Effects of selenocystine on lead-exposed Chinese hamster ovary (CHO) and PC-12 cells

Toxicology and Applied Pharmacology

Volumn 214, Issue 2, 2006, Pages 136-143

  Aykin Burns, Nukhet ^a   Ercal, Nuran ^a  

^a MISSOURI UNIVERSITY OF SCIENCE AND TECHNOLOGY   (United States)

Author keywords

Lead toxicity; Reactive oxygen species; Selenocysteine; Thiol antioxidants

Indexed keywords

CATALASE; GLUTATHIONE; GLUTATHIONE DISULFIDE; LEAD; MALONALDEHYDE; SELENOCYSTINE;

ANIMAL CELL; ARTICLE; CELL CULTURE; CELL LINE; CELL PROLIFERATION; CELL STRAIN; CHO CELL; COLONY FORMATION; CONTROLLED STUDY; ENZYME ACTIVITY; FEMALE; IN VITRO STUDY; INCUBATION TIME; NERVE CELL; NEURITE; NEUROTOXICITY; NONHUMAN; OXIDATIVE STRESS; STATISTICAL SIGNIFICANCE;

ANIMALS; APOPTOSIS; CASPASE 3; CASPASES; CATALASE; CELL PROLIFERATION; CHO CELLS; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CRICETINAE; CRICETULUS; CYSTINE; DOSE-RESPONSE RELATIONSHIP, DRUG; GLUTATHIONE DISULFIDE; GLUTATHIONE PEROXIDASE; MALONDIALDEHYDE; NEURITES; ORGANOMETALLIC COMPOUNDS; ORGANOSELENIUM COMPOUNDS; PC12 CELLS; PROTEIN KINASE C; RATS;

CRICETULUS GRISEUS;

EID: 33745683902     PISSN: 0041008X     EISSN: 10960333     Source Type: Journal    
DOI: 10.1016/j.taap.2005.12.002     Document Type: Article

References (50)

1. Aebi H. Catalase in vitro. In: Packer L. (Ed). Methods Enzymol. vol. 105 (1984), Academic Press, NewYork 121-126
2. Apfel S.C., Arezzo J.C., Lipton R.B., and Kessler J.A. Nerve growth factor prevents experimental cisplatin neuropathy. Ann. Neurol. 31 (1992) 76-80
3. Ayaz M., Ozdemir S., Ugur M., Vassort G., and Turan B. Effects of selenium on altered mechanical and electrical cardiac activities of diabetic rat. Arch. Biochem. Biophys. 1 426 (2004) 83-90
4. Aykin-Burns N., Franklin E.A., and Ercal N. Effects of N-acetylcysteine on lead-exposed PC-12 cells. Arch. Environ. Contam. Toxicol. 49 (2005) 119-123
5. Bank B., DeWeer A., Kuzirian A.M., Ramussen H., and Alkon D.L. Classical conditioning induces long-term translocation of protein kinase C in rabbit hippocampal CA1 cells. Proc. Natl. Acad. Sci. 85 (1988) 1988-1992
6. Baron W., de Jonge J.C., de Vries H., and Hoekstra D. Regulation of oligodendrocyte differentiation: protein kinase C activation prevents differentiation of O-2A progenitor cells toward oligodendrocytes. Glia 22 (1998) 121-129
7. Baron W., de Jonge J.C., de Vries H., and Hoekstra D. Protein kinase C prevents oligodendrocyte differentiation: modulation of actin cytoskeleton and cognate polarized membrane traffic. J. Neurobiol. 41 (1999) 385-398
8. Beers R.F., and Sizer I.W. A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J. Biol. Chem. 195 (1952) 133-140
9. Bjornstedt M., Kumar S., Bjorkhem L., Spyrou G., and Holmgren A. Selenium and the thioredoxin and glutaredoxin systems. Biomed. Environ. Sci. 10 (1997) 271-279
10. Brown K.M., and Arthur J.R. Selenium, selenoproteins and human health: a review. Public Health Nutr. 4 2B (2001) 593-599
11. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-256
12. Burk R.F., Nishiki K., Lawrence R.A., and Chance B. Peroxide removal by selenium-dependent and selenium-independent glutathione peroxidase in hemoglobin-free perfused rat liver. J. Biol. Chem. 10 (1978) 43-46
13. Chen H.H., Ma T., and Ho I.K. Protein kinase C in rat brain is altered by developmental lead exposure. Neurochem. Res. 24 (1998) 415-421
14. Chen H.H., Ma T., Hume A.S., and Ho I.K. Developmental lead exposure alters the distribution of protein kinase C activity in the rat hippocampus. Biomed. Environ. Sci. 11 (1998) 61-69
15. Deng W., and Poretz R.D. Protein kinase C activation is required for the lead-induced inhibition and differentiation of cultured oligodendroglial progenitor cells. Brain Res. 929 (2002) 87-95
16. Draper H.H., Squires E.J., Mahmoodi H., and Agarwal J.S. A comparative evaluation of thiobarbituric acid methods for the determination of malondialdehyde in biological materials. Free Radical Biol. Med. 15 (1993) 353-363
17. Dursun N., Arifoglu C., Suer C., and Keskinol L. Blood pressure relationship to nitric oxide, lipid peroxidation, renal function, and renal blood flow in rats exposed to low lead levels. Biol. Trace Elem. Res. 104 (2005) 141-149
18. Ercal N., Treeratphan P., Lutz P.M., Hammond T.C., and Matthews R.H. N-acetylcysteine protects Chinese Hamster Ovary (CHO) cells from lead-induced oxidative stress. Toxicology 108 (1996) 57-64
19. 2+ dependent isoenzymes of protein kinase C. Arch. Biochem. Biophys. 348 (1997) 25-36
20. Gurer H., and Ercal N. Can antioxidants be beneficial in the treatment of lead poisoning. Free Radical Biol. Med. 29 (2000) 927-945
21. Gurer H., Ozgunes H., Neal R., Spitz D.R., and Ercal N. Antioxidant effects of N-acetylcysteine and succimer in red blood cells from the lead exposed rats. Toxicology 128 (1998) 181-189
22. Gurer H., Neal R., Yang P., Oztezcan S., and Ercal N. Captopril as an antioxidant in lead-exposed Fischer 344 rats. Hum. Exp. Toxicol. 18 (1999) 27-32
23. Gurer H., Ozgunes H., Oztezcan S., and Ercal N. Antioxidant role of alpha-lipoic acid in lead toxicity. Free Radical Biol. Med. 27 (1999) 75-81
24. Gurer H., Ozgunes H., Saygin E., and Ercal N. Antioxidant effect of taurine against lead-induced oxidative stress. Arch. Environ. Contam. Toxicol. 41 (2001) 397-402
25. Hilliard A., Ramesh A., and Zawia N.H. Correlation between lead-induced changes in cerebral ornithine decarboxylase and protein kinase C activities during development and in cultured PC-12 cells. Int. J. Neurosci. 17 (1999) 777-785
26. Hossain M.M.D., Takashima A., Nakayama H., and Doi K. 5-Azacytidine induces toxicity in PC-12 cells by apoptosis. Exp. Toxicol. Pathol. 49 (1997) 201-206
27. Ip C., Hayes C., Budnick RM., and Ganther HE. Chemical form of selenium, critical metabolites, and cancer prevention. Cancer Res. 51 2 (1991) 595-600
28. Lavender O.A., Morris V.C., and Ferretti R.J. Comparative effects of selenium and vitamin E in lead-poisoned rats. J. Nutr. 107 3 (1997) 378-392
29. Lawrence R.A., and Burk R.F. Glutathione peroxidase activity in selenium-deficient rat liver. Biochem. Biophys. Res. Commun. 71 (1976) 952-958
30. Maccarone M., and Catani M.V. Involvement of 5-lipoxygenase in programmed cells death of cancer cells. Cell Death Differ. 4 (1997) 396-402
31. Markovac J., and Goldstein G.W. Picomolar concentrations of lead stimulate brain protein kinase C. Nature 334 (1988) 71-73
32. Morel Y., and Barouki R. Repression of gene expression by oxidative stress. Biochem. J. 342 (1999) 481-496
33. Nagata S. Apoptosis by death factor. Cell 88 (1997) 355-365
34. Neal R., Cooper K., Kellog G., Gurer H., and Ercal N. Effects of some sulfur-containing antioxidants on lead-exposed lenses. Free Radical Biol. Med. 26 (1999) 239-243
35. Nehru B., and Kanwar S.S. N-acetylcysteine exposure on lead-induced lipid peroxidative damage and oxidative defense system in brain regions of rats. Biol. Trace Elem. Res. 101 (2004) 257-264
36. Othman A.I., and El Missiry M. Role of selenium against lead toxicity in male rats. J. Biochem. Mol. Toxicol. 12 (1998) 345-349
37. Pfrieger F.W., and Barres B.A. Synaptic efficacy enhanced by glial cells in vitro. Science 227 (1997) 1684-1687
38. Ramesh G.T., and Jadhav A.L. Levels of protein kinase C and nitric oxide synthase activity in rats exposed to sub chronic low level lead. Mol. Cell. Biochem. 223 (2001) 27-33
39. Rayman M.P. The importance of selenium to human health. Lancet 356 9225 (2000) 233-241
40. Rayman M.P. Selenium in cancer prevention: a review of the evidence and mechanism of action. Proc. Nutr. Soc. 64 4 (2005) 527-542
41. Rotruck J.T., Pope A.L., Ganther H.E., Swanson A.B., Hafeman D.G., and Hoekstra W.G. Selenium: biochemical role as a component of glutathione peroxidase. Science 179 (1973) 588-590
42. Sanchez I., Hassinger L., Paskevich P.A., Shine H.D., and Nixon R.A. Oligodendroglia regulate the regional expansion of axon caliber and local accumulation of microfilaments during development independently of myelin formation. J. Neurosci. 16 (1996) 5095-5105
43. Sarafian T.A., and Bredesen D.E. Is apoptosis mediated by ROS?. Free Radical Res. 21 (1994) 1-8
44. Sharifi A.M., Baniasadi S., Jorjani M., Rahimi F., and Bakhayesh M. Investigation of acute lead poisoning on apoptosis in rat hippocampus in vivo. Neurosci. Lett. 329 (2002) 45-48
45. Sies H. Oxidative stress: introductory remarks. In: Sies H. (Ed). Oxidative Stress: Oxidants and Antioxidants (1985), Academic Press, San Diego 15-22
46. Soltaninejad K., Kebriaeezadeh A., Minaiee B., Ostad S.N., Hosseini R., Azizi E., and Abdollahi M. Biochemical and ultrastructural evidences for toxicity of lead through free radicals in rat brain. Hum. Exp. Toxicol. 22 (2003) 417-423
47. Sortwell C.E., Daley B.F., Pitzer M.R., McGuire S.O., Sladek J.R., and Collier T.J. Oligodendrocyte-type 2 astrocyte-derived trophic factors increase survival of developing dopamine neurons through the inhibition of apoptotic cell death. J. Comp. Neurol. 426 (2000) 143-153
48. Stadtman T.C. Selenocysteine. Annu. Rev. Biochem. 65 (1996) 83-100
49. Winters R.A., Zukowski J., Ercal N., Matthews R.H., and Spitz D.R. Analyisis of glutathione, glutathione disulfide, cysteine, homoycsteine, and other biological thiols by high performance liquid chromatography following derivatiziation with N-(1-Pyrenyl) maleimide. Anal. Biochem. 227 (1995) 14-21
50. Yusof M., Yildiz D., and Ercal N. N-acetyl-l-cysteine protects against δ-aminolevulinic acid-induced 8-hydroxydeoxyguanosine formation. Toxicol. Lett. 106 (1999) 41-47