Table of Contents Author Guidelines Submit a Manuscript
Autism Research and Treatment
Volume 2014, Article ID 164938, 15 pages
http://dx.doi.org/10.1155/2014/164938
Review Article

Potential Role of Selenoenzymes and Antioxidant Metabolism in relation to Autism Etiology and Pathology

1Energy & Environmental Research Center, University of North Dakota, 15 North 23rd Street, Stop 9018, Grand Forks, ND 58202, USA
2Department of Pharmaceutical Sciences, Northeastern University, Boston, MA 02115, USA

Received 11 September 2013; Revised 7 January 2014; Accepted 27 January 2014; Published 5 March 2014

Academic Editor: Klaus-Peter Ossenkopp

Copyright © 2014 Laura J. Raymond 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. A. M. Persico and T. Bourgeron, “Searching for ways out of the autism maze: genetic, epigenetic and environmental clues,” Trends in Neurosciences, vol. 29, no. 7, pp. 349–358, 2006. View at Publisher · View at Google Scholar · View at Scopus
  2. F. R. Zahir and C. J. Brown, “Epigenetic impacts on neurodevelopment: pathophysiological mechanisms and genetic modes of action,” Pediatric Research, vol. 69, no. 5, pp. 92R–100R, 2011. View at Publisher · View at Google Scholar · View at Scopus
  3. M. R. Herbert, “SHANK3, the synapse, and autism,” The New England Journal of Medicine, vol. 365, no. 2, pp. 173–175, 2011. View at Publisher · View at Google Scholar · View at Scopus
  4. E. Fombonne, “Epidemiology of autistic disorder and other pervasive developmental disorders,” The Journal of Clinical Psychiatry, vol. 66, supplement 10, pp. 3–8, 2005. View at Google Scholar · View at Scopus
  5. I. N. Pessah, R. F. Seegal, P. J. Lein et al., “Immunologic and neurodevelopmental susceptibilities of autism,” NeuroToxicology, vol. 29, no. 3, pp. 532–545, 2008. View at Publisher · View at Google Scholar · View at Scopus
  6. M. L. Bauman, “Medical comorbidities in autism: challenges to diagnosis and treatment,” Neurotherapeutics, vol. 7, no. 3, pp. 320–327, 2010. View at Publisher · View at Google Scholar · View at Scopus
  7. S. J. Spence and M. T. Schneider, “The role of epilepsy and epileptiform EEGs in autism spectrum disorders,” Pediatric Research, vol. 65, no. 6, pp. 599–606, 2009. View at Publisher · View at Google Scholar · View at Scopus
  8. Autism and Developmental Disabilities Monitoring Network Surveillance Year 2008 Principal Investigators and Centers for Disease Control and Prevention, “Prevalence of autism spectrum disorders—autism and developmental disabilities monitoring network, 14 sites, United States, 2008,” Morbidity and Mortality Weekly Report: Surveillance Summaries, vol. 61, no. 3, pp. 1–19, 2012. View at Google Scholar · View at Scopus
  9. S. J. Blumberg, M. D. Bramlett, M. D. Kogan, L. A. Schieve, J. R. Jones, and M. C. Lu, “Changes in prevalence of parent-reported autism spectrum disorder in school-aged U.S. children: 2007 to 2011-2012,” National Health Statistics Reports, no. 65, pp. 1–7, 2013. View at Google Scholar
  10. B. Taylor, “Vaccines and the changing epidemiology of autism,” Child, vol. 32, no. 5, pp. 511–519, 2006. View at Publisher · View at Google Scholar · View at Scopus
  11. P. T. Shattuck, “The contribution of diagnostic substitution to the growing administrative prevalence of autism in US special education,” Pediatrics, vol. 117, no. 4, pp. 1028–1037, 2006. View at Publisher · View at Google Scholar · View at Scopus
  12. H. Jick and J. A. Kaye, “Epidemiology and possible causes of autism,” Pharmacotherapy, vol. 23, no. 12, pp. 1524–1530, 2003. View at Publisher · View at Google Scholar · View at Scopus
  13. M. E. McDonald and J. F. Paul, “Timing of increased autistic disorder cumulative incidence,” Environmental Science and Technology, vol. 44, no. 6, pp. 2112–2118, 2010. View at Publisher · View at Google Scholar · View at Scopus
  14. S. J. James, P. Cutler, S. Melnyk et al., “Metabolic biomarkers of increased oxidative stress and impaired methylation capacity in children with autism,” The American Journal of Clinical Nutrition, vol. 80, no. 6, pp. 1611–1617, 2004. View at Google Scholar · View at Scopus
  15. S. J. James, S. Melnyk, S. Jernigan et al., “Metabolic endophenotype and related genotypes are associated with oxidative stress in children with autism,” The American Journal of Medical Genetics B, vol. 141, no. 8, pp. 947–956, 2006. View at Publisher · View at Google Scholar · View at Scopus
  16. D. A. Geier and M. R. Geier, “A clinical and laboratory evaluation of methionine cycle-transsulfuration and androgen pathway markers in children with autistic disorders,” Hormone Research, vol. 66, no. 4, pp. 182–188, 2006. View at Publisher · View at Google Scholar · View at Scopus
  17. J. B. Adams, M. Baral, E. Geis et al., “The severity of autism is associated with toxic metal body burden and red blood cell glutathione levels,” Journal of Toxicology, vol. 2009, Article ID 532640, 7 pages, 2009. View at Publisher · View at Google Scholar
  18. S. P. Paşca, E. Dronca, T. Kaucsár et al., “One carbon metabolism disturbances and the C677T MTHFR gene polymorphism in children with autism spectrum disorders,” Journal of Cellular and Molecular Medicine, vol. 13, no. 10, pp. 4229–4238, 2009. View at Publisher · View at Google Scholar · View at Scopus
  19. É. Pastural, S. Ritchie, Y. Lu et al., “Novel plasma phospholipid biomarkers of autism: mitochondrial dysfunction as a putative causative mechanism,” Prostaglandins Leukotrienes and Essential Fatty Acids, vol. 81, no. 4, pp. 253–264, 2009. View at Publisher · View at Google Scholar · View at Scopus
  20. Y. Al-Gadani, A. El-Ansary, O. Attas, and L. Al-Ayadhi, “Metabolic biomarkers related to oxidative stress and antioxidant status in Saudi autistic children,” Clinical Biochemistry, vol. 42, no. 10-11, pp. 1032–1040, 2009. View at Publisher · View at Google Scholar · View at Scopus
  21. S. Melnyk, G. J. Fuchs, E. Schulz et al., “Metabolic imbalance associated with methylation dysregulation and oxidative damage in children with autism,” Journal of Autism and Developmental Disorders, vol. 42, no. 3, pp. 367–377, 2012. View at Publisher · View at Google Scholar · View at Scopus
  22. S. J. James, S. Melnyk, G. Fuchs et al., “Efficacy of methylcobalamin and folinic acid treatment on glutathione redox status in children with autism,” The American Journal of Clinical Nutrition, vol. 89, no. 1, pp. 425–430, 2009. View at Publisher · View at Google Scholar · View at Scopus
  23. D. A. Geier, J. K. Kern, C. R. Garver et al., “Biomarkers of environmental toxicity and susceptibility in autism,” Journal of the Neurological Sciences, vol. 280, no. 1, pp. 101–108, 2009. View at Publisher · View at Google Scholar · View at Scopus
  24. D. A. Geier, J. K. Kern, C. R. Garver, J. B. Adams, T. Audhya, and M. R. Geier, “A prospective study of transsulfuration biomarkers in autistic disorders,” Neurochemical Research, vol. 34, no. 2, pp. 386–393, 2009. View at Publisher · View at Google Scholar · View at Scopus
  25. J. Chen and M. J. Berry, “Selenium and selenoproteins in the brain and brain diseases,” Journal of Neurochemistry, vol. 86, no. 1, pp. 1–12, 2003. View at Publisher · View at Google Scholar · View at Scopus
  26. U. Schweizer, A. U. Bräuer, J. Köhrle, R. Nitsch, and N. E. Savaskan, “Selenium and brain function: a poorly recognized liaison,” Brain Research Reviews, vol. 45, no. 3, pp. 164–178, 2004. View at Publisher · View at Google Scholar · View at Scopus
  27. M. L. Circu and T. Y. Aw, “Reactive oxygen species, cellular redox systems, and apoptosis,” Free Radical Biology and Medicine, vol. 48, no. 6, pp. 749–762, 2010. View at Publisher · View at Google Scholar · View at Scopus
  28. A. Chauhan, V. Chauhan, W. T. Brown, and I. Cohen, “Oxidative stress in autism: increased lipid peroxidation and reduced serum levels of ceruloplasmin and transferrin—the antioxidant proteins,” Life Sciences, vol. 75, no. 21, pp. 2539–2549, 2004. View at Publisher · View at Google Scholar · View at Scopus
  29. S. S. Zoroglu, F. Armutcu, S. Ozen et al., “Increased oxidative stress and altered activities of erythrocyte free radical scavenging enzymes in autism,” European Archives of Psychiatry and Clinical Neuroscience, vol. 254, no. 3, pp. 143–147, 2004. View at Publisher · View at Google Scholar · View at Scopus
  30. X. Ming, T. P. Stein, M. Brimacombe, W. G. Johnson, G. H. Lambert, and G. C. Wagner, “Increased excretion of a lipid peroxidation biomarker in autism,” Prostaglandins Leukotrienes and Essential Fatty Acids, vol. 73, no. 5, pp. 379–384, 2005. View at Publisher · View at Google Scholar · View at Scopus
  31. R. Sacco, P. Curatolo, B. Manzi et al., “Principal pathogenetic components and biological endophenotypes in autism spectrum disorders,” Autism Research, vol. 3, no. 5, pp. 237–252, 2010. View at Publisher · View at Google Scholar · View at Scopus
  32. J. B. Adams, T. Audhya, S. McDonough-Means et al., “Nutritional and metabolic status of children with autism vs. neurotypical children, and the association with autism severity,” Nutrition and Metabolism, vol. 8, article 34, 2011. View at Publisher · View at Google Scholar · View at Scopus
  33. D. A. Geier and M. R. Geier, “A case series of children with apparent mercury toxic encephalopathies manifesting with clinical symptoms of regressive autistic disorders,” Journal of Toxicology and Environmental Health A, vol. 70, no. 10, pp. 837–851, 2007. View at Publisher · View at Google Scholar · View at Scopus
  34. A. Frustaci, M. Neri, A. Cesario et al., “Oxidative stress-related biomarkers in autism: systematic review and meta-analyses,” Free Radical Biology and Medicine, vol. 52, no. 10, pp. 2128–2141, 2012. View at Publisher · View at Google Scholar
  35. A. Chauhan, T. Audhya, and V. Chauhan, “Brain region-specific glutathione redox imbalance in autism,” Neurochemical Research, vol. 37, no. 8, pp. 1681–1689, 2012. View at Publisher · View at Google Scholar · View at Scopus
  36. S. Rose, S. Melnyk, O. Pavliv et al., “Evidence of oxidative damage and inflammation associated with low glutathione redox status in the autism brain,” Translational Psychiatry, vol. 2, article e134, 2012. View at Publisher · View at Google Scholar
  37. F. Gu, V. Chauhan, and A. Chauhan, “Impaired synthesis and antioxidant defense of glutathione in the cerebellum of autistic subjects: alterations in the activities and protein expression of glutathione-related enzymes,” Free Radical Biology and Medicine, vol. 65, pp. 488–496, 2013. View at Publisher · View at Google Scholar
  38. R. Deth, C. Muratore, J. Benzecry, V.-A. Power-Charnitsky, and M. Waly, “How environmental and genetic factors combine to cause autism: a redox/methylation hypothesis,” NeuroToxicology, vol. 29, no. 1, pp. 190–201, 2008. View at Publisher · View at Google Scholar · View at Scopus
  39. E. Mosharov, M. R. Cranford, and R. Banerjee, “The quantitatively important relationship between homocysteine metabolism and glutathione synthesis by the transsulfuration pathway and its regulation by redox changes,” Biochemistry, vol. 39, no. 42, pp. 13005–13011, 2000. View at Publisher · View at Google Scholar · View at Scopus
  40. V. Bandarian, M. L. Ludwig, and R. G. Matthews, “Factors modulating conformational equilibria in large modular proteins: a case study with cobalamin-dependent methionine synthase,” Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 14, pp. 8156–8163, 2003. View at Publisher · View at Google Scholar · View at Scopus
  41. M. Waly, H. Olteanu, R. Banerjee et al., “Activation of methionine synthase by insulin-like growth factor-1 and dopamine: a target for neurodevelopmental toxins and thimerosal,” Molecular Psychiatry, vol. 9, no. 4, pp. 358–370, 2004. View at Publisher · View at Google Scholar · View at Scopus
  42. C. R. Muratore, N. W. Hodgson, M. S. Trivedi et al., “Age-dependent decrease and alternative splicing of methionine synthase mRNA in human cerebral cortex and an accelerated decrease in autism,” PLoS ONE, vol. 8, no. 2, Article ID e56927, 2013. View at Publisher · View at Google Scholar
  43. A. Kyriakopoulos and D. Behne, “Selenium-containing proteins in mammals and other forms of life,” Reviews of Physiology Biochemistry and Pharmacology, vol. 145, pp. 1–46, 2002. View at Publisher · View at Google Scholar · View at Scopus
  44. V. N. Gladyshev, F. J. Martin-Romero, X.-M. Xu et al., “Molecular biology of selenium and its role in cancer, AIDS and other human diseases,” Recent Research Developments in Biochemistry, vol. 1, pp. 145–167, 1999. View at Google Scholar
  45. S. C. Low and M. J. Berry, “Knowing when not to stop: selenocysteine incorporation in eukaryotes,” Trends in Biochemical Sciences, vol. 21, no. 6, pp. 203–208, 1996. View at Publisher · View at Google Scholar · View at Scopus
  46. S. Gromer, J. K. Eubel, B. L. Lee, and J. Jacob, “Human selenoproteins at a glance,” Cellular and Molecular Life Sciences, vol. 62, no. 21, pp. 2414–2437, 2005. View at Publisher · View at Google Scholar · View at Scopus
  47. J. Jory and W. R. McGinnis, “Red-cell trace minerals in children with autism,” The American Journal of Biochemistry and Biotechnology, vol. 4, no. 2, pp. 101–104, 2008. View at Publisher · View at Google Scholar · View at Scopus
  48. A. Lubkowska and W. Sobieraj, “Concentrations of magnesium, calcium, iron, selenium, zinc and copper in the hair of autistic children,” Trace Elements and Electrolytes, vol. 26, no. 2, pp. 72–77, 2009. View at Publisher · View at Google Scholar · View at Scopus
  49. M. D. L. Priya and A. Geetha, “Level of trace elements (copper, zinc, magnesium and selenium) and toxic elements (lead and mercury) in the hair and nail of children with autism,” Biological Trace Element Research, vol. 142, no. 2, pp. 148–158, 2011. View at Publisher · View at Google Scholar · View at Scopus
  50. G. de Palma, S. Catalani, A. Franco, M. Brighenti, and P. Apostoli, “Lack of correlation between metallic elements analyzed in hair by ICP-MS and autism,” Journal of Autism and Developmental Disorders, vol. 42, no. 3, pp. 342–353, 2012. View at Publisher · View at Google Scholar · View at Scopus
  51. J. Bernal, “Thyroid hormone receptors in brain development and function,” Nature Reviews Endocrinology, vol. 3, no. 3, pp. 249–259, 2007. View at Publisher · View at Google Scholar
  52. I. B. Amara, H. Fetoui, F. Guermazi, and N. Zeghal, “Dietary selenium addition improves cerebrum and cerebellum impairments induced by methimazole in suckling rats,” International Journal of Developmental Neuroscience, vol. 27, no. 7, pp. 719–726, 2009. View at Publisher · View at Google Scholar · View at Scopus
  53. J. Kohrle and R. Gartner, “Selenium and thyroid,” Best Practice & Research Clinical Endocrinology & Metabolism, vol. 23, no. 6, pp. 815–827, 2009. View at Publisher · View at Google Scholar
  54. J. Mittag, T. Behrends, C. S. Hoefig, B. Vennström, and L. Schomburg, “Thyroid hormones regulate selenoprotein expression and selenium status in mice,” PLoS ONE, vol. 5, no. 9, Article ID e12931, 2010. View at Publisher · View at Google Scholar · View at Scopus
  55. F. R. Crantz, J. E. Silva, and P. R. Larsen, “An analysis of the sources and quantity of 3,5,3′-triiodothyronine specifically bound to nuclear receptors in rat cerebral cortex and cerebellum,” Endocrinology, vol. 110, no. 2, pp. 367–375, 1982. View at Publisher · View at Google Scholar · View at Scopus
  56. F. Courtin, F. Chantoux, and J. Francon, “Thyroid hormone metabolism by glial cells in primary culture,” Molecular and Cellular Endocrinology, vol. 48, no. 2-3, pp. 167–178, 1986. View at Publisher · View at Google Scholar · View at Scopus
  57. M. Safran, A. P. Farwell, and J. L. Leonard, “Evidence that type II 5′-deiodinase is not a selenoprotein,” The Journal of Biological Chemistry, vol. 266, no. 21, pp. 13477–13480, 1991. View at Google Scholar · View at Scopus
  58. X. G. Lei, W.-H. Cheng, and J. P. McClung, “Metabolic regulation and function of glutathione peroxidase-1,” Annual Review of Nutrition, vol. 27, pp. 41–61, 2007. View at Publisher · View at Google Scholar · View at Scopus
  59. K. Wingler, M. Böcher, L. Flohé, H. Kollmus, and R. Brigelius-Flohé, “mRNA stability and selenocysteine insertion sequence efficiency rank gastrointestinal glutathione peroxidase high in the hierarchy of selenoproteins,” European Journal of Biochemistry, vol. 259, no. 1-2, pp. 149–157, 1999. View at Publisher · View at Google Scholar · View at Scopus
  60. Y. S. Lee, A. Y. Kim, J. W. Choi et al., “Dysregulation of adipose glutathione peroxidase 3 in obesity contributes to local and systemic oxidative stress,” Molecular Endocrinology, vol. 22, no. 9, pp. 2176–2189, 2008. View at Publisher · View at Google Scholar · View at Scopus
  61. M. Conrad, M. Schneider, A. Seiler, and G. W. Bornkamm, “Physiological role of phospholipid hydroperoxide glutathione peroxidase in mammals,” Biological Chemistry, vol. 388, no. 10, pp. 1019–1025, 2007. View at Publisher · View at Google Scholar · View at Scopus
  62. C. L. Linster and E. van Schaftingen, “Vitamin C: biosynthesis, recycling and degradation in mammals,” The FEBS Journal, vol. 274, no. 1, pp. 1–22, 2007. View at Publisher · View at Google Scholar · View at Scopus
  63. E. S. J. Arnér, “Focus on mammalian thioredoxin reductases—important selenoproteins with versatile functions,” Biochimica et Biophysica Acta, vol. 1790, no. 6, pp. 495–526, 2009. View at Publisher · View at Google Scholar · View at Scopus
  64. M. A. Reeves and P. R. Hoffmann, “The human selenoproteome: recent insights into functions and regulation,” Cellular and Molecular Life Sciences, vol. 66, no. 15, pp. 2457–2478, 2009. View at Publisher · View at Google Scholar · View at Scopus
  65. A. C. Bianco, D. Salvatore, B. Gereben, M. J. Berry, and P. R. Larsen, “Biochemistry, cellular and molecular biology, and physiological roles of the iodothyronine selenodeiodinases,” Endocrine Reviews, vol. 23, no. 1, pp. 38–89, 2002. View at Publisher · View at Google Scholar · View at Scopus
  66. M. A. Reeves, F. P. Bellinger, and M. J. Berry, “The neuroprotective functions of selenoprotein M and its role in cytosolic calcium regulation,” Antioxidants and Redox Signaling, vol. 12, no. 7, pp. 809–818, 2010. View at Publisher · View at Google Scholar · View at Scopus
  67. A. Dikiy, S. V. Novoselov, D. E. Fomenko et al., “SelT, SelW, SelH, and Rdx 12: genomics and molecular insights into the functions of selenoproteins of a novel thioredoxin-like family,” Biochemistry, vol. 46, no. 23, pp. 6871–6882, 2007. View at Publisher · View at Google Scholar · View at Scopus
  68. J. Nordberg and E. S. J. Arnér, “Reactive oxygen species, antioxidants, and the mammalian thioredoxin system,” Free Radical Biology and Medicine, vol. 31, no. 11, pp. 1287–1312, 2001. View at Publisher · View at Google Scholar · View at Scopus
  69. C. Jakupoglu, G. K. H. Przemeck, M. Schneider et al., “Cytoplasmic thioredoxin reductase is essential for embryogenesis but dispensable for cardiac development,” Molecular and Cellular Biology, vol. 25, no. 5, pp. 1980–1988, 2005. View at Publisher · View at Google Scholar · View at Scopus
  70. M. Matsui, M. Oshima, H. Oshima et al., “Early embryonic lethality caused by targeted disruption of the mouse thioredoxin gene,” Developmental Biology, vol. 178, no. 1, pp. 179–185, 1996. View at Publisher · View at Google Scholar · View at Scopus
  71. K. Anestål and E. S. J. Arnér, “Rapid induction of cell death by selenium-compromised thioredoxin reductase 1 but not by the fully active enzyme containing selenocysteine,” The Journal of Biological Chemistry, vol. 278, no. 18, pp. 15966–15972, 2003. View at Publisher · View at Google Scholar · View at Scopus
  72. B. Corvilain, J. van Sande, E. Laurent, and J. E. Dumont, “The H2O2-generating system modulates protein iodination and the activity of the pentose phosphate pathway in dog thyroid,” Endocrinology, vol. 128, no. 2, pp. 779–785, 1991. View at Publisher · View at Google Scholar · View at Scopus
  73. B. Corvilain, E. Laurent, M. Lecomte, J. van sande, and J. E. Dumont, “Role of the cyclic adenosine 3′,5′-monophosphate and the phosphatidylinositol-Ca2+ cascades in mediating the effects of thyrotropin and iodide on hormone synthesis and secretion in human thyroid slices,” The Journal of Clinical Endocrinology and Metabolism, vol. 79, no. 1, pp. 152–159, 1994. View at Publisher · View at Google Scholar · View at Scopus
  74. U. Björkman and R. Ekholm, “Generation of H2O2 in isolated porcine thyroid follicles,” Endocrinology, vol. 115, no. 1, pp. 392–398, 1984. View at Publisher · View at Google Scholar · View at Scopus
  75. S. Villette, G. Bermano, J. R. Arthur, and J. E. Hesketh, “Thyroid stimulating hormone and selenium supply interact to regulate selenoenzyme gene expression in thyroid cells (FRTL-5) in culture,” FEBS Letters, vol. 438, no. 1-2, pp. 81–84, 1998. View at Publisher · View at Google Scholar · View at Scopus
  76. P. Zagrodzki, F. Nicol, M. A. McCoy et al., “Iodine deficiency in cattle: compensatory changes in thyroidal selenoenzymes,” Research in Veterinary Science, vol. 64, no. 3, pp. 209–211, 1998. View at Publisher · View at Google Scholar · View at Scopus
  77. A. F. Howie, S. W. Walker, B. Akesson, J. R. Arthur, and G. J. Beckett, “Thyroidal extracellular glutathione peroxidase: a potential regulator of thyroid-hormone synthesis,” Biochemical Journal, vol. 308, no. 3, pp. 713–717, 1995. View at Google Scholar · View at Scopus
  78. A. F. Howie, J. R. Arthur, F. Nicol, S. W. Walker, S. G. Beech, and G. J. Beckett, “Identification of a 57-kilodalton selenoprotein in human thyrocytes as thioredoxin reductase and evidence that its expression is regulated through the calcium-phosphoinositol signaling pathway,” The Journal of Clinical Endocrinology and Metabolism, vol. 83, no. 6, pp. 2052–2058, 1998. View at Publisher · View at Google Scholar · View at Scopus
  79. M. Oertel, R. O. Hesch, and J. Kohrle, “Expression of iodothyronine deiodinase in cultured thyroid cells,” Experimental and Clinical Endocrinology, vol. 97, no. 2-3, pp. 182–186, 1991. View at Publisher · View at Google Scholar · View at Scopus
  80. R. Schreck, F. Schnieders, C. Schmutzler, and J. Kohrle, “Retinoids stimulate type I iodothyronine 5′-deiodinase activity in human follicular thyroid carcinoma cell lines,” The Journal of Clinical Endocrinology and Metabolism, vol. 79, no. 3, pp. 791–798, 1994. View at Publisher · View at Google Scholar · View at Scopus
  81. S. G. Beech, S. W. Walker, A. M. Dorrance et al., “The role of thyroidal type-I iodothyronine deiodinase in tri-iodothyronine production by human and sheep thyrocytes in primary culture,” The Journal of Endocrinology, vol. 136, no. 3, pp. 361–370, 1993. View at Publisher · View at Google Scholar · View at Scopus
  82. S. G. Beech, S. W. Walker, G. J. Beckett, J. R. Arthur, F. Nicol, and D. Lee, “Effect of selenium depletion on thyroidal type-I iodothyronine deiodinase activity in isolated human thyrocytes and rat thyroid and liver,” Analyst, vol. 120, no. 3, pp. 827–831, 1995. View at Publisher · View at Google Scholar · View at Scopus
  83. G. Bermano, F. Nicol, J. A. Dyer et al., “Tissue-specific regulation of selenoenzyme gene expression during selenium deficiency in rats,” Biochemical Journal, vol. 311, no. 2, pp. 425–430, 1995. View at Google Scholar · View at Scopus
  84. A. Demelash, J.-O. Karlsson, M. Nilsson, and U. Björkman, “Selenium has a protective role in caspase-3-dependent apoptosis induced by H2O2 in primary cultured pig thyrocytes,” European Journal of Endocrinology, vol. 150, no. 6, pp. 841–849, 2004. View at Publisher · View at Google Scholar · View at Scopus
  85. E. K. Wirth, M. Conrad, J. Winterer et al., “Neuronal selenoprotein expression is required for interneuron development and prevents seizures and neurodegeneration,” The FASEB Journal, vol. 24, no. 3, pp. 844–852, 2010. View at Publisher · View at Google Scholar · View at Scopus
  86. M. Bartos, I. Vida, and P. Jonas, “Synaptic mechanisms of synchronized gamma oscillations in inhibitory interneuron networks,” Nature Reviews Neuroscience, vol. 8, no. 1, pp. 45–56, 2007. View at Publisher · View at Google Scholar · View at Scopus
  87. J. de Almeida and G. Mengod, “D2 and D4 dopamine receptor mRNA distribution in pyramidal neurons and GABAergic subpopulations in monkey prefrontal cortex: implications for schizophrenia treatment,” Neuroscience, vol. 170, no. 4, pp. 1133–1139, 2010. View at Publisher · View at Google Scholar · View at Scopus
  88. J. M. Swanson, M. Kinsbourne, J. Nigg et al., “Etiologic subtypes of attention-deficit/hyperactivity disorder: brain imaging, molecular genetic and environmental factors and the dopamine hypothesis,” Neuropsychology Review, vol. 17, no. 1, pp. 39–59, 2007. View at Publisher · View at Google Scholar · View at Scopus
  89. J.-H. Cabungcal, D. Nicolas, R. Kraftsik, M. Cuénod, K. Q. Do, and J.-P. Hornung, “Glutathione deficit during development induces anomalies in the rat anterior cingulate GABAergic neurons: relevance to schizophrenia,” Neurobiology of Disease, vol. 22, no. 3, pp. 624–637, 2006. View at Publisher · View at Google Scholar · View at Scopus
  90. P. Steullet, J.-H. Cabungcal, A. Kulak et al., “Redox dysregulation affects the ventral but not dorsal hippocampus: impairment of parvalbumin neurons, gamma oscillations, and related behaviors,” The Journal of Neuroscience, vol. 30, no. 7, pp. 2547–2558, 2010. View at Publisher · View at Google Scholar · View at Scopus
  91. V. A. Shchedrina, Y. Zhang, V. M. Labunskyy, D. L. Hatfield, and V. N. Gladyshev, “Structure—function relations, physiological roles, and evolution of mammalian ER-resident selenoproteins,” Antioxidants and Redox Signaling, vol. 12, no. 7, pp. 839–849, 2010. View at Publisher · View at Google Scholar · View at Scopus
  92. L. Schomburg, U. Schweizer, B. Holtmann, L. Flohé, M. Sendtner, and J. Köhrle, “Gene disruption discloses role of selenoprotein P in selenium delivery to target tissues,” Biochemical Journal, vol. 370, no. 2, pp. 397–402, 2003. View at Publisher · View at Google Scholar · View at Scopus
  93. K. E. Hill, J. Zhou, W. J. McMahan et al., “Deletion of selenoprotein P alters distribution of selenium in the mouse,” The Journal of Biological Chemistry, vol. 278, no. 16, pp. 13640–13646, 2003. View at Publisher · View at Google Scholar · View at Scopus
  94. Y. Zhang, Y. Zhou, U. Schweizer et al., “Comparative analysis of selenocysteine machinery and selenoproteome gene expression in mouse brain identifies neurons as key functional sites of selenium in mammals,” The Journal of Biological Chemistry, vol. 283, no. 4, pp. 2427–2438, 2008. View at Publisher · View at Google Scholar · View at Scopus
  95. K. E. Hill, J. Zhou, W. J. McMahan, A. K. Motley, and R. F. Burk, “Neurological dysfunction occurs in mice with targeted deletion of the selenoprotein P gene,” The Journal of Nutrition, vol. 134, no. 1, pp. 157–161, 2004. View at Google Scholar · View at Scopus
  96. R. A. Sunde, A. M. Raines, K. M. Barnes, and J. K. Evenson, “Selenium status highly regulates selenoprotein mRNA levels for only a subset of the selenoproteins in the selenoproteome,” Bioscience Reports, vol. 29, no. 5, pp. 329–338, 2009. View at Publisher · View at Google Scholar · View at Scopus
  97. M. Scharpf, U. Schweizer, T. Arzberger, W. Roggendorf, L. Schomburg, and J. Köhrle, “Neuronal and ependymal expression of selenoprotein P in the human brain,” Journal of Neural Transmission, vol. 114, no. 7, pp. 877–884, 2007. View at Publisher · View at Google Scholar · View at Scopus
  98. I. Kazanis and C. Ffrench-Constant, “The number of stem cells in the subependymal zone of the adult rodent brain is correlated with the number of ependymal cells and not with the volume of the niche,” Stem Cells and Development, vol. 21, no. 7, pp. 1090–1096, 2012. View at Publisher · View at Google Scholar · View at Scopus
  99. M. Pérez-Martín, M. Cifuentes, J. M. Grondona et al., “IGF-I stimulates neurogenesis in the hypothalamus of adult rats,” European Journal of Neuroscience, vol. 31, no. 9, pp. 1533–1548, 2010. View at Publisher · View at Google Scholar
  100. G. E. Olson, V. P. Winfrey, S. K. NagDas, K. E. Hill, and R. F. Burk, “Apolipoprotein E receptor-2 (ApoER2) mediates selenium uptake from selenoprotein P by the mouse testis,” The Journal of Biological Chemistry, vol. 282, no. 16, pp. 12290–12297, 2007. View at Publisher · View at Google Scholar · View at Scopus
  101. R. F. Burk, K. E. Hill, G. E. Olson et al., “Deletion of apolipoprotein E receptor-2 in mice lowers brain selenium and causes severe neurological dysfunction and death when a low-selenium diet is fed,” The Journal of Neuroscience, vol. 27, no. 23, pp. 6207–6211, 2007. View at Publisher · View at Google Scholar · View at Scopus
  102. N. Hodgson, M. Trivedi, C. Muratore, S. Li, and R. Deth, “Soluble oligomers of amyloid-β cause changes in redox state, DNA methylation, and gene transcription by inhibiting EAAT3 mediated cysteine uptake,” Journal of Alzheimer's Disease, vol. 36, pp. 197–209, 2013. View at Publisher · View at Google Scholar
  103. A. Bailey, A. Le Couteur, I. Gottesman et al., “Autism as a strongly genetic disorder: evidence from a British twin study,” Psychological Medicine, vol. 25, no. 1, pp. 63–77, 1995. View at Publisher · View at Google Scholar · View at Scopus
  104. R. S. E. Hurley, M. Losh, M. Parlier, J. S. Reznick, and J. Piven, “The broad autism phenotype questionnaire,” Journal of Autism and Developmental Disorders, vol. 37, no. 9, pp. 1679–1690, 2007. View at Publisher · View at Google Scholar · View at Scopus
  105. J. N. Constantino and R. D. Todd, “Intergenerational transmission of subthreshold autistic traits in the general population,” Biological Psychiatry, vol. 57, no. 6, pp. 655–660, 2005. View at Publisher · View at Google Scholar · View at Scopus
  106. S. Jamain, H. Quach, C. Betancur et al., “Mutations of the X-linked genes encoding neuroligins NLGN3 and NLGN4 are associated with autism,” Nature Genetics, vol. 34, no. 1, pp. 27–29, 2003. View at Publisher · View at Google Scholar · View at Scopus
  107. C. M. Durand, C. Betancur, T. M. Boeckers et al., “Mutations in the gene encoding the synaptic scaffolding protein SHANK3 are associated with autism spectrum disorders,” Nature Genetics, vol. 39, no. 1, pp. 25–27, 2007. View at Publisher · View at Google Scholar · View at Scopus
  108. J. Sebat, B. Lakshmi, D. Malhotra et al., “Strong association of de novo copy number mutations with autism,” Science, vol. 316, no. 5823, pp. 445–449, 2007. View at Publisher · View at Google Scholar · View at Scopus
  109. C. R. Marshall, A. Noor, J. B. Vincent et al., “Structural variation of chromosomes in autism spectrum disorder,” The American Journal of Human Genetics, vol. 82, no. 2, pp. 477–488, 2008. View at Publisher · View at Google Scholar · View at Scopus
  110. L. A. Weiss, D. E. Arking, Gene Discovery Project of Johns Hopkins & the Autism Consortium, M. J. Daly, and A. Chakravarti, “A genome-wide linkage and association scan reveals novel loci for autism,” Nature, vol. 461, no. 7265, pp. 802–808, 2009. View at Publisher · View at Google Scholar
  111. L. A. Weiss, Y. Shen, J. M. Korn et al., “Association between microdeletion and microduplication at 16p11.2 and autism,” The New England Journal of Medicine, vol. 358, no. 7, pp. 667–675, 2008. View at Publisher · View at Google Scholar · View at Scopus
  112. R. A. Kumar, S. Karamohamed, J. Sudi et al., “Recurrent 16p11.2 microdeletions in autism,” Human Molecular Genetics, vol. 17, no. 4, pp. 628–638, 2008. View at Publisher · View at Google Scholar · View at Scopus
  113. K. Wang, H. Zhang, D. Ma et al., “Common genetic variants on 5p14.1 associate with autism spectrum disorders,” Nature, vol. 459, no. 7246, pp. 528–533, 2009. View at Publisher · View at Google Scholar · View at Scopus
  114. B. A. Fernandez, W. Roberts, B. Chung et al., “Phenotypic spectrum associated with de novo and inherited deletions and duplications at 16p11.2 in individuals ascertained for diagnosis of autism spectrum disorder,” Journal of Medical Genetics, vol. 47, no. 3, pp. 195–203, 2010. View at Publisher · View at Google Scholar · View at Scopus
  115. J. T. Glessner, K. Wang, G. Cai et al., “Autism genome-wide copy number variation reveals ubiquitin and neuronal genes,” Nature, vol. 459, no. 7246, pp. 569–572, 2009. View at Publisher · View at Google Scholar · View at Scopus
  116. D. Pinto, A. T. Pagnamenta, L. Klei, R. Anney, D. Merico, R. Regan et al., “Functional impact of global rare copy number variation in autism,” Nature, vol. 466, no. 7304, pp. 368–372, 2010. View at Publisher · View at Google Scholar
  117. B. Devlin, N. Melhem, and K. Roeder, “Do common variants play a role in risk for autism? Evidence and theoretical musings,” Brain Research, vol. 1380, pp. 78–84, 2011. View at Publisher · View at Google Scholar · View at Scopus
  118. J. Hallmayer, S. Cleveland, A. Torres et al., “Genetic heritability and shared environmental factors among twin pairs with autism,” Archives of General Psychiatry, vol. 68, no. 11, pp. 1095–1102, 2011. View at Publisher · View at Google Scholar · View at Scopus
  119. F. J. Serajee, R. Nabi, H. Zhong, and A. H. M. M. Huq, “Polymorphisms in xenobiotic metabolism genes and autism,” Journal of Child Neurology, vol. 19, no. 6, pp. 413–417, 2004. View at Google Scholar · View at Scopus
  120. S. P. Paşca, B. Nemeş, L. Vlase et al., “High levels of homocysteine and low serum paraoxonase 1 arylesterase activity in children with autism,” Life Sciences, vol. 78, no. 19, pp. 2244–2248, 2006. View at Publisher · View at Google Scholar · View at Scopus
  121. X. Ming, W. G. Johnson, E. S. Stenroos, A. Mars, G. H. Lambert, and S. Buyske, “Genetic variant of glutathione peroxidase 1 in autism,” Brain and Development, vol. 32, no. 2, pp. 105–109, 2010. View at Publisher · View at Google Scholar · View at Scopus
  122. T. A. Williams, A. E. Mars, S. G. Buyske et al., “Risk of autistic disorder in affected offspring of mothers with a glutathione S-transferase P1 haplotype,” Archives of Pediatrics and Adolescent Medicine, vol. 161, no. 4, pp. 356–361, 2007. View at Publisher · View at Google Scholar · View at Scopus
  123. A. K. Merikangas, A. P. Corvin, and L. Gallagher, “Copy-number variants in neurodevelopmental disorders: promises and challenges,” Trends in Genetics, vol. 25, no. 12, pp. 536–544, 2009. View at Publisher · View at Google Scholar · View at Scopus
  124. C. Guerrero-Bosagna, M. Settles, B. Lucker, and M. K. Skinner, “Epigenetic transgenerational actions of vinclozolin on promoter regions of the sperm epigenome,” PLoS ONE, vol. 5, no. 9, Article ID e13100, 2010. View at Publisher · View at Google Scholar · View at Scopus
  125. J. Andrews, W. Kennette, J. Pilon et al., “Multi-platform whole-genome microarray analyses refine the epigenetic signature of breast cancer metastasis with gene expression and copy number,” PLoS ONE, vol. 5, no. 1, Article ID e8665, 2010. View at Publisher · View at Google Scholar · View at Scopus
  126. J. R. McCarrey, “The epigenome as a target for heritable environmental disruptions of cellular function,” Molecular and Cellular Endocrinology, vol. 354, no. 1-2, pp. 9–15, 2012. View at Publisher · View at Google Scholar · View at Scopus
  127. C. Murgatroyd and D. Spengler, “Epigenetics of early child development,” Frontiers in Psychiatry, vol. 2, article 16, 2011. View at Publisher · View at Google Scholar
  128. M. K. Skinner, M. Manikkam, and C. Guerrero-Bosagna, “Epigenetic transgenerational actions of endocrine disruptors,” Reproductive Toxicology, vol. 31, no. 3, pp. 337–343, 2011. View at Publisher · View at Google Scholar · View at Scopus
  129. C. R. Beck, J. L. Garcia-Perez, R. M. Badge, and J. V. Moran, “LINE-1 elements in structural variation and disease,” Annual Review of Genomics and Human Genetics, vol. 12, pp. 187–215, 2011. View at Publisher · View at Google Scholar · View at Scopus
  130. A. R. Muotri, M. C. N. Marchetto, N. G. Coufal et al., “L1 retrotransposition in neurons is modulated by MeCP2,” Nature, vol. 468, no. 7322, pp. 443–446, 2010. View at Publisher · View at Google Scholar · View at Scopus
  131. S. M. Wernimont, A. G. Clark, P. J. Stover et al., “Folate network genetic variation, plasma homocysteine, and global genomic methylation content: a genetic association study,” BMC Medical Genetics, vol. 12, article 150, 2011. View at Publisher · View at Google Scholar · View at Scopus
  132. T. Singer, M. J. McConnell, M. C. N. Marchetto, N. G. Coufal, and F. H. Gage, “LINE-1 retrotransposons: mediators of somatic variation in neuronal genomes?” Trends in Neurosciences, vol. 33, no. 8, pp. 345–354, 2010. View at Publisher · View at Google Scholar · View at Scopus
  133. T. Buie, D. B. Campbell, G. J. Fuchs III et al., “Evaluation, diagnosis, and treatment of gastrointestinal disorders in individuals with ASDs: a consensus report,” Pediatrics, vol. 125, no. 1, supplement, pp. S1–S18, 2010. View at Publisher · View at Google Scholar · View at Scopus
  134. D. A. Rossignol and R. E. Frye, “A review of research trends in physiological abnormalities in autism spectrum disorders: immune dysregulation, inflammation, oxidative stress, mitochondrial dysfunction and environmental toxicant exposures,” Molecular Psychiatry, vol. 17, no. 4, pp. 389–401, 2012. View at Publisher · View at Google Scholar · View at Scopus
  135. C. C. Y. Wong, E. L. Meaburn, A. Ronald et al., “Methylomic analysis of monozygotic twins discordant for autism spectrum disorder and related behavioural traits,” Molecular Psychiatry, 2013. View at Publisher · View at Google Scholar
  136. Y.-H. Jiang, T.-F. Tsai, J. Bressler, and A. L. Beaudet, “Imprinting in Angelman and Prader-Willi syndromes,” Current Opinion in Genetics and Development, vol. 8, no. 3, pp. 334–342, 1998. View at Publisher · View at Google Scholar · View at Scopus
  137. T. Bienvenu and J. Chelly, “Molecular genetics of Rett syndrome: when DNA methylation goes unrecognized,” Nature Reviews Genetics, vol. 7, no. 6, pp. 415–426, 2006. View at Publisher · View at Google Scholar · View at Scopus
  138. N. Dolzhanskaya, G. Merz, J. M. Aletta, and R. B. Denman, “Methylation regulates the intracellular protein-protein and protein-RNA interactions of FMRP,” Journal of Cell Science, vol. 119, no. 9, pp. 1933–1946, 2006. View at Publisher · View at Google Scholar · View at Scopus
  139. P. D. Whanger, “Selenium and the brain: a review,” Nutritional Neuroscience, vol. 4, no. 2, pp. 81–97, 2001. View at Google Scholar · View at Scopus
  140. N. V. C. Ralston and L. J. Raymond, “Dietary selenium's protective effects against methylmercury toxicity,” Toxicology, vol. 278, no. 1, pp. 112–123, 2010. View at Publisher · View at Google Scholar · View at Scopus
  141. C. M. L. Carvalho, E.-H. Chew, S. I. Hashemy, J. Lu, and A. Holmgren, “Inhibition of the human thioredoxin system: a molecular mechanism of mercury toxicity,” The Journal of Biological Chemistry, vol. 283, no. 18, pp. 11913–11923, 2008. View at Publisher · View at Google Scholar · View at Scopus
  142. A. P. Neal and T. R. Guilarte, “Mechanisms of lead and manganese neurotoxicity,” Toxicology Research, no. 2, pp. 99–114, 2013. View at Publisher · View at Google Scholar
  143. J. K. Kern, B. D. Grannemann, M. H. Trivedi, and J. B. Adams, “Sulfhydryl-reactive metals in autism,” Journal of Toxicology and Environmental Health A, vol. 70, no. 8, pp. 715–721, 2007. View at Publisher · View at Google Scholar · View at Scopus
  144. M. E. Obrenovich, R. J. Shamberger, and D. Lonsdale, “Altered heavy metals and transketolase found in autistic spectrum disorder,” Biological Trace Element Research, vol. 144, no. 1–3, pp. 475–486, 2011. View at Publisher · View at Google Scholar · View at Scopus
  145. A. S. Holmes, M. F. Blaxill, and B. E. Haley, “Reduced levels of mercury in first baby haircuts of autistic children,” International Journal of Toxicology, vol. 22, no. 4, pp. 277–285, 2003. View at Publisher · View at Google Scholar · View at Scopus
  146. M. D. Majewska, E. Urbanowicz, P. Rok-Bujko, I. Namysłowska, and P. Mierzejewski, “Age-dependent lower or higher levels of hair mercury in autistic children than in healthy controls,” Acta Neurobiologiae Experimentalis, vol. 70, no. 2, pp. 196–208, 2010. View at Google Scholar · View at Scopus
  147. I. Hertz-Picciotto, P. G. Green, L. Delwiche, R. Hansen, C. Walker, and I. N. Pessah, “Blood mercury concentrations in CHARGE study children with and without autism,” Environmental Health Perspectives, vol. 118, no. 1, pp. 161–166, 2010. View at Publisher · View at Google Scholar · View at Scopus
  148. S. E. Owens, M. L. Summar, K. K. Ryckman et al., “Lack of association between autism and four heavy metal regulatory genes,” NeuroToxicology, vol. 32, no. 6, pp. 769–775, 2011. View at Publisher · View at Google Scholar · View at Scopus
  149. B. Stamova, P. G. Green, Y. Tian et al., “Correlations between gene expression and mercury levels in blood of boys with and without autism,” Neurotoxicity Research, vol. 19, no. 1, pp. 31–48, 2011. View at Publisher · View at Google Scholar · View at Scopus
  150. Y. Arai, J. Ohgane, S. Yagi et al., “Epigenetic assessment of environmental chemicals detected in maternal peripheral and cord blood samples,” The Journal of Reproduction and Development, vol. 57, no. 4, pp. 507–517, 2011. View at Publisher · View at Google Scholar · View at Scopus
  151. T. C. Stummann, L. Hareng, and S. Bremer, “Hazard assessment of methylmercury toxicity to neuronal induction in embryogenesis using human embryonic stem cells,” Toxicology, vol. 257, no. 3, pp. 117–126, 2009. View at Publisher · View at Google Scholar · View at Scopus
  152. C. Tamm, J. Duckworth, O. Hermanson, and S. Ceccatelli, “High susceptibility of neural stem cells to methylmercury toxicity: effects on cell survival and neuronal differentiation,” Journal of Neurochemistry, vol. 97, no. 1, pp. 69–78, 2006. View at Publisher · View at Google Scholar · View at Scopus
  153. S. Bernard, A. Enayati, L. Redwood, H. Roger, and T. Binstock, “Autism: a novel form of mercury poisoning,” Medical Hypotheses, vol. 56, no. 4, pp. 462–471, 2001. View at Publisher · View at Google Scholar · View at Scopus
  154. J. G. Dórea, “Making sense of epidemiological studies of young children exposed to thimerosal in vaccines,” Clinica Chimica Acta, vol. 411, no. 21-22, pp. 1580–1586, 2010. View at Publisher · View at Google Scholar · View at Scopus
  155. D. A. Geier, B. S. Hooker, J. K. Kern, P. G. King, L. K. Sykes, and M. R. Geier, “A two-phase study evaluating the relationship between Thimerosal-containing vaccine administration and the risk for an autism spectrum disorder diagnosis in the United States,” Translational Neurodegeneration, vol. 2, no. 1, article 25, 2013. View at Publisher · View at Google Scholar
  156. C. M. Gallagher and M. S. Goodman, “Hepatitis B vaccination of male neonates and autism diagnosis, NHIS 1997–2002,” Journal of Toxicology and Environmental Health A, vol. 73, no. 24, pp. 1665–1677, 2010. View at Publisher · View at Google Scholar · View at Scopus
  157. R. Schechter and J. K. Grether, “Continuing increases in autism reported to California's developmental services system: mercury in retrograde,” Archives of General Psychiatry, vol. 65, no. 1, pp. 19–24, 2008. View at Publisher · View at Google Scholar · View at Scopus
  158. S. T. Schultz, H. S. Klonoff-Cohen, D. L. Wingard, N. A. Akshoomoff, C. A. Macera, and J. Ming, “Acetaminophen (paracetamol) use, measles-mumps-rubella vaccination, and autistic disorder: the results of a parent survey,” Autism, vol. 12, no. 3, pp. 293–307, 2008. View at Publisher · View at Google Scholar · View at Scopus
  159. C. S. Price, W. W. Thompson, B. Goodson et al., “Prenatal and infant exposure to thimerosal from vaccines and immunoglobulins and risk of autism,” Pediatrics, vol. 126, no. 4, pp. 656–664, 2010. View at Publisher · View at Google Scholar · View at Scopus
  160. D. M. Walker and A. C. Gore, “Transgenerational neuroendocrine disruption of reproduction,” Nature Reviews Endocrinology, vol. 7, no. 4, pp. 197–207, 2011. View at Publisher · View at Google Scholar · View at Scopus
  161. O. Yorbik, A. Sayal, C. Akay, D. I. Akbiyik, and T. Sohmen, “Investigation of antioxidant enzymes in children with autistic disorder,” Prostaglandins Leukotrienes and Essential Fatty Acids, vol. 67, no. 5, pp. 341–343, 2002. View at Publisher · View at Google Scholar · View at Scopus
  162. N. A. Meguid, A. A. Dardir, E. R. Abdel-Raouf, and A. Hashish, “Evaluation of oxidative stress in autism: defective antioxidant enzymes and increased lipid peroxidation,” Biological Trace Element Research, vol. 143, no. 1, pp. 58–65, 2011. View at Publisher · View at Google Scholar · View at Scopus
  163. J. Castañeda, P. Genzor, and A. Bortvin, “PiRNAs, transposon silencing, and germline genome integrity,” Mutation Research, vol. 714, no. 1-2, pp. 95–104, 2011. View at Publisher · View at Google Scholar · View at Scopus
  164. O. Gokcumen, P. L. Babb, R. C. Iskow et al., “Refinement of primate copy number variation hotspots identifies candidate genomic regions evolving under positive selection,” Genome Biology, vol. 12, no. 5, article R52, 2011. View at Publisher · View at Google Scholar · View at Scopus
  165. J. Li, R. A. Harris, S. W. Cheung et al., “Genomic hypomethylation in the human germline associates with selective structural mutability in the human genome,” PLoS Genetics, vol. 8, no. 5, Article ID e1002692, 2012. View at Publisher · View at Google Scholar
  166. R. C. Iskow, M. T. McCabe, R. E. Mills et al., “Natural mutagenesis of human genomes by endogenous retrotransposons,” Cell, vol. 141, no. 7, pp. 1253–1261, 2010. View at Publisher · View at Google Scholar · View at Scopus
  167. R. M. LoPachin and D. S. Barber, “Synaptic cysteine sulfhydryl groups as targets of electrophilic neurotoxicants,” Toxicological Sciences, vol. 94, no. 2, pp. 240–255, 2006. View at Publisher · View at Google Scholar · View at Scopus
  168. L. J. Chun, M. J. Tong, R. W. Busuttil, and J. R. Hiatt, “Acetaminophen hepatotoxicity and acute liver failure,” Journal of Clinical Gastroenterology, vol. 43, no. 4, pp. 342–349, 2009. View at Publisher · View at Google Scholar · View at Scopus
  169. S. T. Schultz, “Does thimerosal or other mercury exposure increase the risk for autism? A review of current literature,” Acta Neurobiologiae Experimentalis, vol. 70, no. 2, pp. 187–195, 2010. View at Google Scholar · View at Scopus
  170. P. Good, “Did acetaminophen provoke the autism epidemic?” Alternative Medicine Review, vol. 14, no. 4, pp. 364–372, 2009. View at Google Scholar · View at Scopus
  171. N. R. Pumford, B. M. Martin, and J. A. Hinson, “A metabolite of acetaminophen covalently binds to the 56 kDa selenium binding protein,” Biochemical and Biophysical Research Communications, vol. 182, no. 3, pp. 1348–1355, 1992. View at Publisher · View at Google Scholar · View at Scopus
  172. D. J. Hoivik, J. E. Manautou, A. Tveit, D. C. Mankowski, E. A. Khairallah, and S. D. Cohen, “Evidence suggesting the 58-kDa acetaminophen binding protein is a preferential target for acetaminophen electrophile,” Fundamental and Applied Toxicology, vol. 32, no. 1, pp. 79–86, 1996. View at Publisher · View at Google Scholar · View at Scopus
  173. T. Ishida, M. Abe, K. Oguri, and H. Yamada, “Enhancement of acetaminophen cytotoxicity in selenium-binding protein-overexpressed COS-1 cells,” Drug Metabolism and Pharmacokinetics, vol. 19, no. 4, pp. 290–296, 2004. View at Publisher · View at Google Scholar · View at Scopus
  174. J. Mattow, I. Demuth, G. Haeselbarth, P. R. Jungblut, and J. Klose, “Selenium-binding protein 2, the major hepatic target for acetaminophen, shows sex differences in protein abundance,” Electrophoresis, vol. 27, no. 8, pp. 1683–1691, 2006. View at Publisher · View at Google Scholar · View at Scopus
  175. Y. Masubuchi, J. Nakayama, and Y. Watanabe, “Sex difference in susceptibility to acetaminophen hepatotoxicity is reversed by buthionine sulfoximine,” Toxicology, vol. 287, no. 1–3, pp. 54–60, 2011. View at Publisher · View at Google Scholar · View at Scopus
  176. K. J. Heard, “Acetylcysteine for acetaminophen poisoning,” The New England Journal of Medicine, vol. 359, no. 3, pp. 285–292, 2008. View at Publisher · View at Google Scholar · View at Scopus