DOI QR코드

DOI QR Code

Overexpression of Ref-1 Inhibits Lead-induced Endothelial Cell Death via the Upregulation of Catalase

  • Lee, Kwon-Ho (Department of Physiology, School of Medicine, Chungnam National University) ;
  • Lee, Sang-Ki (Department of Physiology, School of Medicine, Chungnam National University) ;
  • Kim, Hyo-Shin (Department of Physiology, School of Medicine, Chungnam National University) ;
  • Cho, Eun-Jung (Department of Physiology, School of Medicine, Chungnam National University) ;
  • Joo, Hee-Kyoung (Department of Physiology, School of Medicine, Chungnam National University) ;
  • Lee, Eun-Ji (Department of Physiology, School of Medicine, Chungnam National University) ;
  • Lee, Ji-Young (Department of Physiology, School of Medicine, Chungnam National University) ;
  • Park, Myoung-Soo (Department of Physiology, School of Medicine, Chungnam National University) ;
  • Chang, Seok-Jong (Department of Physiology, College of Medicine, Seonam University) ;
  • Cho, Chung-Hyun (Department of Physiology, School of Medicine, Chungnam National University) ;
  • Park, Jin-Bong (Department of Physiology, School of Medicine, Chungnam National University) ;
  • Jeon, Byeong-Hwa (Department of Physiology, School of Medicine, Chungnam National University)
  • 발행 : 2009.12.31

초록

The role of apurinic/apyrimidinic endonuclease1/redox factor-1 (Ref-1) on the lead (Pb)-induced cellular response was investigated in the cultured endothelial cells. Pb caused progressive cellular death in endothelial cells, which occurred in a concentration- and time-dependent manner. However, Ref-1 overexpression with AdRef-1 significantly inhibited Pb-induced cell death in the endothelial cells. Also the overexpression of Ref-1 significantly suppressed Pb-induced superoxide and hydrogen peroxide elevation in the endothelial cells. Pb exposure induced the downregulation of catalase, it was inhibited by the Ref-1 overexpression in the endothelial cells. Taken together, our data suggests that the overexpression of Ref-1 inhibited Pb-induced cell death via the upregulation of catalase in the cultured endothelial cells.

키워드

참고문헌

  1. Adhikari N, Sinha N, Narayan R, Saxena DK. Lead-induced cell death in testes of young rats. J Appl Toxicol 21: 275-277, 2001 https://doi.org/10.1002/jat.754
  2. Angkeow P, Deshpande SS, Qi B, Liu YX, Park YC, Jeon BH, Ozaki M, Irani K. Redox factor-1: an extra-nuclear role in the regulation of endothelial oxidative stress and apoptosis. Cell Death Differ 9: 717-725, 2002 https://doi.org/10.1038/sj.cdd.4401025
  3. Cheng YJ, Yang BC, Hsieh WC, Huang BM, Liu MY. Enhancement of TNF-alpha expression does not trigger apoptosis upon exposure of glial cells to lead and lipopolysaccharide. Toxicology 178: 183-191, 2002 https://doi.org/10.1016/S0300-483X(02)00225-1
  4. Chetty CS, Vemuri MC, Reddy GR, Suresh C. Protective effect of 17-beta-estradiol in human neurocellular models of lead exposure. Neurotoxicology 28: 396-401, 2007 https://doi.org/10.1016/j.neuro.2006.03.012
  5. Chovolou Y, Watjen W, Kampkotter A, Kahl R. Resistance to tumor necrosis factor-alpha (TNF-alpha)-induced apoptosis in rat hepatoma cells expressing TNF-alpha is linked to low antioxidant enzyme expression. J Biol Chem 278: 29626-29632, 2003 https://doi.org/10.1074/jbc.M208665200
  6. Clerch LB, Massaro D. Oxidation-reduction-sensitive binding of lung protein to rat catalase mRNA. J Biol Chem 267: 2853-2855, 1992
  7. Clerch LB, Wright A, Chung DJ, Massaro D. Early divergent lung antioxidant enzyme expression in response to lipopolysaccharide. Am J Physiol 271: L949-954, 1996
  8. Demple B, Herman T, Chen DS. Cloning and expression of APE, the cDNA encoding the major human apurinic endonuclease: definition of a family of DNA repair enzymes. Proc Natl Acad Sci U S A 88: 11450-11454, 1991 https://doi.org/10.1073/pnas.88.24.11450
  9. Ercal N, Gurer-Orhan H, Aykin-Burns N. Toxic metals and oxidative stress part I: mechanisms involved in metal-induced oxidative damage. Curr Top Med Chem 1: 529-539, 2001 https://doi.org/10.2174/1568026013394831
  10. Evans AR, Limp-Foster M, Kelley MR. Going APE over ref-1. Mutat Res 461: 83-108, 2000 https://doi.org/10.1016/S0921-8777(00)00046-X
  11. Fischer JL, Lancia JK, Mathur A, Smith ML. Selenium protection from DNA damage involves a Ref1/p53/Brca1 protein complex. Anticancer Res 26: 899-904, 2006
  12. Fox DA, He L, Poblenz AT, Medrano CJ, Blocker YS, Srivastava D. Lead-induced alterations in retinal cGMP phosphodiesterase trigger calcium overload, mitochondrial dysfunction and rod photoreceptor apoptosis. Toxicol Lett 102-103: 359-361, 1998 https://doi.org/10.1016/S0378-4274(98)00232-X
  13. Gonick HC, Ding Y, Bondy SC, Ni Z, Vaziri ND. Lead-induced hypertension: interplay of nitric oxide and reactive oxygen species. Hypertension 30: 1487-1492, 1997
  14. Grosch S, Fritz G, Kaina B. Apurinic endonuclease (Ref-1) is induced in mammalian cells by oxidative stress and involved in clastogenic adaptation. Cancer Res 58: 4410-4416, 1998
  15. Hsu JM. Lead toxicity as related to glutathione metabolism. J Nutr 111: 26-33, 1981
  16. Hsu PC, Guo YL. Antioxidant nutrients and lead toxicity. Toxicology 180: 33-44, 2002 https://doi.org/10.1016/S0300-483X(02)00380-3
  17. Hunaiti A, Soud M, Khalil A. Lead concentration and the level of glutathione, glutathione S-transferase, reductase and peroxidase in the blood of some occupational workers from Irbid City, Jordan. Sci Total Environ 170: 95-100, 1995 https://doi.org/10.1016/0048-9697(95)04606-2
  18. Jeon BH, Gupta G, Park YC, Qi B, Haile A, Khanday FA, Liu YX, Kim JM, Ozaki M, White AR, Berkowitz DE, Irani K. Apurinic/ apyrmidinic endonuclease 1 regulates endothelial NO production and vascular tone. Circ Res 95: 902-910, 2004 https://doi.org/10.1161/01.RES.0000146947.84294.4c
  19. Kim CS, Son SJ, Kim EK, Kim SN, Yoo DG, Kim HS, Ryoo SW, Lee SD, Irani K, Jeon BH. Apurinic/apyrimidinic endonuclease1/ redox factor-1 inhibits monocyte adhesion in endothelial cells. Cardiovasc Res 69: 520-526, 2006 https://doi.org/10.1016/j.cardiores.2005.10.014
  20. Lee HM, Jeon BH, Won KJ, Lee CK, Park TK, Choi WS, Bae YM, Kim HS, Lee SK, Park SH, Irani K, Kim B. Gene transfer of redox factor-1 inhibits neointimal formation: involvement of platelet-derived growth factor-beta receptor signaling via the inhibition of the reactive oxygen species-mediated Syk pathway. Circ Res 104: 219-227, 2009 https://doi.org/10.1161/CIRCRESAHA.108.178699
  21. Lupertz R, Chovolou Y, Kampkotter A, Watjen W, Kahl R. Catalase overexpression impairs TNF-alpha induced NF-kappaB activation and sensitizes MCF-7 cells against TNF-alpha. J Cell Biochem 103: 1497-1511, 2008 https://doi.org/10.1002/jcb.21538
  22. Massanyi P, Lukac N, Makarevich AV, Chrenek P, Forgacs Z, Zakrzewski M, Stawarz R, Toman R, Lazor P, Flesarova S. Lead-induced alterations in rat kidneys and testes in vivo. J Environ Sci Health A Tox Hazard Subst Environ Eng 42: 671-676, 2007 https://doi.org/10.1080/10934520701244474
  23. Mosmann T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J Immunol Methods 65: 55-63, 1983 https://doi.org/10.1016/0022-1759(83)90303-4
  24. Nakamura H, Nakamura K, Yodoi J. Redox regulation of cellular activation. Annu Rev Immunol 15: 351-369, 1997 https://doi.org/10.1146/annurev.immunol.15.1.351
  25. Nenoi M, Ichimura S, Mita K, Yukawa O, Cartwright IL. Regulation of the catalase gene promoter by Sp1, CCAAT-recognizing factors, and a WT1/Egr-related factor in hydrogen peroxide-resistant HP100 cells. Cancer Res 61: 5885-5894, 2001
  26. Ni Z, Hou S, Barton CH, Vaziri ND. Lead exposure raises superoxide and hydrogen peroxide in human endothelial and vascular smooth muscle cells. Kidney Int 66: 2329-2336, 2004 https://doi.org/10.1111/j.1523-1755.2004.66032.x
  27. Ozaki M, Suzuki S, Irani K. Redox factor-1/APE suppresses oxidative stress by inhibiting the rac1 GTPase. FASEB J 16: 889-890, 2002
  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 11: 114-127, 2006
  29. Sharp DS, Osterloh J, Becker CE, Bernard B, Smith AH, Fisher JM, Syme SL, Holman BL, Johnston T. Blood pressure and blood lead concentration in bus drivers. Environ Health Perspect 78: 131-137, 1988 https://doi.org/10.2307/3430514
  30. Silber JR, Bobola MS, Blank A, Schoeler KD, Haroldson PD, Huynh MB, Kolstoe DD. The apurinic/apyrimidinic endonuclease activity of Ape1/Ref-1 contributes to human glioma cell resistance to alkylating agents and is elevated by oxidative stress. Clin Cancer Res 8: 3008-3018, 2002
  31. Song YJ, Lee JY, Joo HK, Kim HS, Lee SK, Lee KH, Cho CH, Park JB, Jeon BH. Tat-APE1/ref-1 protein inhibits TNF-alpha-induced endothelial cell activation. Biochem Biophys Res Commun 368: 68-73, 2008 https://doi.org/10.1016/j.bbrc.2008.01.037
  32. Stacchiotti A, Morandini F, Bettoni F, Schena I, Lavazza A, Grigolato PG, Apostoli P, Rezzani R, Aleo MF. Stress proteins and oxidative damage in a renal derived cell line exposed to inorganic mercury and lead. Toxicology 264: 215-224, 2009 https://doi.org/10.1016/j.tox.2009.08.014
  33. Suresh C, Dennis AO, Heinz J, Vemuri MC, Chetty CS. Melatonin protection against lead-induced changes in human neuroblastoma cell cultures. Int J Toxicol 25: 459-464, 2006 https://doi.org/10.1080/10915810600959576
  34. Tell G, Damante G, Caldwell D, Kelley MR. The intracellular localization of APE1/Ref-1: more than a passive phenomenon? Antioxid Redox Signal 7: 367-384, 2005 https://doi.org/10.1089/ars.2005.7.367
  35. Tomicic M, Eschbach E, Kaina B. Expression of yeast but not human apurinic/apyrimidinic endonuclease renders Chinese hamster cells more resistant to DNA damaging agents. Mutat Res 383: 155-165, 1997 https://doi.org/10.1016/S0921-8777(96)00055-9
  36. Ushakova T, Melkonyan H, Nikonova L, Afanasyev V, Gaziev AI, Mudrik N, Bradbury R, Gogvadze V. Modification of gene expression by dietary antioxidants in radiation-induced apoptosis of mice splenocytes. Free Radic Biol Med 26: 887-891, 1999 https://doi.org/10.1016/S0891-5849(98)00281-0
  37. Vaziri ND. Pathogenesis of lead-induced hypertension: role of oxidative stress. J Hypertens Suppl 20: S15-20, 2002
  38. Vaziri ND, Lin CY, Farmand F, Sindhu RK. Superoxide dismutase, catalase, glutathione peroxidase and NADPH oxidase in lead- induced hypertension. Kidney Int 63: 186-194, 2003 https://doi.org/10.1046/j.1523-1755.2003.00711.x
  39. Wang L, Wang H, Hu M, Cao J, Chen D, Liu Z. Oxidative stress and apoptotic changes in primary cultures of rat proximal tubular cells exposed to lead. Arch Toxicol 83: 417-427, 2009 https://doi.org/10.1007/s00204-009-0425-z
  40. Wassmann S, Wassmann K, Nickenig G. Modulation of oxidant and antioxidant enzyme expression and function in vascular cells. Hypertension 44: 381-386, 2004 https://doi.org/10.1161/01.HYP.0000142232.29764.a7
  41. Yoo YH, Lim YJ, Park SE, Kim JM, Park YC. Overexpression of redox factor-1 negatively regulates NO synthesis and apoptosis in LPS-stimulated RAW 264.7 macrophages. FEBS Lett 556: 39-42, 2004 https://doi.org/10.1016/S0014-5793(03)01361-9

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