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Oxidative Medicine and Cellular Longevity
Volume 2017 (2017), Article ID 7028583, 6 pages
https://doi.org/10.1155/2017/7028583
Review Article

Possible Mechanisms of Mercury Toxicity and Cancer Promotion: Involvement of Gap Junction Intercellular Communications and Inflammatory Cytokines

1Department of Medical and Surgical Sciences, University of Foggia, Via L. Pinto 1, 71122 Foggia, Italy
2Department of Clinical and Experimental Medicine, University of Foggia, Via L. Pinto 1, 71122 Foggia, Italy

Correspondence should be addressed to Roberto Zefferino; ti.gfinu@onireffez.otrebor

Received 28 July 2017; Accepted 29 November 2017; Published 21 December 2017

Academic Editor: Pan Chen

Copyright © 2017 Roberto Zefferino 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. T. Syversen and P. Kaur, “The toxicology of mercury and its compounds,” Journal of Trace Elements in Medicine and Biology, vol. 26, no. 4, pp. 215–226, 2012. View at Publisher · View at Google Scholar · View at Scopus
  2. E.-J. Park and K. Park, “Induction of reactive oxygen species and apoptosis in BEAS-2B cells by mercuric chloride,” Toxicology In Vitro, vol. 21, no. 5, pp. 789–794, 2007. View at Publisher · View at Google Scholar · View at Scopus
  3. D. Grotto, J. Valentini, M. Fillion et al., “Mercury exposure and oxidative stress in communities of the Brazilian Amazon,” Science of the Total Environment, vol. 408, no. 4, pp. 806–811, 2010. View at Publisher · View at Google Scholar · View at Scopus
  4. C. Piccoli, A. D'Aprile, R. Scrima, L. Ambrosi, R. Zefferino, and N. Capitanio, “Subcytotoxic mercury chloride inhibits gap junction intercellular communication by a redox- and phosphorylation-mediated mechanism,” Free Radical Biology & Medicine, vol. 52, no. 5, pp. 916–927, 2012. View at Publisher · View at Google Scholar · View at Scopus
  5. J. Albrecht and E. Matyja, “Glutamate: a potential mediator of inorganic mercury neurotoxicity,” Metabolic Brain Disease, vol. 11, no. 2, pp. 175–184, 1996. View at Publisher · View at Google Scholar · View at Scopus
  6. M. Aschner and J. L. Aschner, “Mercury neurotoxicity: mechanisms of blood-brain barrier transport,” Neuroscience and Biobehavioral Reviews, vol. 14, no. 2, pp. 169–176, 1990. View at Publisher · View at Google Scholar · View at Scopus
  7. N. Brookes and D. A. Kristt, “Inhibition of amino acid transport and protein synthesis by HgCl2 and methylmercury in astrocytes: selectivity and reversibility,” Journal of Neurochemistry, vol. 53, no. 4, pp. 1228–1237, 1989. View at Publisher · View at Google Scholar · View at Scopus
  8. M. Yoshida, C. Watanabe, M. Kishimoto et al., “Behavioral changes in metallothionein-null mice after the cessation of long-term, low-level exposure to mercury vapor,” Toxicology Letters, vol. 161, no. 3, pp. 210–218, 2006. View at Publisher · View at Google Scholar · View at Scopus
  9. H. Steinbrenner, B. Speckmann, and L. O. Klotz, “Selenoproteins: antioxidant selenoenzymes and beyond,” Archives of Biochemistry and Biophysics, vol. 595, pp. 113–119, 2016. View at Publisher · View at Google Scholar · View at Scopus
  10. V. Branco, P. Ramos, J. Canário, J. Lu, A. Holmgren, and C. Carvalho, “Biomarkers of adverse response to mercury: histopathology versus thioredoxin reductase activity,” Journal of Biomedicine and Biotechnology, vol. 2012, Article ID 359879, 9 pages, 2012. View at Publisher · View at Google Scholar · View at Scopus
  11. C. Sasakura and K. T. Suzuki, “Biological interaction between transition metals (Ag, Cd and Hg), selenide/sulfide and selenoprotein P,” Journal of Inorganic Biochemistry, vol. 71, no. 3-4, pp. 159–162, 1998. View at Publisher · View at Google Scholar · View at Scopus
  12. 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
  13. M. Farina, F. A. Soares, A. Feoli et al., “In vitro effects of selenite and mercuric chloride on liver thiobarbituric acid-reactive substances and non-protein thiols from rats: influences of dietary cholesterol and polyunsaturated and saturated fatty acids,” Nutrition, vol. 19, no. 6, pp. 531–535, 2003. View at Publisher · View at Google Scholar · View at Scopus
  14. I. Yamamoto, “Effect of various amounts of selenium on the metabolism of mercuric chloride in mice,” Biochemical Pharmacology, vol. 34, no. 15, pp. 2713–2720, 1985. View at Publisher · View at Google Scholar · View at Scopus
  15. A. B. Kobal, M. Horvat, M. Prezelj et al., “The impact of long-term past exposure to elemental mercury on antioxidative capacity and lipid peroxidation in mercury miners,” Journal of Trace Elements in Medicine and Biology, vol. 17, no. 4, pp. 261–274, 2004. View at Publisher · View at Google Scholar · View at Scopus
  16. M. S. Nielsen, L. N. Axelsen, P. L. Sorgen, V. Verma, M. Delmar, and N. H. Holstein-Rathlou, “Gap junctions,” Comprehensive Physiology, vol. 2, no. 3, pp. 1981–2035, 2012. View at Publisher · View at Google Scholar · View at Scopus
  17. S. Sisakhtnezhad and L. Khosravi, “Emerging physiological and pathological implications of tunneling nanotubes formation between cells,” European Journal of Cell Biology, vol. 94, no. 10, pp. 429–443, 2015. View at Publisher · View at Google Scholar · View at Scopus
  18. J. M. Pitt, G. Kroemer, and L. Zitvogel, “Extracellular vesicles: masters of intercellular communication and potential clinical interventions,” The Journal of Clinical Investigation, vol. 126, no. 4, pp. 1139–1143, 2016. View at Publisher · View at Google Scholar · View at Scopus
  19. R. Zefferino, A. Leone, S. Piccaluga, R. Cincione, and L. Ambrosi, “Mercury modulates interplay between IL-1β, TNF-α, and gap junctional intercellular communication in keratinocytes: mitigation by lycopene,” Journal of Immunotoxicology, vol. 5, no. 4, pp. 353–360, 2008. View at Publisher · View at Google Scholar · View at Scopus
  20. A. Pivarcsi, L. Kemény, and A. Dobozy, “Innate immune functions of the keratinocytes. A review,” Acta Microbiologica et Immunologica Hungarica, vol. 51, no. 3, pp. 303–310, 2004. View at Publisher · View at Google Scholar · View at Scopus
  21. R. Zefferino, S. Piccaluga, M. Lasalvia, G. D'Andrea, M. Margaglione, and L. Ambrosi, “Role of tumour necrosis factor alpha and interleukin 1 beta in promoter effect induced by mercury in human keratinocytes,” International Journal of Immunopathology and Pharmacology, vol. 19, Supplement 4, pp. 15–20, 2006. View at Google Scholar
  22. P. Moszczyński, “Mercury compounds and the immune system: a review,” International Journal of Occupational Medicine and Environmental Health, vol. 10, no. 3, pp. 247–258, 1997. View at Google Scholar
  23. P. Intarasunanont, P. Navasumrit, S. Waraprasit et al., “Effects of arsenic exposure on DNA methylation in cord blood samples from newborn babies and in a human lymphoblast cell line,” Environmental Health, vol. 11, no. 1, p. 31, 2012. View at Publisher · View at Google Scholar · View at Scopus
  24. S. Virani, K. M. Rentschler, M. Nishijo et al., “DNA methylation is differentially associated with environmental cadmium exposure based on sex and smoking status,” Chemosphere, vol. 145, pp. 284–290, 2016. View at Publisher · View at Google Scholar · View at Scopus
  25. K. E. Pelch, E. J. Tokar, B. A. Merrick, and M. P. Waalkes, “Differential DNA methylation profile of key genes in malignant prostate epithelial cells transformed by inorganic arsenic or cadmium,” Toxicology and Applied Pharmacology, vol. 286, no. 3, pp. 159–167, 2015. View at Publisher · View at Google Scholar · View at Scopus
  26. J. Brocato and M. Costa, “Basic mechanics of DNA methylation and the unique landscape of the DNA methylome in metal-induced carcinogenesis,” Critical Reviews in Toxicology, vol. 43, no. 6, pp. 493–514, 2013. View at Publisher · View at Google Scholar · View at Scopus
  27. R. Magaye, J. Zhao, L. Bowman, and M. DING, “Genotoxicity and carcinogenicity of cobalt-, nickel- and copper-based nanoparticles,” Experimental and Therapeutic Medicine, vol. 4, no. 4, pp. 551–561, 2012. View at Publisher · View at Google Scholar · View at Scopus
  28. J. Brocato and M. Costa, “10th NTES conference: nickel and arsenic compounds alter the epigenome of peripheral blood mononuclear cells,” Journal of Trace Elements in Medicine and Biology, vol. 31, pp. 209–213, 2015. View at Publisher · View at Google Scholar · View at Scopus
  29. Q. Ke, T. Ellen, and M. Costa, “Nickel compounds induce histone ubiquitination by inhibiting histone deubiquitinating enzyme activity,” Toxicology and Applied Pharmacology, vol. 228, no. 2, pp. 190–199, 2008. View at Publisher · View at Google Scholar · View at Scopus
  30. X. Zhou, Q. Li, A. Arita, H. Sun, and M. Costa, “Effects of nickel, chromate, and arsenite on histone 3 lysine methylation,” Toxicology and Applied Pharmacology, vol. 236, no. 1, pp. 78–84, 2009. View at Publisher · View at Google Scholar · View at Scopus
  31. L. Ma, Y. Bai, H. Pu et al., “Histone methylation in nickel-smelting industrial workers,” PLoS One, vol. 10, no. 10, article e0140339, 2015. View at Publisher · View at Google Scholar · View at Scopus
  32. J. Z. J. Maccani, D. C. Koestler, B. Lester et al., “Placental DNA methylation related to both infant toenail mercury and adverse neurobehavioral outcomes,” Environmental Health Perspectives, vol. 123, no. 7, pp. 723–729, 2015. View at Publisher · View at Google Scholar · View at Scopus
  33. J. M. Goodrich, N. Basu, A. Franzblau, and D. C. Dolinoy, “Mercury biomarkers and DNA methylation among Michigan dental professionals,” Environmental and Molecular Mutagenesis, vol. 54, no. 3, pp. 195–203, 2013. View at Publisher · View at Google Scholar · View at Scopus
  34. L. Zong, L. Zhou, Y. Hou et al., “Genetic and epigenetic regulation on the transcription of GABRB2: genotype-dependent hydroxymethylation and methylation alterations in schizophrenia,” Journal of Psychiatric Research, vol. 88, pp. 9–17, 2017. View at Publisher · View at Google Scholar
  35. http://monographs.iarc.fr/ENG/Classification/ClassificationsGroupOrder.pdf.
  36. I. V. Budunova and G. M. Williams, “Cell culture assays for chemicals with tumor-promoting or tumor-inhibiting activity based on the modulation of intercellular communication,” Cell Biology and Toxicology, vol. 10, no. 2, pp. 71–116, 1994. View at Publisher · View at Google Scholar · View at Scopus
  37. J. E. Klaunig and Y. Shi, “Assessment of gap junctional intercellular communication,” Current Protocols in Toxicology, 2009, Chapter 2, Unit 2.17. View at Publisher · View at Google Scholar · View at Scopus
  38. R. A. Alyea, N. P. Moore, M. J. LeBaron, B. B. Gollapudi, and R. J. Rasoulpour, “Is the current product safety assessment paradigm protective for epigenetic mechanisms?” Journal of Pharmacological and Toxicological Methods, vol. 66, no. 3, pp. 207–214, 2012. View at Publisher · View at Google Scholar · View at Scopus