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Glutathione S-transferase is a good biomarker in acrylamide induced neurotoxicity and genotoxicity Cover

Glutathione S-transferase is a good biomarker in acrylamide induced neurotoxicity and genotoxicity

Open Access
|Mar 2019

References

  1. Abbott NJ, Rönnbäck L, Hansson E. (2006). Astrocyte–endothelial interactions at the blood–brain barrier. Nat Rev Neurosci7(1): 41–53.10.1038/nrn1824
  2. Abramovitz M, Listowsky I. (1987). Selective expression of a unique glutathione S-transferase Yb3 gene in rat brain. Journal of Biological Chemistry262(16): 7770–7773.10.1016/S0021-9258(18)47634-X
  3. Adler ID, Zouh R, Schmid E. (1993). Perturbation of cell division by acrylamide in vitro and in vivo. Mutat Res301(4): 249–54.10.1016/0165-7992(93)90065-4
  4. Allam A, El-Ghareeb AA, Abdul-Hamid M, Baikry A, Sabri MI. (2011). Prenatal and perinatal acrylamide disrupts the development of cerebellum in rat: biochemical and morphological studies. Toxicol Ind Health27(4): 1–16.10.1177/0748233710386412
  5. Allam AA, Abdul-Hamid M, Bakry A, El-Ghareeb A, Ajarem JS, Sabri M. (2013). Effect of acrylamide on cerebral neurons development in albino rat. Life Sci10(3): 1814–1825.
  6. Armstrong RN. (1994). Glutathione S-Transferases: Structure and Mechanism of an Archetypical Detoxication Enzyme. Adv Enzymol Relat Areas Mol Biol69: 1–44.10.1002/9780470123157.ch1
  7. Arakawa S. (2013). Utilization of glutathione S-transferase Mu 1-and Theta 1-null mice as animal models for absorption, distribution, metabolism, excretion and toxicity studies. Expert Opin Drug Metab Toxicol9(6): 725–736.10.1517/17425255.2013.780027
  8. Awad ME, Abdel-Rahman MS, Hassan SA. (1998). Acrylamide toxicity in isolated rat hepatocytes. Toxicol In Vitro12(6): 699–704.10.1016/S0887-2333(98)00051-4
  9. Besaratinia A, Pfeifer GP. (2003). Weak yet distinct mutagenicity of acrylamide in mammalian cells. J Natl Cancer Inst95(12): 889–896.10.1093/jnci/95.12.889
  10. Besaratinia A, Pfeifer GP. (2004). Genotoxicity of acrylamide and glycidamide. J Natl Cancer Inst96(13): 1023–1029.10.1093/jnci/djh186
  11. Björk K, Saarikoski ST, Arlinde C, Kovanen L, Osei-Hyiaman D, Ubaldi M, Reimers M, Hyytiä P, Heilig M, Sommer WH. (2006). Glutathione-S-transferase expression in the brain: possible role in ethanol preference and longevity. FASEB J20(11): 1826–1835.10.1096/fj.06-5896com
  12. Bull S. (2007). Review of Environmental Chemicals and Neurotoxicity: Focus on Neurological Diseases. Health Protection Agency, Govt. of UK.
  13. Cammer W, Tansey F, Abramovitz M, Ishigaki S, Listowsky I. (1989). Differential localization of glutathione-S-transferase Yp and Yb subunits in oligodendrocytes and astrocytes of rat brain. J Neurochem52(3): 876–883.10.1111/j.1471-4159.1989.tb02536.x
  14. Choi SD, Wania F. (2011). On the reversibility of environmental contamination with persistent organic pollutants. Environ Sci Technol45(20): 8834–8841.10.1021/es2017544
  15. da Fonseca RR, Johnson WE, O’Brien SJ, Vasconcelos V, Antunes A. (2010). Molecular evolution and the role of oxidative stress in the expansion and functional diversification of cytosolic glutathione transferases. BMC Evol Biol10(1): 281.10.1186/1471-2148-10-281
  16. Das M, Mukhtar H, Seth PK. (1982). Effect of acrylamide on brain and hepatic mixed-function oxidases and glutathione-S-transferase in rats. Toxicol Appl Pharmacol66(3): 420–6.10.1016/0041-008X(82)90308-8
  17. Dasari S, Ganjayi MS, Oruganti L, Balaji H, Meriga B. (2017a). Glutathione S-transferases Detoxify Endogenous and Exogenous Toxic Agents - Minireview. JDVAR5(5): 00154.10.15406/jdvar.2017.05.00154
  18. Dasari S, Ganjayi MS, Meriga B, Kedam T. (2017b). Developmental neurotoxicity of acrylamide: defensive role of chick embryo glutathione S-transferases. Adv Anim Vet Sci5(7): 299–306.
  19. Dearfield KL, Douglas GR, Ehling UH, Moore MM, Sega GA, Brusick DJ. (1995). Acrylamide: a review of its genotoxicity and an assessment of heritable genetic risk. Mutat Res330(1): 71–99.10.1016/0027-5107(95)00037-J
  20. de Leon J, Susce MT, Pan RM, Koch WH, Wedlund PJ. (2005). Polymorphic variations in GSTM1, GSTT1, PgP, CYP2D6, CYP3A5, and dopamine D2 and D3 receptors and their association with tardive dyskinesia in severe mental illness. J Clin Psychopharmacol25(5): 448–456.10.1097/01.jcp.0000177546.34799.af
  21. Deng H, He F, Zhang S, Calleman CJ, Costa LG. (1993). Quantitative measurements of vibration threshold in healthy adults and acrylamide workers. Int Arch Occup Environ Health65(1): 53–56.10.1007/BF00586059
  22. Ding Y, Ortelli F, Rossiter LC, Hemingway J, Ranson H. (2003). The Anopheles gambiae glutathione transferase supergene family: annotation, phylogeny and expression profiles. BMC Genomics4(1): 35.10.1186/1471-2164-4-35
  23. Duru NK, Morshedi M, Oehninger S. (2000). Effects of hydrogen peroxide on DNA and plasma membrane integrity of human spermatozoa. Fertil Steril74(6): 1200–1207.10.1016/S0015-0282(00)01591-0
  24. Ellinger-Ziegelbauer H, Gmuender H, Bandenburg A, Ahr HJ. (2008). Prediction of a carcinogenic potential of rat hepatocarcinogens using toxicogenomics analysis of short-term in vivo studies. Mutat Res637(1): 23–39.10.1016/j.mrfmmm.2007.06.010
  25. Frova C. (2006). Glutathione transferases in the genomics era: new insights and perspectives. Biomol Eng23(4): 149–169.10.1016/j.bioeng.2006.05.020
  26. Friedman M. (2003). Chemistry, biochemistry, and safety of acrylamide. A review. J Agric Food Chem51(16): 4504–4526.10.1021/jf030204+
  27. Garey J, Paule MG. (2010). Effects of chronic oral acrylamide exposure on incremental repeated acquisition (learning) task performance in Fischer 344 rats. Neurotoxicol Teratol32(2): 220–225.10.1016/j.ntt.2009.10.001
  28. Habig WH, Pabst MJ, Jakoby WB. (1974). Glutathione S-transferases the first enzymatic step in mercapturic acid formation. J Biol Chem249(22): 7130–7139.10.1016/S0021-9258(19)42083-8
  29. Hayes JD, Flanagan JU, Jowsey IR. (2005). Glutathione transferases. Annu Rev Pharmacol Toxicol45: 51–88.10.1146/annurev.pharmtox.45.120403.095857
  30. Hayes JD, Mclellan LI. (1999). Glutathione and glutathione-dependent enzymes represent a coordinately regulated defence against oxidative stress. Free Radic Res31(4): 273–300.10.1080/10715769900300851
  31. Hayes JD, Pulford DJ. (1995). The glut athione S-transferase supergene family: regulation of GST and the contribution of the lsoenzymes to cancer chemoprotection and drug resistance part II. Crit Rev Biochem Mol Biol30(6): 521–600.10.3109/10409239509083492
  32. Halliwell B, Gutteridge JM. (2015). Free radicals in biology and medicine. Oxford University Press, USA.10.1093/acprof:oso/9780198717478.001.0001
  33. Helm PA, Milne J, Hiriart-Baer V, Crozier P, Kolic T, Lega R, Chen T, MacPherson K, Gewurtz S, Winter J, Myers A. (2011). Lake-wide distribution and depositional history of current-and past-use persistent organic pollutants in Lake Simcoe, Ontario, Canada. J Great Lakes Res37: 132–141.10.1016/j.jglr.2011.03.016
  34. Hiratsuka A, Yokoi A, Sebata N, Watabe T, Hatayama I, Sato K. (1989). Glutathione conjugation of the fluorophotometric epoxide substrate, 7-glycidoxycoumarin (GOC), by rat liver glutathione transferase isoenzymes. Biochem Pharmacol38(16): 2609–2613.10.1016/0006-2952(89)90545-5
  35. Honig LS, Rosenberg RN. (2000). Apoptosis and neurologic disease. The Am J Med108(4): 317–330.10.1016/S0002-9343(00)00291-6
  36. Johnson JA, el Barbary AI, Kornguth SE, Brugge JF, Siegel FL. (1993). Glutathione S-transferase isoenzymes in rat brain neurons and glia. J Neurosci13(5): 2013–2023.10.1523/JNEUROSCI.13-05-02013.1993
  37. Konings EJ, Baars AJ, Van Klaveren JD, Spanjer MC, Rensen PM, Hiemstra M, Van Kooij JA, Peters PW. (2003). Acrylamide exposure from foods of the Dutch population and an assessment of the consequent risks. Food Chem Toxicol41(11): 1569–1579.10.1016/S0278-6915(03)00187-X
  38. Korte F, Kvesitadze G, Ugrekhelidze D, Gordeziani M, Khatisashvili G, Buadze O, Zaalishvili G, Coulston F. (2000). Organic toxicants and plants. Ecotoxicology and environmental safety47(1): 1–26.10.1006/eesa.2000.1929
  39. Kumar A, Dhull DK, Gupta V, Channana P, Singh A, Bhardwaj M, Ruhal P, Mittal R. (2017). Role of Glutathione-S-transferases in neurological problems. Expert Opin Ther Pat27(3): 299–309.10.1080/13543776.2017.1254192
  40. Lehning EJ, Balaban CD, Ross JF, LoPachin RM. (2003). Acrylamide neuropathy: II. Spatiotemporal characteristics of nerve cell damage in brainstem and spinal cord. Neurotoxicology24(1): 109–23.10.1016/S0161-813X(02)00192-4
  41. Lo HW, Ali-Osman F. (2007). Genetic polymorphism and function of glutathione S-transferases in tumor drug resistance. Curr Opin Pharmacol7(4): 367–374.10.1016/j.coph.2007.06.009
  42. LoPachin RM, Balaban CD, Ross JF. (2003). Acrylamide axonopathy revisited. Toxicol Appl Pharmacol188(3): 135–153.10.1016/S0041-008X(02)00072-8
  43. LoPachin RM, DeCaprio AP. (2005). Protein adduct formation as a molecular mechanism in neurotoxicity. Toxicol Sci86(2): 214–225.10.1093/toxsci/kfi197
  44. LoPachin RM, Barber DS, He D, Das S. (2006). Acrylamide inhibits dopamine uptake in rat striatal synaptic vesicles. Toxicol Sci89(1): 224–234.10.1093/toxsci/kfj005
  45. LoPachin RM, Gavin T. (2012). Molecular mechanism of acrylamide neurotoxicity: lessons learned from organic chemistry. Environ Health Perspect120(12): 1650–1657.10.1289/ehp.1205432
  46. Maier A, Kohrman-Vincent M, Hertzberg R, Allen B, Haber LT, Dourson M. (2012). Critical review of dose–response options for F344 rat mammary tumors for acrylamide–Additional insights based on mode of action. Food Chem Toxicol50(5): 1763–1775.10.1016/j.fct.2012.02.002
  47. Mannervik B, Danielson UH, Ketterer B. (1988). Glutathione transferases—structure and catalytic activity. CRC Crit Rev Biochem23(3): 283–337.10.3109/10409238809088226
  48. Mannervik B. (1986). Glutathione and the evolution of enzymes for detoxication of products of oxygen metabolism. Chemica Scripta263: 281–284.
  49. Martinez-Lara E, Siles E, Hernández R, Cañuelo AR, del Moral ML, Jiménez A, Blanco S, López-Ramos JC, Esteban FJ, Pedrosa JA, Peinado MA. (2003). Glutathione S-transferase isoenzymatic response to aging in rat cerebral cortex and cerebellum. Neurobiol Aging24(3): 501–509.10.1016/S0197-4580(02)00139-2
  50. Mottram DS, Wedzicha BL, Dodson AT. (2002). Food chemistry: acrylamide is formed in the Maillard reaction. Nature419(6906): 448–449.10.1038/419448a
  51. Nordin-Andersson M, Walum E, Kjellstrand P, Forsby A. (2003). Acrylamideinduced effects on general and neurospecific cellular functions during exposure and recovery. Cell Biol Toxicol19(1): 43–51.10.1023/A:1022017731328
  52. Haider RA, Robin MA, Fang JK, Avadhani NG. (2002). Multiple isoforms of mitochondrial glutathione S-transferases and their differential induction under oxidative stress. Biochem J366(1): 45–55.10.1042/bj20020533
  53. Rydberg P, Eriksson S, Tareke E, Karlsson P, Ehrenberg L, Törnqvist M. (2003). Investigations of factors that influence the acrylamide content of heated foodstuffs. J Agric Food Chem51(24): 7012–7018.10.1021/jf034649+
  54. Satoh K, Hatayama I, Tsuchida S, Sato K. (1991). Biochemical characteristics of a preneoplastic marker enzyme glutathione S-transferase P-form (7-7). Arch Biochem Biophys285(2): 312–316.10.1016/0003-9861(91)90365-P
  55. Seale SM, Feng Q, Agarwal AK, El-Alfy AT. (2012). Neurobehavioral and transcriptional effects of acrylamide in juvenile rats. Pharmacol Biochem Behav101(1): 77–84.10.1016/j.pbb.2011.12.006
  56. Shao L, Young LT, Wang JF. (2005). Chronic treatment with mood stabilizers lithium and valproate prevents excitotoxicity by inhibiting oxidative stress in rat cerebral cortical cells. Biol Psychiatry58(11): 879–884.10.1016/j.biopsych.2005.04.052
  57. Sheehan D, MEADE G, FOLEY VM. (2001). Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily. Biochem J360(1): 1–6.10.1042/bj3600001
  58. Shukla PK, Khanna VK, Ali MM, Maurya RR, Handa SS, Srimal RC. 2002. Protective effect of Acorus calamus against acrylamide induced neurotoxicity. Phytother Res16(3): 256–60.10.1002/ptr.85412164272
  59. Sreenivasulu D, Balaji M. (2016). Rat brain glutathione S-transferases potentially defends acrylamide induced neurotoxicity and genotoxicity. IOSR-JBB2(6): 75–80.
  60. Srivastava S, Sabri MI, Agrawal AK, Seth PK. (1986). Effect of single and repeated doses of acrylamide and bis-acrylamide on glutathione-S-transferase and dopamine receptors in rat brain. Brain Res371(2): 319–23.10.1016/0006-8993(86)90369-0
  61. Struzynska L, Sulkowski G, Lenkiewicz A, Rafalowska U. (2002). Lead stimulates the glutathione system in selective regions of rat brain. Folia Neuropathol40(4): 203–209.
  62. Stadler RH, Blank I, Varga N, Robert F, Hau J, Guy PA, Robert MC, Riediker S. (2002). Food chemistry: acrylamide from Maillard reaction products. Nature419(6906): 449–450.10.1038/419449a
  63. Tansey FA, Cammer W. (1991). A Pi Form of Glutathione-S-Transferase Is a Myelin-and Oligodendrocyte-Associated Enzyme in Mouse Brain. Journal of neurochemistry57(1): 95–102.10.1111/j.1471-4159.1991.tb02104.x
  64. Tareke E, Rydberg P, Karlsson P, Eriksson S, Törnqvist M. (2002). Analysis of acrylamide, a carcinogen formed in heated foodstuffs. J Agric Food Chem50(17): 4998–5006.10.1021/jf020302f
  65. Van der Oost R, Beyer J, Vermeulen NP. (2003). Fish bioaccumulation and bio-markers in environmental risk assessment: a review. Environ Toxicol Pharmacol13(2): 57–149.10.1016/S1382-6689(02)00126-6
  66. Weiss G. (2002). Acrylamide in food: Uncharted territory. Science297(5578): 27.10.1126/science.297.5578.27a
  67. Wilce MC, Board PG, Feil SC, Parker MW. (1995). Crystal structure of a theta-class glutathione transferase. EMBO J14(10): 2133–2143.10.1002/j.1460-2075.1995.tb07207.x
  68. Yang HJ, Lee SH, Jin Y, Choi JH, Han CH, Lee MH. (2005). Genotoxicity and toxicological effects of acrylamide on reproductive system in male rats. J Vet Sci6(2): 103–109.10.4142/jvs.2005.6.2.103
  69. Yousef MI, El-Demerdash FM. (2006). Acrylamide-induced oxidative stress and biochemical perturbations in rats. Toxicology219(1): 133–141.10.1016/j.tox.2005.11.008
  70. Zhang L, Gavin T, Barber DS, LoPachin RM. (2011). Role of the Nrf2-ARE pathway in acrylamide neurotoxicity. Toxicol Lett205(1): 1–7.10.1016/j.toxlet.2011.04.011
  71. Zhang M, Chen M, Tong W. (2011). Is toxicogenomics a more reliable and sensitive biomarker than conventional indicators from rats to predict drug-induced liver injury in humans? Chem Res Toxicol25(1): 122–129.10.1021/tx200320e22122743
  72. Zimniak P. (2008). Detoxification reactions: relevance to aging. Ageing Res Rev7(4): 281–300.10.1016/j.arr.2008.04.001
DOI: https://doi.org/10.2478/intox-2018-0007 | Journal eISSN: 1337-9569 | Journal ISSN: 1337-6853
Language: English
Page range: 115 - 121
Submitted on: Jun 29, 2017
Accepted on: Dec 13, 2017
Published on: Mar 2, 2019
Published by: Slovak Academy of Sciences, Institute of Experimental Pharmacology & Toxicology, Centre of Experimental Medicine
In partnership with: Paradigm Publishing Services
Publication frequency: 4 issues per year

© 2019 Sreenivasulu Dasari, Muni Swamy Ganjayi, Balaji Meriga, published by Slovak Academy of Sciences, Institute of Experimental Pharmacology & Toxicology, Centre of Experimental Medicine
This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.