, B.A., Wieder, T., Huber, S.M., Duranton, C. and Lang, F. Stimulation of eryhrocyte phosphatidylserie exposure by lead ions. Am. J. Physiol. Cell Physiol. 288 (2005) 396-402.
  • 32. Berg, C.P., Engels, I.H., Rothbart, A., Lauber, K., Renz, A., Schlosser, S.F., Schulze-Osthoff, K. and Wesselborg, S. Human mature red blood cells express caspase-3 and caspase-8, but are devoid of mitochondrial regulators of apoptosis. Cell Death Differ. 8 (2001) 1197-1206.
  • 33. Bratosin, D., Estaquier, J., Petit, F., Arnoult, D., Quatannens, B., Tissier, J.P., Slomianny, C., Sartiaux, C., Alonso, C., Huart, J.J., Montreuil, J. and Ameisen, J.C. Programmed cell death in mature erythrocytes: a model for investigating death effector pathways operating in the absence of mitochondria. Cell Death Differ. 8 (2001) 1143-1156.
  • 34. Daugas, E., Cande, C. and Kroemer, G. Erythrocytes: death of a mummy. Cell Death Differ. 8 (2001) 1131-1133.
  • 35. Bortner, C.D. and Cidlowski, J.A. Caspase independent/dependent regulation of K+ , cell shrinkage, and mitochondrial membrane potential during lymphocyte apoptosis. J. Biol. Chem. 274 (1999) 21953-21962.
  • 36. Bortner, C.D., Hughes, F.M. Jr. and Cidlowski, J.A. A primary role for K+ and Na+ efflux in the activation of apoptosis. J. Biol. Chem. 272 (1997) 32436-32442.
  • 37. Fadok, V.A., de Cathelineau, A., Daleke, D.L., Henson, P.M. and Bratton, D.L. Loss of phospholipid asymmetry and surface exposure of phosphatidylserine is required for phagocytosis of apoptotic cells by macrophages and fibroblasts. J. Biol. Chem. 276 (2001) 1071-1077.
  • 38. Hughes, F.M. Jr. and Cidlowski, J.A. Potassium is a critical regulator of apoptotic enzymes in vitro and in vivo. Adv. Enzyme Regul. 39 (1999) 157-171.
  • 39. Hughes, F.M. Jr, Bortner, C.D., Purdy, G.D. and Cidlowski, J.A. Intracellular K+ suppresses the activation of apoptosis in lymphocytes. J. Biol. Chem. 272 (1997) 30567-30576.
  • 40. Montague, J.W., Bortner, C.D., Hughes, F.M. Jr. and Cidlowski, J.A. A necessary role for reduced intracellular potassium during the DNA degradation phase of apoptosis. Steroids 64 (1999) 563-569.
  • 41. Perez, G.I., Maravei, D.V., Trbovich, A.M., Cidlowski, J.A., Tilly, J.L. and Hughes, F.M. Jr. Identification of potassium-dependent and -independent components of the apoptotic machinery in mouse ovarian germ cells and granulosa cells. Biol. Reprod. 63 (2000) 1358-1369.

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

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