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Journal of Biomedicine and Biotechnology
Volume 2010 (2010), Article ID 395785, 9 pages
http://dx.doi.org/10.1155/2010/395785
Research Article

Epoetin Delta Reduces Oxidative Stress in Primary Human Renal Tubular Cells

1Laboratory of Pathophysiology, Faculties of Medicine and Biomedical, Pharmaceutical and Veterinary Sciences, University of Antwerp, Universiteitsplein 1, 2610 Antwerp, Belgium
2Department of Nephrology, The Second Hospital, Shandong University, Jinan 250033, China

Received 16 November 2009; Revised 17 February 2010; Accepted 17 February 2010

Academic Editor: Xudong Huang

Copyright © 2010 Annelies De Beuf et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. G. W. Dryden Jr., I. Deaciuc, G. Arteel, and C. J. McClain, “Clinical implications of oxidative stress and antioxidant therapy,” Current Gastroenterology Reports, vol. 7, no. 4, pp. 308–316, 2005.
  2. L. Forsberg, U. de Faire, and R. Morgenstern, “Oxidative stress, human genetic variation, and disease,” Archives of Biochemistry and Biophysics, vol. 389, no. 1, pp. 84–93, 2001. View at Publisher · View at Google Scholar · View at PubMed
  3. J.-C. Lee, J. Kim, J.-K. Park, G.-H. Chung, and Y.-S. Jang, “The antioxidant, rather than prooxidant, activities of quercetin on normal cells: quercetin protects mouse thymocytes from glucose oxidase-mediated apoptosis,” Experimental Cell Research, vol. 291, no. 2, pp. 386–397, 2003. View at Publisher · View at Google Scholar
  4. C. A. Rice-Evans, N. J. Miller, P. G. Bolwell, P. M. Bramley, and J. B. Pridham, “The relative antioxidant activities of plant-derived polyphenolic flavonoids,” Free Radical Research, vol. 22, no. 4, pp. 375–383, 1995.
  5. P. Katavetin, K. Tungsanga, S. Eiam-Ong, and M. Nangaku, “Antioxidative effects of erythropoietin,” Kidney International, no. 107, pp. S10–S15, 2007.
  6. F. H. Bahlmann and D. Fliser, “Erythropoietin and renoprotection,” Current Opinion in Nephrology and Hypertension, vol. 18, no. 1, pp. 15–20, 2009. View at Publisher · View at Google Scholar · View at PubMed
  7. M. J. F. Helbert, S. E. H. Dauwe, I. Van der Biest, E. J. Nouwen, and M. E. De Broe, “Immunodissection of the human proximal nephron: flow sorting of S1S2SS3, S1S2 and S3 proximal tubular cells,” Kidney International, vol. 52, no. 2, pp. 414–428, 1997.
  8. M. J. F. Helbert, S. E. H. Dauwe, and M. E. De Broe, “Flow cytometric immunodissection of the human distal tubule and cortical collecting duct system,” Kidney International, vol. 59, no. 2, pp. 554–564, 2001. View at Publisher · View at Google Scholar · View at PubMed
  9. R. E. Gibson-D'Ambrosio, M. Samuel, C. C. Chang, J. E. Trosko, and S. M. D'Ambrosio, “Characteristics of long-term human epithelial cell cultures derived from normal human fetal kidney,” In Vitro Cellular & Developmental Biology, vol. 23, no. 4, pp. 279–287, 1987.
  10. A. Barbouti, P.-T. Doulias, L. Nousis, M. Tenopoulou, and D. Galaris, “DNA damage and apoptosis in hydrogen peroxide-exposed Jurkat cells: bolus addition versus continuous generation of H2O2,” Free Radical Biology and Medicine, vol. 33, no. 5, pp. 691–702, 2002. View at Publisher · View at Google Scholar
  11. H. Gong, W. Wang, T.-H. Kwon, et al., “EPO and α-MSH prevent ischemia/reperfusion-induced down-regulation of AQPs and sodium transporters in rat kidney,” Kidney International, vol. 66, no. 2, pp. 683–695, 2004. View at Publisher · View at Google Scholar · View at PubMed
  12. D. A. Vesey, C. Cheung, B. Pat, Z. Endre, G. Gobé, and D. W. Johnson, “Erythropoietin protects against ischaemic acute renal injury,” Nephrology Dialysis Transplantation, vol. 19, no. 2, pp. 348–355, 2004. View at Publisher · View at Google Scholar
  13. A. Kirkeby, J. van Beek, J. Nielsen, M. Leist, and L. Helboe, “Functional and immunochemical characterisation of different antibodies against the erythropoietin receptor,” Journal of Neuroscience Methods, vol. 164, no. 1, pp. 50–58, 2007. View at Publisher · View at Google Scholar · View at PubMed
  14. Y. Li, G. Takemura, H. Okada, et al., “Reduction of inflammatory cytokine expression and oxidative damage by erythropoietin in chronic heart failure,” Cardiovascular Research, vol. 71, no. 4, pp. 684–694, 2006. View at Publisher · View at Google Scholar · View at PubMed
  15. F. Pajonk, A. Weil, A. Sommer, R. Suwinski, and M. Henke, “The erythropoietin-receptor pathway modulates survival of cancer cells,” Oncogene, vol. 23, no. 55, pp. 8987–8991, 2004. View at Publisher · View at Google Scholar · View at PubMed
  16. A. De Beuf, A. Verhulst, M. Helbert, et al., “Tubular erythropoietin receptor expression mediates erythropoietin-induced renoprotection,” The Open Hematology Journal, vol. 3, pp. 1–10, 2009.
  17. K. A. Kirkby and C. A. Adin, “Products of heme oxygenase and their potential therapeutic applications,” American Journal of Physiology, vol. 290, no. 3, pp. F563–F571, 2006. View at Publisher · View at Google Scholar · View at PubMed
  18. M. Wagner, P. Cadetg, R. Ruf, L. Mazzucchelli, P. Ferrari, and C. A. Redaelli, “Heme oxygenase-1 attenuates ischemia/reperfusion-induced apoptosis and improves survival in rat renal allografts,” Kidney International, vol. 63, no. 4, pp. 1564–1573, 2003. View at Publisher · View at Google Scholar · View at PubMed
  19. T. D. Blydt-Hansen, M. Katori, C. Lassman, et al., “Gene transfer-induced local heme oxygenase-1 overexpression protects rat kidney transplants from ischemia/reperfusion injury,” Journal of the American Society of Nephrology, vol. 14, no. 3, pp. 745–754, 2003. View at Publisher · View at Google Scholar
  20. P. Katavetin, R. Inagi, T. Miyata, et al., “Erythropoietin induces heme oxygenase-1 expression and attenuates oxidative stress,” Biochemical and Biophysical Research Communications, vol. 359, no. 4, pp. 928–934, 2007. View at Publisher · View at Google Scholar · View at PubMed
  21. S. W. Ryter and A. M. K. Choi, “Heme oxygenase-1/carbon monoxide: from metabolism to molecular therapy,” American Journal of Respiratory Cell and Molecular Biology, vol. 41, no. 3, pp. 251–260, 2009. View at Publisher · View at Google Scholar · View at PubMed
  22. S. Nielsen, J. Frøkiaer, D. Marples, T.-H. Kwon, P. Agre, and M. A. Knepper, “Aquaporins in the kidney: from molecules to medicine,” Physiological Reviews, vol. 82, no. 1, pp. 205–244, 2002.
  23. M. Echevarría, A. M. Muñoz-Cabello, R. Sánchez-Silva, J. J. Toledo-Aral, and J. López-Barneo, “Development of cytosolic hypoxia and hypoxia-inducible factor stabilization are facilitated by aquaporin-1 expression,” Journal of Biological Chemistry, vol. 282, no. 41, pp. 30207–30215, 2007. View at Publisher · View at Google Scholar · View at PubMed
  24. E. J. Sharples, N. Patel, P. Brown, et al., “Erythropoietin protects the kidney against the injury and dysfunction caused by ischemia-reperfusion,” Journal of the American Society of Nephrology, vol. 15, no. 8, pp. 2115–2124, 2004. View at Publisher · View at Google Scholar · View at PubMed
  25. C. W. Yang, C. Li, J. Y. Jung, et al., “Preconditioning with erythropoietin protects against subsequent ischemia-reperfusion injury in rat kidney,” The FASEB Journal, vol. 17, no. 12, pp. 1754–1755, 2003.
  26. D. Reverter, K. Maskos, F. Tan, R. A. Skidgel, and W. Bode, “Crystal structure of human carboxypeptidase M, a membrane-bound enzyme that regulates peptide hormone activity,” Journal of Molecular Biology, vol. 338, no. 2, pp. 257–269, 2004. View at Publisher · View at Google Scholar · View at PubMed
  27. K. Deiteren, G. Surpateanu, K. Gilany, et al., “The role of the S1 binding site of carboxypeptidase M in substrate specificity and turn-over,” Biochimica et Biophysica Acta, vol. 1774, no. 2, pp. 267–277, 2007. View at Publisher · View at Google Scholar · View at PubMed
  28. K. Deiteren, D. Hendriks, S. Scharpé, and A. M. Lambeir, “Carboxypeptidase M: multiple alliances and unknown partners,” Clinica Chimica Acta, vol. 399, no. 1-2, pp. 24–39, 2009. View at Publisher · View at Google Scholar · View at PubMed
  29. G. B. McGwire, R. P. Becker, and R. A. Skidgel, “Carboxypeptidase M, a glycosylphosphatidylinositol-anchored protein, is localized on both the apical and basolateral domains of polarized Madin-Darby canine kidney cells,” Journal of Biological Chemistry, vol. 274, no. 44, pp. 31632–31640, 1999. View at Publisher · View at Google Scholar
  30. Y. Nishioka, T. Higuchi, Y. Sato, et al., “Human migrating extravillous trophoblasts express a cell surface peptidase, carboxypeptidase-M,” Molecular Human Reproduction, vol. 9, no. 12, pp. 799–806, 2003. View at Publisher · View at Google Scholar
  31. A.-M. Lambeir, C. Durinx, S. Scharpé, and I. De Meester, “Dipeptidyl-peptidase IV from bench to bedside: an update on structural properties, functions, and clinical aspects of the enzyme DPP IV,” Critical Reviews in Clinical Laboratory Sciences, vol. 40, no. 3, pp. 209–294, 2003.
  32. A.-M. Lambeir, S. Scharpé, and I. De Meester, “DPP4 inhibitors for diabetes—what next?” Biochemical Pharmacology, vol. 76, no. 12, pp. 1637–1643, 2008. View at Publisher · View at Google Scholar · View at PubMed
  33. W. Zhai, M. Cardell, I. De Meester, et al., “Intragraft DPP IV inhibition attenuates post-transplant pulmonary ischemia/reperfusion injury after extended ischemia,” Journal of Heart and Lung Transplantation, vol. 26, no. 2, pp. 174–180, 2007. View at Publisher · View at Google Scholar · View at PubMed
  34. F. J. Jung, L. Yang, I. De Meester, et al., “CD26/dipeptidylpeptidase IV-targeted therapy of acute lung rejection in rats,” Journal of Heart and Lung Transplantation, vol. 25, no. 9, pp. 1109–1116, 2006. View at Publisher · View at Google Scholar · View at PubMed
  35. A. Belyaev, X. Zhang, K. Augustyns, et al., “Structure-activity relationship of diaryl phosphonate esters as potent irreversible dipeptidyl peptidase IV inhibitors,” Journal of Medicinal Chemistry, vol. 42, no. 6, pp. 1041–1052, 1999. View at Publisher · View at Google Scholar · View at PubMed
  36. A. J. Kenny, A. G. Booth, and S. G. George, “Dipeptidyl peptidase IV, a kidney brush border serine peptidase,” Biochemical Journal, vol. 157, no. 1, pp. 169–182, 1976.
  37. H. Fujiwara, T. Higuchi, Y. Sato, et al., “Regulation of human extravillous trophoblast function by membrane-bound peptidases,” Biochimica et Biophysica Acta, vol. 1751, no. 1, pp. 26–32, 2005. View at Publisher · View at Google Scholar · View at PubMed
  38. E. Fordel, E. Geuens, S. Dewilde, W. De Coen, and L. Moens, “Hypoxia/ischemia and the regulation of neuroglobin and cytoglobin expression,” IUBMB Life, vol. 56, no. 11-12, pp. 681–687, 2004. View at Publisher · View at Google Scholar · View at PubMed
  39. A. Pesce, M. Bolognesi, A. Bocedi, et al., “Neuroglobin and cytoglobin. Fresh blood for the vertebrate globin family,” EMBO Reports, vol. 3, no. 12, pp. 1146–1151, 2002. View at Publisher · View at Google Scholar · View at PubMed
  40. A. Shigematsu, Y. Adachi, J. Matsubara, et al., “Analyses of expression of cytoglobin by immunohistochemical studies in human tissues,” Hemoglobin, vol. 32, no. 3, pp. 287–296, 2008. View at Publisher · View at Google Scholar · View at PubMed
  41. T. Burmester, F. Gerlach, and T. Hankeln, “Regulation and role of neuroglobin and cytoglobin under hypoxia,” Advances in Experimental Medicine and Biology, vol. 618, pp. 169–180, 2007. View at Publisher · View at Google Scholar
  42. N. J. Hodges, N. Innocent, S. Dhanda, and M. Graham, “Cellular protection from oxidative DNA damage by over-expression of the novel globin cytoglobin in vitro,” Mutagenesis, vol. 23, no. 4, pp. 293–298, 2008. View at Publisher · View at Google Scholar · View at PubMed
  43. R. Xu, P. M. Harrison, M. Chen, et al., “Cytoglobin overexpression protects against damage-induced fibrosis,” Molecular Therapy, vol. 13, no. 6, pp. 1093–1100, 2006. View at Publisher · View at Google Scholar · View at PubMed