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ISRN Chromatography
Volume 2013 (2013), Article ID 801840, 21 pages
http://dx.doi.org/10.1155/2013/801840
Review Article

Metal Species in Biology: Bottom-Up and Top-Down LC Approaches in Applied Toxicological Research

Department of Chemistry, University of Calgary, 2500 University Drive NW, Calgary, AB, T2N 1N4, Canada

Received 30 January 2013; Accepted 19 February 2013

Academic Editors: B. K. Mandal, A. Namera, Y. Qiu, and A. I. Suarez

Copyright © 2013 Jürgen Gailer. 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. M. Tswett, “Physical chemical studies on chlorophyll adsorptions,” Berichte der Deutschen botanischen Gesellschaft, vol. 24, pp. 316–326, 1906.
  2. A. J. P. Martin and R. L. M. Synge, “A new form of chromatogram employing two liquid phases,” Biochemical Journal, vol. 35, pp. 1358–1368, 1941.
  3. L. S. Ettre and K. I. Sakodynskii, “M.S. Tswett and the discovery of chromatography. I: early work (1899–1903),” Chromatographia, vol. 35, no. 3-4, pp. 223–231, 1993. View at Publisher · View at Google Scholar · View at Scopus
  4. A. Zotou, “An overview of recent advances in HPLC instrumentation,” Central European Journal of Chemistry, vol. 10, no. 3, pp. 554–569, 2012. View at Publisher · View at Google Scholar
  5. K. K. Unger and A. I. Liapis, “Adsorbents and columns in analytical high-performance liquid chromatography: a perspective with regard to development and understanding,” Journal of Separation Science, vol. 35, no. 10-11, pp. 1201–1212, 2012. View at Publisher · View at Google Scholar
  6. D. Ishii, K. Asai, K. Hibi, T. Jonokuchi, and M. Nagaya, “A study of micro-high-performance liquid chromatography. I. Development of technique for miniaturization of high-performance liquid chromatography,” Journal of Chromatography, vol. 144, no. 2, pp. 157–168, 1977. View at Scopus
  7. C. G. Horvath, B. A. Preiss, and S. R. Lipsky, “Fast liquid chromatography: an investigation of operating parameters and the separation of nucleotides on pellicular ion exchangers,” Analytical Chemistry, vol. 39, no. 12, pp. 1422–1428, 1967. View at Publisher · View at Google Scholar
  8. P. D. McDonald and D. Patrick, “Fifty years of innovation in analysis and purification,” Chemical Heritage, vol. 26, no. 2, pp. 32–37, 2008.
  9. M. E. Swartz, “UPLC: an introduction and review,” Journal of Liquid Chromatography & Related Technologies, vol. 28, no. 7-8, pp. 1253–1263, 2005. View at Publisher · View at Google Scholar
  10. L. Anderson and C. L. Hunter, “Quantitative mass spectrometric multiple reaction monitoring assays for major plasma proteins,” Molecular & Cellular Proteomics, vol. 5, no. 4, pp. 573–588, 2006.
  11. D. J. States, G. S. Omenn, T. W. Blackwell et al., “Challenges in deriving high-confidence protein identifications from data gathered by a HUPO plasma proteome collaborative study,” Nature Biotechnology, vol. 24, no. 3, pp. 333–338, 2006. View at Publisher · View at Google Scholar · View at Scopus
  12. S. P. Gygi, B. Rist, T. J. Griffin, et al., “Proteome analysis of low-abundance proteins using multidimensional chromatography and isotope-coded affinity tags,” Journal of Proteome Research, vol. 1, no. 1, pp. 47–54, 2002. View at Publisher · View at Google Scholar
  13. D. S. Wishart, “Advances in metabolite identification,” Bioanalysis, vol. 3, no. 15, pp. 1769–1782, 2011. View at Publisher · View at Google Scholar
  14. K. A. Francesconi and F. Pannier, “Selenium metabolites in urine: a critical overview of past work and current status,” Clinical Chemistry, vol. 50, no. 12, pp. 2240–2253, 2004. View at Publisher · View at Google Scholar · View at Scopus
  15. R. F. Service, “Proteomics: ponders prime time,” Science, vol. 321, no. 5897, pp. 1758–1761, 2008. View at Publisher · View at Google Scholar · View at Scopus
  16. J. K. Nicholson and J. C. Lindon, “Systems biology: metabonomics,” Nature, vol. 455, no. 7216, pp. 1054–1056, 2008. View at Publisher · View at Google Scholar · View at Scopus
  17. S. C. Booth, M. L. Workentine, A. M. Weljie, and R. J. Turner, “Metabolomics and its application to studying metal toxicity,” Metallomics, vol. 3, pp. 1142–1152, 2011. View at Publisher · View at Google Scholar
  18. J. van der Greef, P. Stroobant, and R. van der Heijden, “The role of analytical sciences in medical systems biology,” Current Opinion in Chemical Biology, vol. 8, no. 5, pp. 559–565, 2004. View at Publisher · View at Google Scholar
  19. L. Hood, “A systems approach to medicine will transform healthcare,” in Physical Biology from Atoms to Medicine, A. H. Zewail, Ed., pp. 337–366, Imperial College Press, London, UK, 2008.
  20. G. Xindu and W. Lili, “Liquid chromatography of recombinant proteins and protein drugs,” Journal of Chromatography B, vol. 866, no. 1-2, pp. 133–153, 2008. View at Publisher · View at Google Scholar
  21. R. J. McGorrin, “One hundred years of progress in food analysis,” Journal of Agricultural and Food Chemistry, vol. 57, no. 18, pp. 8076–8088, 2009. View at Publisher · View at Google Scholar
  22. L. S. Jackson, “Chemical food safety issues in the United States: past, present, and future,” Journal of Agricultural and Food Chemistry, vol. 57, no. 18, pp. 8161–8170, 2009. View at Publisher · View at Google Scholar · View at Scopus
  23. S. J. Hill, A. Fisher, and M. Foulkes, “Basic concepts and instrumentation for plasma spectrometry,” in Inductively Coupled Plasma Spectrometry and Its Applications, S. J. Hill, Ed., pp. 61–97, Blackwell Publishing, Ames, Iowa, USA, 2007. View at Publisher · View at Google Scholar
  24. F. van Heuveln, H. Meijering, and J. Wieling, “Inductively coupled plasma-MS in drug development: bioanalytical aspects and applications,” Bioanalysis, vol. 4, no. 15, pp. 1933–1965, 2012. View at Publisher · View at Google Scholar
  25. S. Mounicou, J. Szpunar, and R. Lobinski, “Metallomics: the concept and methodology,” Chemical Society Reviews, vol. 38, no. 4, pp. 1119–1138, 2009. View at Publisher · View at Google Scholar · View at Scopus
  26. J. L. Gómez-Ariza, E. Z. Jahromi, M. González-Fernández, T. García-Barrera, and J. Gailer, “Liquid chromatography-inductively coupled plasma-based metallomic approaches to probe health-relevant interactions between xenobiotics and mammalian organisms,” Metallomics, vol. 3, no. 6, pp. 566–577, 2011. View at Publisher · View at Google Scholar · View at Scopus
  27. J. P. Barnett, D. J. Scanlan, and C. A. Blindauer, “Protein fractionation and detection for metalloproteomics: challenges and approaches,” Analytical and Bioanalytical Chemistry, vol. 402, no. 10, pp. 3311–3322, 2012. View at Publisher · View at Google Scholar
  28. J. Szpunar, “Advances in analytical methodology for bioinorganic speciation analysis: metallomics, metalloproteomics and heteroatom-tagged proteomics and metabolomics,” Analyst, vol. 130, no. 4, pp. 442–465, 2005. View at Publisher · View at Google Scholar · View at Scopus
  29. R. Dufault, B. LeBlanc, R. Schnoll, et al., “Mercury from chlor-alkali plants: measured concentrations in food product sugar,” Environmental Health, vol. 8, article 2, 2009. View at Publisher · View at Google Scholar
  30. D. Gilbert-Diamond, K. L. Cottingham, J. F. Gruber et al., “Rice consumption contributes to arsenic exposure in US women,” Proceedings of the National Academy of Sciences of the United States of America, vol. 108, no. 51, pp. 20656–20660, 2011. View at Publisher · View at Google Scholar
  31. H. H. Harris, I. J. Pickering, and G. N. George, “The chemical form of mercury in fish,” Science, vol. 301, no. 5637, p. 1203, 2003. View at Publisher · View at Google Scholar · View at Scopus
  32. J. Gailer, “Arsenic-selenium and mercury-selenium bonds in biology,” Coordination Chemistry Reviews, vol. 251, no. 1-2, pp. 234–254, 2007. View at Publisher · View at Google Scholar
  33. A. Bhatnagar, “Environmental cardiology: studying mechanistic links between pollution and heart disease,” Circulation Research, vol. 99, no. 7, pp. 692–705, 2006. View at Publisher · View at Google Scholar · View at Scopus
  34. J. Gailer, “Probing the bioinorganic chemistry of toxic metals in the mammalian bloodstream to advance human health,” Journal of Inorganic Biochemistry, vol. 108, pp. 128–132, 2012. View at Publisher · View at Google Scholar
  35. E. Z. Jahromi and J. Gailer, “Probing bioinorganic chemistry processes in the bloodstream to gain new insights into the origin of human diseases,” Dalton Transactions, vol. 39, no. 2, pp. 329–336, 2010. View at Publisher · View at Google Scholar · View at Scopus
  36. E. Z. Jahromi and J. Gailer, “In vitro assessment of chelating agents with regard to their abstraction efficiency of Cd2+ bound to plasma proteins,” Metallomics, vol. 4, no. 9, pp. 995–1003, 2012. View at Publisher · View at Google Scholar
  37. M. Sooriyaarachchi, A. Narendran, and J. Gailer, “The effect of sodium thiosulfate on the metabolism of cis-platin in human plasma in vitro,” Metallomics, vol. 4, no. 9, pp. 960–967, 2012. View at Publisher · View at Google Scholar
  38. M. Montes-Bayón, K. DeNicola, and J. A. Caruso, “Liquid chromatography-inductively coupled plasma mass spectrometry,” Journal of Chromatography A, vol. 1000, no. 1-2, pp. 457–476, 2003. View at Publisher · View at Google Scholar
  39. J. López-Barea and J. L. Gómez-Ariza, “Environmental proteomics and metallomics,” Proteomics, vol. 6, supplement 1, pp. S51–S62, 2006. View at Scopus
  40. M. A. O. da Silva, A. Sussulini, and M. A. Z. Arruda, “Metalloproteomics as an interdisciplinary area involving proteins and metals,” Expert Review of Proteomics, vol. 7, no. 3, pp. 387–400, 2010. View at Publisher · View at Google Scholar · View at Scopus
  41. W. Shi and M. R. Chance, “Metalloproteomics: forward and reverse approaches in metalloprotein structural and functional characterization,” Current Opinion in Chemical Biology, vol. 15, no. 1, pp. 144–148, 2011. View at Publisher · View at Google Scholar
  42. W. Mertz, “The essential trace elements,” Science, vol. 213, no. 4514, pp. 1332–1338, 1981. View at Scopus
  43. N. C. Andrews and P. J. Schmidt, “Iron homeostasis,” Annual Reviews of Physiology, vol. 69, pp. 69–85, 2007. View at Publisher · View at Google Scholar
  44. W. Maret and Y. Li, “Coordination dynamics of zinc in proteins,” Chemical Reviews, vol. 109, no. 10, pp. 4682–4707, 2009. View at Publisher · View at Google Scholar · View at Scopus
  45. J. T. Rubino and K. J. Franz, “Coordination chemistry of copper proteins: how nature handles a toxic cargo for essential function,” Journal of Inorganic Biochemistry, vol. 107, no. 1, pp. 129–143, 2012. View at Publisher · View at Google Scholar
  46. S. M. Yannone, S. Hartung, A. L. Menon, M. W. W. Adams, and J. A. Tainer, “Metals in biology: defining metalloproteomes,” Current Opinion in Biotechnology, vol. 23, no. 1, pp. 89–95, 2012. View at Publisher · View at Google Scholar
  47. S. L. Sensi, P. Paoletti, A. I. Bush, and I. Sekler, “Zinc in the physiology and pathology of the CNS,” Nature Reviews Neuroscience, vol. 10, no. 11, pp. 780–791, 2009. View at Publisher · View at Google Scholar · View at Scopus
  48. K. J. Waldron, J. C. Rutherford, D. Ford, and N. J. Robinson, “Metalloproteins and metal sensing,” Nature, vol. 460, no. 7257, pp. 823–830, 2009. View at Publisher · View at Google Scholar · View at Scopus
  49. W. Maret, “Metalloproteomics, metalloproteomes, and the annotation of metalloproteins,” Metallomics, vol. 2, no. 2, pp. 117–125, 2010. View at Publisher · View at Google Scholar · View at Scopus
  50. J. K. Nicholson and I. D. Wilson, “Understanding 'global' systems biology: metabonomics and the continuum of metabolism,” Nature Reviews Drug Discovery, vol. 2, no. 8, pp. 668–676, 2003. View at Scopus
  51. J. L. Peters, T. S. Perlstein, M. J. Perry, E. McNeely, and J. Weuve, “Cadmium exposure in association with history of stroke and heart failure,” Environmental Research, vol. 110, no. 2, pp. 199–206, 2010. View at Publisher · View at Google Scholar · View at Scopus
  52. O. Andersen, “Chemical and biological considerations in the treatment of metal intoxications by chelating agents,” Mini-Reviews in Medicinal Chemistry, vol. 4, no. 1, pp. 11–21, 2004. View at Publisher · View at Google Scholar
  53. M. Sooriyaarachchi, A. Narendran, and J. Gailer, “Comparative hydrolysis and plasma protein binding of cis-platin and carboplatin in human plasma in vitro,” Metallomics, vol. 3, no. 1, pp. 49–55, 2011. View at Publisher · View at Google Scholar · View at Scopus
  54. T. W. Hambley, “Developing new metal-based therapeutics: challenges and opportunities,” Dalton Transactions, no. 43, pp. 4929–4937, 2007. View at Publisher · View at Google Scholar · View at Scopus
  55. J. Reedijk, “Why does cisplatin reach guanine-N7 with competing S-donor ligands available in the cell?” Chemical Reviews, vol. 99, no. 9, pp. 2499–2510, 1999. View at Publisher · View at Google Scholar
  56. B. H. Ali and M. S. Al Moundhri, “Agents ameliorating or augmenting the nephrotoxicity of cisplatin and other platinum compounds: a review of some recent research,” Food and Chemical Toxicology, vol. 44, no. 8, pp. 1173–1183, 2006. View at Publisher · View at Google Scholar · View at Scopus
  57. K. C. M. Campbell, R. P. Meech, J. J. Klemens et al., “Prevention of noise- and drug-induced hearing loss with d-methionine,” Hearing Research, vol. 226, no. 1-2, pp. 92–103, 2007. View at Publisher · View at Google Scholar · View at Scopus
  58. G. D. Zeevalk and W. J. Nicklas, “Mechanisms underlying initiation of excitotoxicity associated with metabolic inhibition,” Journal of Pharmacology and Experimental Therapeutics, vol. 257, no. 2, pp. 870–878, 1991.
  59. S. Cestèle and W. A. Catterall, “Molecular mechanisms of neurotoxin action on voltage-gated sodium channels,” Biochimie, vol. 82, no. 9-10, pp. 883–892, 2000. View at Publisher · View at Google Scholar
  60. K. Cottingham, “Systems biology: a boon for analytical chemists?” Analytical Chemistry, vol. 77, no. 9, pp. 197A–200A, 2005. View at Publisher · View at Google Scholar
  61. J. Gailer, G. N. George, I. J. Pickering et al., “Structural basis of the antagonism between inorganic mercury and selenium in mammals,” Chemical Research in Toxicology, vol. 13, no. 11, pp. 1135–1142, 2000. View at Publisher · View at Google Scholar · View at Scopus
  62. J. Gailer, G. N. George, I. J. Pickering et al., “A metabolic link between arsenite and selenite: the seleno-bis(S- glutathionyl) arsinium ion,” Journal of the American Chemical Society, vol. 122, no. 19, pp. 4637–4639, 2000. View at Publisher · View at Google Scholar · View at Scopus
  63. J. Gailer, S. Madden, G. A. Buttigieg, M. B. Denton, and H. S. Younis, “Identification of [(GS)2AsSe] in rabbit bile by size-exclusion chromatography and simultaneous multielement-specific detection by inductively coupled plasma atomic emission spectroscopy,” Applied Organometallic Chemistry, vol. 16, no. 2, pp. 72–75, 2002. View at Publisher · View at Google Scholar
  64. J. Gailer, L. Ruprecht, P. Reitmeir, B. Benker, and P. Schramel, “Mobilization of exogenous and endogenous selenium to bile after the intravenous administration of environmentally relevant doses of arsenite to rabbits,” Applied Organometallic Chemistry, vol. 18, no. 12, pp. 670–675, 2004. View at Publisher · View at Google Scholar · View at Scopus
  65. J. Gailer, G. N. George, I. J. Pickering, R. C. Prince, H. S. Younis, and J. J. Winzerling, “Biliary excretion of [(GS)2AsSe]- after intravenous injection of rabbits with arsenite and selenate,” Chemical Research in Toxicology, vol. 15, no. 11, pp. 1466–1471, 2002. View at Publisher · View at Google Scholar · View at Scopus
  66. P. Hunter, P. Robbins, and D. Noble, “The IUPS human physiome project,” Pflügers Archiv, vol. 445, no. 1, pp. 1–9, 2002. View at Publisher · View at Google Scholar
  67. L. Hood, J. R. Heath, M. E. Phelps, and B. Lin, “Systems biology and new technologies enable predictive and preventative medicine,” Science, vol. 306, no. 5696, pp. 640–643, 2004. View at Publisher · View at Google Scholar · View at Scopus
  68. L. M. Gierasch and A. Gershenson, “Post-reductionist protein science, or putting Humpty Dumpty back together again,” Nature Chemical Biology, vol. 5, pp. 774–777, 2009. View at Publisher · View at Google Scholar
  69. D. Noble, The Music of Life, Biology Beyond Genes, Oxford University Press, New York, NY, USA, 2006.
  70. F. R. Luo, S. D. Wyrick, and S. G. Chaney, “Biotransformations of oxaliplatin in rat blood in vitro,” Journal of Biochemical and Molecular Toxicology, vol. 13, no. 3-4, pp. 159–169, 1999. View at Scopus
  71. C. Jumarie, C. Fortin, M. Houde, P. G. C. Campbell, and F. Denizeau, “Cadmium uptake by Caco-2 cells: effects of Cd complexation by chloride, glutathione, and phytochelatins,” Toxicology and Applied Pharmacology, vol. 170, no. 1, pp. 29–38, 2001. View at Publisher · View at Google Scholar · View at Scopus
  72. R. K. Zalups, “Molecular interactions with mercury in the kidney,” Pharmacological Reviews, vol. 52, no. 1, pp. 113–143, 2000.
  73. R. K. Zalups and S. Ahmad, “Molecular handling of cadmium in transporting epithelia,” Toxicology and Applied Pharmacology, vol. 186, no. 3, pp. 163–188, 2003. View at Publisher · View at Google Scholar
  74. J. L. Webb, “Arsenicals,” in Enzyme and Metabolic Inhibitors, J. L. Webb, Ed., vol. 3, pp. 595–793, Academic Press, London, UK, 1966.
  75. S. A. Manley and J. Gailer, “Analysis of the plasma metalloproteome by SEC-ICP-AES: bridging proteomics and metabolomics,” Expert Review of Proteomics, vol. 6, no. 3, pp. 251–265, 2009. View at Publisher · View at Google Scholar · View at Scopus
  76. G. Chillemi, G. Mancini, N. Sanna et al., “Evidence for sevenfold coordination in the first solvation shell of Hg(II) aqua ion,” Journal of the American Chemical Society, vol. 129, no. 17, pp. 5430–5436, 2007. View at Publisher · View at Google Scholar · View at Scopus
  77. G. M. Whitesides, P. W. Snyder, D. T. Moustakas, and K. A. Mirica, “Designing ligands to bind tightly to proteins,” in Physical Biology, from Atoms to Medicine, A. H. Zewail, Ed., pp. 189–215, Imperial College Press, London, UK, 2008. View at Publisher · View at Google Scholar
  78. J. P. K. Rooney, “The role of thiols, dithiols, nutritional factors and interacting ligands in the toxicology of mercury,” Toxicology, vol. 234, no. 3, pp. 145–156, 2007. View at Publisher · View at Google Scholar · View at Scopus
  79. A. Casini and J. Reedijk, “Interactions of anticancer Pt compounds with proteins: an overlooked topic in medicinal inorganic chemistry?” Chemical Science, vol. 3, no. 11, pp. 3135–3144, 2012. View at Publisher · View at Google Scholar
  80. A. R. Timerbaev, C. G. Hartinger, S. S. Aleksenko, and B. K. Keppler, “Interactions of antitumor metallodrugs with serum proteins: advances in characterization using modern analytical methodology,” Chemical Reviews, vol. 106, no. 6, pp. 2224–2248, 2006. View at Publisher · View at Google Scholar · View at Scopus
  81. M. Knipp, “Metallothioneins and platinum(II) anti-tumor compounds,” Current Medicinal Chemistry, vol. 16, pp. 522–537, 2009. View at Publisher · View at Google Scholar
  82. J. Gailer, “Reactive selenium metabolites as targets of toxic metals/metalloids in mammals: a molecular toxicological perspective,” Applied Organometallic Chemistry, vol. 16, no. 12, pp. 701–707, 2002. View at Publisher · View at Google Scholar
  83. W. Hu, Q. Luo, K. Wu et al., “The anticancer drug cisplatin can cross-link the interdomain zinc site on human albumin,” Chemical Communications, vol. 47, no. 21, pp. 6006–6008, 2011. View at Publisher · View at Google Scholar · View at Scopus
  84. J. Gailer, “Chronic toxicity of AsIII in mammals: the role of (GS)2AsSe-,” Biochimie, vol. 91, no. 10, pp. 1268–1272, 2009. View at Publisher · View at Google Scholar · View at Scopus
  85. M. T. Le, J. Gailer, and E. J. Prenner, “Hg2+ and Cd2+ interact differently with biomimetic erythrocyte membranes,” BioMetals, vol. 22, no. 2, pp. 261–274, 2009. View at Publisher · View at Google Scholar · View at Scopus
  86. N. Ballatori, “Transport of toxic metals by molecular mimicry,” Environmental Health Perspectives, vol. 110, no. 5, pp. 689–694, 2002. View at Scopus
  87. R. H. Holm, P. Kennepohl, and E. I. Solomon, “Structural and functional aspects of metal sites in biology,” Chemical Reviews, vol. 96, no. 7, pp. 2239–2314, 1996. View at Scopus
  88. B. P. Esposito and R. Najjar, “Interactions of antitumoral platinum-group metallodrugs with albumin,” Coordination Chemistry Reviews, vol. 232, no. 1-2, pp. 137–149, 2002. View at Publisher · View at Google Scholar
  89. N. Ballatori and A. T. Truong, “Mechanisms of hepatic methylmercury uptake,” Journal of Toxicology and Environmental Health, vol. 46, no. 3, pp. 343–353, 1995. View at Scopus
  90. N. Shimojo, Y. Kumagai, and J. Nagafune, “Difference between kidney and liver in decreased manganese superoxide dismutase activity caused by exposure of mice to mercuric chloride,” Archives of Toxicology, vol. 76, no. 7, pp. 383–387, 2002. View at Publisher · View at Google Scholar · View at Scopus
  91. S. A. Manley, G. N. George, I. J. Pickering et al., “The seleno bis(S-glutathionyl) arsinium ion is assembled in erythrocyte lysate,” Chemical Research in Toxicology, vol. 19, no. 4, pp. 601–607, 2006. View at Publisher · View at Google Scholar · View at Scopus
  92. A. Meister, “Glutathione metabolism and its selective modification,” Journal of Biological Chemistry, vol. 263, no. 33, pp. 17205–17208, 1988. View at Scopus
  93. J. M. Mates, J. A. Segura, and F. J. Alonso, “Roles of dioxins and heavy metals in cancer and neurological diseases using ROS-mediated mechanisms,” Free Radical Biology and Medicine, vol. 49, no. 9, pp. 1328–1341, 2010. View at Publisher · View at Google Scholar
  94. T. J. Hagele, J. N. Mazerik, A. Gregory et al., “Mercury activates vascular endothelial cell phospholipase D through thiols and oxidative stress,” International Journal of Toxicology, vol. 26, no. 1, pp. 57–69, 2007. View at Publisher · View at Google Scholar · View at Scopus
  95. S. Bhattacharya, S. Bose, B. Mukhopadhyay et al., “Specific binding of inorganic mercury to Na- K-ATPase in rat liver plasma membrane and signal transduction,” BioMetals, vol. 10, no. 3, pp. 157–162, 1997. View at Publisher · View at Google Scholar · View at Scopus
  96. D. R. Green and G. Kroemer, “The pathophysiology of mitochondrial cell death,” Science, vol. 305, no. 5684, pp. 626–629, 2004. View at Publisher · View at Google Scholar · View at Scopus
  97. S. Orrenius and B. Zhivotovsky, “The future of toxicology—does it matter how cells die?” Chemical Research in Toxicology, vol. 19, pp. 729–733, 2006. View at Publisher · View at Google Scholar
  98. J. D. Robertson and S. Orrenius, “Molecular mechanisms of apoptosis Induced by cytotoxic chemicals,” Critical Reviews in Toxicology, vol. 30, no. 5, pp. 609–627, 2000. View at Publisher · View at Google Scholar
  99. U. Landegren, J. Vänelid, M. Hammond et al., “Opportunities for sensitive plasma proteome analysis,” Analytical Chemistry, vol. 84, no. 4, pp. 1824–1830, 2012. View at Publisher · View at Google Scholar
  100. S. A. Manley, S. Byrns, A. W. Lyon, P. Brown, and J. Gailer, “Simultaneous Cu-, Fe-, and Zn-specific detection of metalloproteins contained in rabbit plasma by size-exclusion chromatography-inductively coupled plasma atomic emission spectroscopy,” JBIC Journal of Biological Inorganic Chemistry, vol. 14, no. 1, pp. 61–74, 2009. View at Publisher · View at Google Scholar
  101. P. J. Sadler and J. H. Viles, “1H and 113Cd NMR investigations of Cd2+ and Zn2+ binding sites on serum albumin: competition with Ca2+, Ni2+, Cu2+, and Zn2+,” Inorganic Chemistry, vol. 35, no. 15, pp. 4490–4496, 1996. View at Publisher · View at Google Scholar
  102. D. C. Carter and J. X. Ho, “Structure of serum albumin,” Advances in Protein Chemistry, vol. 45, pp. 153–203, 1994. View at Publisher · View at Google Scholar
  103. V. Sahni, D. Choudhury, and Z. Ahmed, “Chemotherapy-associated renal dysfunction,” Nature Reviews Nephrology, vol. 5, pp. 450–462, 2009. View at Publisher · View at Google Scholar
  104. D. Wang and S. J. Lippard, “Cellular processing of platinum anticancer drugs,” Nature Reviews Drug Discovery, vol. 4, pp. 307–320, 2005. View at Publisher · View at Google Scholar
  105. F. Caurant, M. Navarro, and J. C. Amiard, “Mercury in pilot whales: possible limits to the detoxification process,” Science of the Total Environment, vol. 186, no. 1-2, pp. 95–104, 1996. View at Publisher · View at Google Scholar · View at Scopus
  106. M. Korbas, J. L. O. 'Donoghue, G. E. Watson et al., “The chemical nature of mercury in human brain following poisoning or environmental exposure,” ACS Chemical Neuroscience, vol. 1, no. 12, pp. 810–818, 2010. View at Publisher · View at Google Scholar
  107. J. P. Berry and P. Galle, “Selenium-arsenic interaction in renal cells: role of lysosomes. Electron microprobe study,” Journal of Submicroscopic Cytology and Pathology, vol. 26, no. 2, pp. 203–210, 1994. View at Scopus
  108. S. Hann, G. Koellensperger, Z. Stefánka et al., “Application of HPLC-ICP-MS to speciation of cisplatin and its degradation products in water containing different chloride concentrations and in human urine,” Journal of Analytical Atomic Spectrometry, vol. 18, pp. 1391–1395, 2003. View at Publisher · View at Google Scholar
  109. Z. Gregus and C. D. Klaassen, “Disposition of metals in rats: a comparative study of fecal, urinary, and biliary excretion and tissue distribution of eighteen metals,” Toxicology and Applied Pharmacology, vol. 85, no. 1, pp. 24–38, 1986. View at Publisher · View at Google Scholar
  110. K. T. Suzuki, “Direct connection of high-speed liquid chromatograph (equipped with gel permeation column) to atomic absorption spectrophotometer for metalloprotein analysis: metallothionein,” Analytical Biochemistry, vol. 102, no. 1, pp. 31–34, 1980. View at Publisher · View at Google Scholar
  111. K. T. Suzuki, H. Sunaga, E. Kobayashi, and N. Shimojo, “Mercaptalbumin as a selective cadmium-binding protein in rat serum,” Toxicology and Applied Pharmacology, vol. 86, no. 3, pp. 466–473, 1986. View at Publisher · View at Google Scholar
  112. S. J. Berners-Price and P. J. Sadler, “Coordination chemistry of metallodrugs: insights into biological speciation from NMR spectroscopy,” Coordination Chemistry Reviews, vol. 151, pp. 1–40, 1996.
  113. M. Groessl and P. J. Dyson, “Bioanalytical and biophysical techniques for the elucidation of the mode of action of metal-based drugs,” Current Topics in Medicinal Chemistry, vol. 11, no. 21, pp. 2632–2646, 2011. View at Publisher · View at Google Scholar
  114. V. Mah and F. Jalilehvand, “Cadmium(II) complex formation with glutathione,” JBIC Journal of Biological Inorganic Chemistry, vol. 15, no. 3, pp. 441–458, 2010. View at Publisher · View at Google Scholar
  115. R. Ortega, A. Carmona, I. Llorens, and P. L. Solari, “X-ray absorption spectroscopy of biological samples. A tutorial,” Journal of Analytical Atomic Spectrometry, vol. 27, pp. 2054–2065, 2012. View at Publisher · View at Google Scholar
  116. N. Cetinbas, M. I. Webb, J. A. Dubland, and C. J. Walsby, “Serum-protein interactions with anticancer Ru(III) complexes KP1019 and KP418 characterized by EPR,” JBIC Journal of Biological Inorganic Chemistry, vol. 15, no. 2, pp. 131–145, 2010. View at Publisher · View at Google Scholar
  117. Y. Kasherman, S. Sturup, and D. Gibson, “Is glutathione the major cellular target of cisplatin? A study of the interactions of cisplatin with cancer cell extracts,” Journal of Medicinal Chemistry, vol. 52, no. 14, pp. 4319–4328, 2009. View at Publisher · View at Google Scholar · View at Scopus
  118. D. Gibson, “The mechanism of action of platinum anticancer agents—what do we really know about it?” Dalton Transactions, no. 48, pp. 10681–10689, 2009. View at Publisher · View at Google Scholar · View at Scopus
  119. E. Z. Jahromi, W. White, Q. Wu, R. Yamdagni, and J. Gailer, “Remarkable effect of mobile phase buffer on the SEC-ICP-AES derived Cu, Fe and Zn-metalloproteome pattern of rabbit blood plasma,” Metallomics, vol. 2, no. 7, pp. 460–468, 2010. View at Publisher · View at Google Scholar · View at Scopus
  120. C. C. Wu, P. H. Peng, Y. T. Chang et al., “Identification of potential serum markers for nasopharyngeal carcinoma from a xenografted mouse model using Cy-dye labeling combined with three-dimensional fractionation,” Proteomics, vol. 8, no. 17, pp. 3605–3620, 2008. View at Publisher · View at Google Scholar · View at Scopus
  121. K. L. Pei, M. Sooriyaarachchi, D. A. Sherrell, G. N. George, and J. Gailer, “Probing the coordination behavior of Hg2+, CH3Hg+, and Cd2+ towards mixtures of two biological thiols by HPLC-ICP-AES,” Journal of Inorganic Biochemistry, vol. 105, no. 3, pp. 375–381, 2011. View at Publisher · View at Google Scholar · View at Scopus
  122. E. K. M. Ueda, P. W. Gout, and L. Morganti, “Current and prospective applications of metal ion-protein binding,” Journal of Chromatography A, vol. 988, no. 1, pp. 1–23, 2003. View at Publisher · View at Google Scholar · View at Scopus
  123. L. Andersson, E. Sulkowski, and J. Porath, “Immobilized metal ion affinity chromatography of serum albumins.,” Bioseparation, vol. 2, no. 1, pp. 15–22, 1991. View at Scopus
  124. L. Gelunaite, V. Lukša, O. Sudžiuviene, V. Bumelis, and H. Pesliakas, “Chelated mercury as a ligand in immobilized metal ion affinity chromatography of proteins,” Journal of Chromatography A, vol. 904, no. 2, pp. 131–143, 2000. View at Publisher · View at Google Scholar · View at Scopus
  125. A. Meister and M. E. Anderson, “Glutathione,” Annual Review of Biochemistry, vol. 52, pp. 711–760, 1983. View at Publisher · View at Google Scholar
  126. N. Kaplowitz, T. Y. Aw, and M. Ookhtens, “The regulation of hepatic glutathione,” Annual Review of Pharmacology and Toxicology, vol. 25, pp. 715–744, 1985. View at Publisher · View at Google Scholar
  127. K. L. Haas and K. F. Franz, “Application of metal coordination chemistry to explore and manipulate cell biology,” Chemical Reviews, vol. 109, no. 10, pp. 4921–4960. View at Publisher · View at Google Scholar
  128. R. K. Singhal, M. E. Anderson, and A. Meister, “Glutathione, a first line of defense against cadmium toxicity,” FASEB Journal, vol. 1, no. 3, pp. 220–223, 1987. View at Scopus
  129. A. Naganuma, M. E. Anderson, and A. Meister, “Cellular glutathione as a determinant of sensitivity to mercuric chloride toxicity: prevention of toxicity by giving glutathione monoester,” Biochemical Pharmacology, vol. 40, no. 4, pp. 693–697, 1990. View at Publisher · View at Google Scholar · View at Scopus
  130. D. L. Rabenstein, “Metal complexes of glutathione and their biological significance,” in Glutathione: Chemical, Biochemical, and Medical Aspects, D. Dolphin, O. Avramovic, and R. Poulson, Eds., pp. 147–186, John Wiley & Sons, New York, NY, USA, 1989.
  131. J. Gailer, G. N. George, I. J. Pickering, G. A. Buttigieg, M. B. Denton, and R. S. Glass, “Synthesis, X-ray absorption spectroscopy and purification of the seleno-bis (S-glutathionyl) arsinium anion from selenide, arsenite and glutathione,” Journal of Organometallic Chemistry, vol. 650, no. 1-2, pp. 108–113, 2002. View at Publisher · View at Google Scholar · View at Scopus
  132. L. H. Lash and D. P. Jones, “Distribution of oxidized and reduced forms of glutathione and cysteine in rat plasma,” Archives of Biochemistry and Biophysics, vol. 240, no. 2, pp. 583–592, 1985. View at Publisher · View at Google Scholar
  133. B. Sebille, N. Thuaud, and J. P. Tillement, “Retention data methods for the determination of drug-protein binding parameters by high-performance liquid chromatography,” Journal of Chromatography, vol. 204, pp. 285–291, 1981. View at Scopus
  134. B. Sebille and N. Thuaud, “Determination of tryptophan-human serum albumin binding from retention data and separation of tryptophan enantiomer by high performance liquid chromatography,” Journal of Liquid Chromatography, vol. 3, no. 2, pp. 299–308, 1980. View at Publisher · View at Google Scholar
  135. J. Gailer and W. Lindner, “On-column formation of arsenic-glutathione species detected by size-exclusion chromatography in conjunction with arsenic-specific detectors,” Journal of Chromatography B, vol. 716, pp. 83–93, 1998. View at Publisher · View at Google Scholar
  136. A. J. Percy and J. Gailer, “Methylated trivalent arsenic-glutathione complexes are more stable than their arsenite analog,” Bioinorganic Chemistry and Applications, vol. 2008, Article ID 539082, 8 pages, 2008. View at Publisher · View at Google Scholar
  137. K. Rehman and H. Naranmandura, “Arsenic metabolism and thioarsenicals,” Metallomics, vol. 4, no. 9, pp. 881–892, 2012. View at Publisher · View at Google Scholar
  138. S. V. Kala, M. W. Neely, G. Kala et al., “The MRP2/cMOAT transporter and arsenic-glutathione complex formation are required for biliary excretion of arsenic,” Journal of Biological Chemistry, vol. 275, no. 43, pp. 33404–33408, 2000. View at Publisher · View at Google Scholar · View at Scopus
  139. E. M. Leslie, “Arsenic-glutathione conjugate transport by the human multidrug resistance proteins (MRPs/ABCCs),” Journal of Inorganic Biochemistry, vol. 108, pp. 141–149, 2012. View at Publisher · View at Google Scholar
  140. E. M. Leslie, R. G. Deely, and S. P. C. Cole, “Toxicological relevance of the multidrug resistance protein 1, MRP1 (ABCC1) and related transporters,” Toxicology, vol. 167, no. 1, pp. 3–23, 2001. View at Publisher · View at Google Scholar
  141. N. Ballatori, S. M. Krance, R. Marchan, and C. L. Hammond, “Plasma membrane glutathione transporters and their roles in cell physiology and pathophysiology,” Molecular Aspects of Medicine, vol. 30, no. 1-2, pp. 13–28, 2009. View at Publisher · View at Google Scholar · View at Scopus
  142. R. S. Braman and C. C. Foreback, “Methylated forms of arsenic in the environment,” Science, vol. 182, no. 4118, pp. 1247–1249, 1973. View at Scopus
  143. A. J. Percy, M. Korbas, G. N. George, and J. Gailer, “Reversed-phase high-performance liquid chromatographic separation of inorganic mercury and methylmercury driven by their different coordination chemistry towards thiols,” Journal of Chromatography A, vol. 1156, no. 1-2, pp. 331–339, 2007. View at Publisher · View at Google Scholar · View at Scopus
  144. Š. Baláž, M. Wiese, and J. K. Seydel, “A time hierarchy-based model for kinetics of drug disposition and its use in quantitative structure-activity relationships,” Journal of Pharmaceutical Sciences, vol. 81, no. 9, pp. 849–857, 1992. View at Publisher · View at Google Scholar
  145. J. D. Meers, E. Z. Jahromi, B. Heyne, and J. Gailer, “Improved RP-HPLC separation of Hg2+ and CH3Hg+ using a mixture of thiol-based mobile phase additives,” Journal of Environmental Science and Health A, vol. 47, no. 1, pp. 149–154, 2012. View at Publisher · View at Google Scholar
  146. G. Girardi and M. M. Elias, “Effectiveness of N-acetylcysteine in protecting against mercuric chloride-induced nephrotoxicity,” Toxicology, vol. 67, no. 2, pp. 155–164, 1991. View at Publisher · View at Google Scholar · View at Scopus
  147. N. Ballatori, M. W. Lieberman, and W. Wang, “N-acetylcysteine as an antidote in methylmercury poisoning,” Environmental Health Perspectives, vol. 106, no. 5, pp. 267–271, 1998. View at Scopus
  148. A. S. Koh, T. A. Simmons-Willis, J. B. Pritchard, S. M. Grassl, and N. Ballatori, “Identification of a mechanism by which the methylmercury antidotes N-acetylcysteine and dimercaptopropanesulfonate enhance urinary metal excretion: transport by the renal organic anion transporter-1,” Molecular Pharmacology, vol. 62, no. 4, pp. 921–926, 2002. View at Publisher · View at Google Scholar · View at Scopus
  149. E. Hjortsø, J. S. Fomsgaard, and N. Fogh-Andersen, “Does N-acetylcysteine increase the excretion of trace metals (calcium, magnesium, iron, zinc and copper) when given orally?” European Journal of Clinical Pharmacology, vol. 39, no. 1, pp. 29–31, 1990. View at Publisher · View at Google Scholar
  150. L. Chapman and H. M. Chan, “The influence of nutrition on methyl mercury intoxication,” Environmental Health Perspectives, vol. 108, no. 1, pp. 29–56, 2000. View at Scopus
  151. R. K. Zalups and L. H. Lash, “Interactions between glutathione and mercury in the kidney, liver, and blood,” in Toxicology of Metals, L. W. Chang, Ed., pp. 145–163, CRC Lewis Publishers, Boca Raton, Fla, USA, 1996.
  152. E. Mitchell, S. Frisbie, and B. Sarkar, “Exposure to multiple metals from groundwater-a global crisis: geology, climate change, health effects, testing, and mitigation,” Metallomics, vol. 3, no. 9, pp. 874–908, 2011. View at Publisher · View at Google Scholar
  153. K. P. DuBois, A. L. Moxon, and O. E. Olson, “Further studies on the effective ness of arsenic in preventing selenium poisoning,” Journal of Nutrition, vol. 19, pp. 477–482, 1940.
  154. B. Michalke, “Selenspeziation mit SAX-ICP-MS und RPLC-ICP-MS,” in Moderne Techniken Der Ionenanalyse, K. Fischer and D. Jensen, Eds., pp. 50–60, ECOMED Verlagsgesellschaft, Landsberg, Germany, 2002.
  155. J. Gailer, S. Madden, M. F. Burke, M. B. Denton, and H. V. Aposhian, “Simultaneous multielement-specific detection of a novel glutathione-arsenic-selenium ion [(GS)2AsSe] by ICP AES after micellar size- exclusion chromatography,” Applied Organometallic Chemistry, vol. 14, no. 7, pp. 355–363, 2000.
  156. J. Parizek and I. Ostadalova, “The protective effect of small amounts of selenite in sublimate intoxication,” Experientia, vol. 23, no. 2, pp. 142–143, 1967. View at Publisher · View at Google Scholar
  157. S. Yoneda and K. T. Suzuki, “Equimolar Hg-Se complex binds to selenoprotein P,” Biochemical and Biophysical Research Communications, vol. 231, no. 1, pp. 7–11, 1997. View at Publisher · View at Google Scholar
  158. M. M. El-Begearmi, H. E. Ganther, and M. L. Sunde, “Dietary interaction between methylmercury, selenium, arsenic, and sulfur amino acids in Japanese quail,” Poultry Science, vol. 61, no. 2, pp. 272–279, 1982. View at Scopus
  159. A. Naganuma and N. Imura, “Methylmercury binds to a low molecular weight substance in rabbit and human erythrocytes,” Toxicology and Applied Pharmacology, vol. 47, no. 3, pp. 613–616, 1979. View at Publisher · View at Google Scholar
  160. Y. Sugiura, Y. Tamai, and H. Tanaka, “Selenium protection against mercury toxicity: high binding affinity of methylmercury by selenium-containing ligands in comparison with sulfur-containing ligands,” Bioinorganic Chemistry, vol. 9, no. 2, pp. 167–180, 1978. View at Publisher · View at Google Scholar
  161. M. Korbas, A. J. Percy, J. Gailer, and G. N. George, “A possible molecular link between the toxicological effects of arsenic, selenium and methylmercury: methylmercury(II) seleno bis(S-glutathionyl) arsenic(III),” JBIC Journal of Biological Inorganic Chemistry, vol. 13, no. 3, pp. 461–470, 2008. View at Publisher · View at Google Scholar
  162. T. W. Hambley, “Chemistry: metal-based therapeutics,” Science, vol. 318, no. 5855, pp. 1392–1393, 2007. View at Publisher · View at Google Scholar · View at Scopus
  163. K. H. Thompson and C. Orvig, “Boon and bane of metal ions in medicine,” Science, vol. 300, no. 5621, pp. 936–939, 2003. View at Publisher · View at Google Scholar · View at Scopus
  164. M. J. Abrams and B. A. Murrer, “Metal compounds in therapy and diagnosis,” Science, vol. 261, no. 5122, pp. 725–730, 1993. View at Scopus
  165. A. M. Pizarro and P. J. Sadler, “Unusual DNA binding modes for metal anticancer complexes,” Biochimie, vol. 91, no. 10, pp. 1198–1211, 2009. View at Publisher · View at Google Scholar · View at Scopus
  166. S. Van Zutphen and J. Reedijk, “Targeting platinum anti-tumour drugs: overview of strategies employed to reduce systemic toxicity,” Coordination Chemistry Reviews, vol. 249, no. 24, pp. 2845–2853, 2005. View at Publisher · View at Google Scholar · View at Scopus
  167. T. W. Hambley, “The influence of structure on the activity and toxicity of Pt anti-cancer drugs,” Coordination Chemistry Reviews, vol. 166, pp. 181–223, 1997. View at Publisher · View at Google Scholar
  168. B. W. Harper, A. M. Krause-Heuer, M. P. Grant, M. Manohar, K. B. Garbutcheon-Singh, and J. R. Aldrich-Wright, “Advances in platinum chemotherapeutics,” Chemistry, vol. 16, no. 24, pp. 7064–7077, 2010. View at Publisher · View at Google Scholar · View at Scopus
  169. J. C. Dabrowiak, J. Goodisman, and A. K. Souid, “Kinetic study of the reaction of cisplatin with thiols,” Drug Metabolism and Disposition, vol. 30, no. 12, pp. 1378–1384, 2002. View at Publisher · View at Google Scholar · View at Scopus
  170. T. Ishikawa and F. Ali-Osman, “Glutathione-associated cis-diamminedichloroplatinum(II) metabolism and ATP-dependent efflux from leukemia cells. Molecular characterization of glutathione-platinum complex and its biological significance,” Journal of Biological Chemistry, vol. 268, no. 27, pp. 20116–20125, 1993. View at Scopus
  171. K. W. Lee and D. S. J. Martin, “Cis-dichlorodiammineplatinum(II). Aquation equilibria and isotopic exchange of chloride ligands with free chloride and tetrachloroplatinate(II),” Inorganica Chimica Acta, vol. 17, pp. 105–110, 1976. View at Publisher · View at Google Scholar
  172. A. V. Klein and T. W. Hambley, “Platinum drug distribution in cancer cells and tumors,” Chemical Reviews, vol. 109, no. 10, pp. 4911–4920, 2009. View at Publisher · View at Google Scholar · View at Scopus
  173. X. Wang and Z. Guo, “The role of sulfur in platinum anticancer chemotherapy,” Anti-Cancer Agents in Medicinal Chemistry, vol. 7, no. 1, pp. 19–34, 2007. View at Publisher · View at Google Scholar
  174. A. I. I. Ivanov, J. Christodoulou, J. A. Parkinson et al., “Cisplatin binding sites on human albumin,” The Journal of Biological Chemistry, vol. 273, no. 24, pp. 14721–14730, 1998. View at Publisher · View at Google Scholar
  175. L. Trynda-Lemiesz, H. Kozlowski, and B. K. Keppler, “Effect of cis-, trans-diamminedichloroplatinum(II) and DBP on human serum albumin,” Journal of Inorganic Biochemistry, vol. 77, no. 3-4, pp. 141–146, 1999. View at Publisher · View at Google Scholar · View at Scopus
  176. N. Ohta, D. Chen, S. Ito, T. Futo, T. Yotsuyanagi, and K. Ikeda, “Effect of trans-diamminedichloroplatinum(II) on human serum albumin: conformational changes through partial disulfide bond cleavage,” International Journal of Pharmaceutics, vol. 118, no. 1, pp. 85–93, 1995. View at Publisher · View at Google Scholar · View at Scopus
  177. D. Esteban-Fernández, M. Montes-Bayón, E. B. González, M. M. Gómez-Gómez, M. A. Palacios, and A. Sanz-Medel, “Atomic (HPLC-ICP-MS) and molecular mass spectrometry (ESI-Q-TOF) to study cis-platin interactions with serum proteins,” Journal of Analytical Atomic Spectrometry, vol. 23, pp. 378–384, 2008. View at Publisher · View at Google Scholar
  178. H. Sun, H. Li, and P. J. Sadler, “Transferrin as a metal ion mediator,” Chemical Reviews, vol. 99, no. 9, pp. 2817–2842, 1999. View at Scopus
  179. J. M. El Hage Chahine, M. Hemadi, and N. T. Ha-Duong, “Uptake and release of metal ions by transferrin and interaction with receptor,” Biochimica et Biophysica Acta, vol. 1820, no. 3, pp. 334–347, 2012. View at Publisher · View at Google Scholar
  180. M. Groessl, M. Terenghi, A. Casini, L. Elviri, R. Lobinski, and P. J. Dyson, “Reactivity of anticancer metallodrugs with serum proteins: new insights from size exclusion chromatography-ICP-MS and ESI-MS,” Journal of Analytical Atomic Spectrometry, vol. 25, no. 3, pp. 305–313, 2010. View at Publisher · View at Google Scholar · View at Scopus
  181. A. J. Stewart, C. A. Blindauer, S. Berezenko, D. Sleep, and P. J. Sadler, “Interdomain zinc site on human albumin,” Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 7, pp. 3701–3706, 2003. View at Publisher · View at Google Scholar · View at Scopus
  182. C. B. Kissinger and P. T. Kissinger, “Your bioanalytical data are only as good as your samples,” Bioanalysis, vol. 4, no. 12, pp. 1411–1415, 2012. View at Publisher · View at Google Scholar
  183. S. Döker, S. Mounicou, M. Doǧan, and R. Lobinski, “Probing the metal-homeostatis effects of the administration of chromium(vi) to mice by ICP MS and size-exclusion chromatography-ICP MS,” Metallomics, vol. 2, no. 8, pp. 549–555, 2010. View at Publisher · View at Google Scholar · View at Scopus
  184. M. Gonzalez-Fernández, M. A. García-Sevilliano, R. Jara-Biedma et al., “Size characterization of metal species in liver and brain from free-living (Mus spretus) and laboratory (Mus Musculus) mice by SEC-ICP-MS: application to environmental contamination assessment,” Journal of Analytical Atomic Spectrometry, vol. 26, no. 1, pp. 141–149, 2011. View at Publisher · View at Google Scholar
  185. R. Montes-Nieto, C. A. Fuentes-Almagro, D. Bonilla-Valverde et al., “Proteomics in free-living Mus spretus to monitor terrestrial ecosystems,” Proteomics, vol. 7, no. 23, pp. 4376–4387, 2007. View at Publisher · View at Google Scholar · View at Scopus
  186. J. Riuz-Laguna, N. Abril, T. García-Barrera, J. L. Gómez-Ariza, J. López-Barea, and C. Pueyo, “Absolute transcript expression signatures of Cyp and Gst genes in Mus spretus to detect environmental contamination,” Environmental Science & Technology, vol. 40, no. 11, pp. 3646–3652, 2006. View at Publisher · View at Google Scholar
  187. Y. H. Huang, C. M. Shih, C. J. Huang et al., “Effects of cadmium on structure and enzymatic activity of Cu, Zn-SOD and oxidative status in neural cells,” Journal of Cellular Biochemistry, vol. 98, no. 3, pp. 577–589, 2006. View at Publisher · View at Google Scholar · View at Scopus
  188. L. E. Scott and C. Orvig, “Medicinal inorganic chemistry approaches to passivation and removal of aberrant metal ions in disease,” Chemical Reviews, vol. 109, no. 10, pp. 4885–4910, 2009. View at Publisher · View at Google Scholar · View at Scopus
  189. W. B. Cannon, “Organization for physiological homeostasis,” Physiological Reviews, vol. 9, no. 3, pp. 399–431, 1929.
  190. W. J. Crinnion and J. Q. Tran, “Organic foods contain higher levels of certain nutrients, lower levels of pesticides, and may provide health benefits for the consumer,” Alternative Medicine Review, vol. 15, pp. 303–310, 2010.
  191. L. Charlet, Y. Chapron, P. Faller, R. Kirsch, A. T. Stone, and P. C. Baveye, “Neurodegenerative diseases and exposure to the environmental metals Mn, Pb, and Hg,” Coordination Chemistry Reviews, vol. 256, no. 19-20, pp. 2147–2163, 2012. View at Publisher · View at Google Scholar
  192. G. N. George, R. C. Prince, J. Gailer et al., “Mercury binding to the chelation therapy agents DMSA and DMPS and the rational design of custom chelators for mercury,” Chemical Research in Toxicology, vol. 17, no. 8, pp. 999–1006, 2004. View at Publisher · View at Google Scholar · View at Scopus
  193. J. W. Scannell, A. Blanckley, H. Boldon, and B. Warrington, “Diagnosing the decline in pharmaceutical R&D efficiency,” Nature Reviews Drug Discovery, vol. 11, pp. 191–200, 2012. View at Publisher · View at Google Scholar
  194. D. Malakoff, “Can treatment costs be tamed?” Science, vol. 331, no. 6024, pp. 1545–1547, 2011. View at Publisher · View at Google Scholar · View at Scopus
  195. S. Castellino, “MALDI imaging MS analysis of drug distribution in tissue: the right time!(?),” Bioanalysis, vol. 4, no. 21, pp. 2549–2551, 2012. View at Publisher · View at Google Scholar
  196. S. Tuncel, F. Dumoulin, J. Gailer et al., “A set of highly water-soluble tetraethyleneglycol-substituted Zn(II) phthalocyanines: synthesis, photochemical and photophysical properties, interaction with plasma proteins and in vitro phototoxicity,” Dalton Transactions, vol. 40, no. 16, pp. 4067–4079, 2011. View at Publisher · View at Google Scholar · View at Scopus
  197. J. Moretto, B. Chauffert, F. Ghiringhelli, J. R. Aldrich-Wright, and F. Bouyer, “Discrepancy between in vitro and in vivo antitumor effect of a new platinum(II) metallointercalator,” Investigational New Drugs, vol. 29, no. 6, pp. 1164–1176, 2011. View at Publisher · View at Google Scholar
  198. J. Szpunar, A. Makarov, T. Pieper, B. K. Keppler, and R. Lobinski, “Investigation of metallodrug-protein interactions by size-exclusion chromatography coupled with inductively coupled plasma mass spectrometry (ICP-MS),” Analytica Chimica Acta, vol. 387, no. 2, pp. 135–144, 1999. View at Publisher · View at Google Scholar
  199. R. Mandal, R. Kalke, and X. F. Li, “Interaction of oxaliplatin, cisplatin, and carboplatin with hemoglobin and the resulting release of a heme group,” Chemical Research in Toxicology, vol. 17, no. 10, pp. 1391–1397, 2004. View at Publisher · View at Google Scholar
  200. R. Baliga, Z. Zhang, M. Baliga, N. Ueda, and S. V. Shah, “In vitro and in vivo evidence suggesting a role for iron in cisplatin-induced nephrotoxicity,” Kidney International, vol. 53, no. 2, pp. 394–401, 1998. View at Publisher · View at Google Scholar · View at Scopus
  201. V. Calderone, A. Casini, S. Mangani, L. Messori, and P. L. Orioli, “Structural investigation of cisplatin-protein interactions: selective platination of His19 in a cuprozinc superoxide dismutase,” Angewandte Chemie, vol. 45, no. 8, pp. 1267–1269, 2006. View at Publisher · View at Google Scholar · View at Scopus
  202. X. Sun, C. N. Tsang, and H. Sun, “Identification and characterization of metallodrug binding proteins by (metallo) proteomics,” Metallomics, vol. 1, no. 1, pp. 25–31, 2009. View at Publisher · View at Google Scholar · View at Scopus
  203. K. L. Pei and J. Gailer, “Probing the interaction of arsenobetaine with blood plasma constituents in vitro: an SEC-ICP-AES study,” Metallomics, vol. 1, no. 5, pp. 403–408, 2009. View at Publisher · View at Google Scholar · View at Scopus
  204. D. A. Smith, L. Di, and E. H. Kerns, “The effect of plasma protein binding on in vivo efficacy: misconceptions in drug discovery,” Nature Reviews Drug Discovery, vol. 9, pp. 929–939, 2010. View at Publisher · View at Google Scholar
  205. M. Kirberger and J. J. Yang, “Structural differences between Pb2+- and Ca2+-binding sites in proteins: implications with respect to toxicity,” Journal of Inorganic Biochemistry, vol. 102, no. 10, pp. 1901–1909, 2008. View at Publisher · View at Google Scholar
  206. J. M. Swanson, S. Entringer, C. Buss, and P. D. Wadhwa, “Developmental origins of health and disease: environmental exposures,” Seminars in Reproductive Medicine, vol. 27, no. 5, pp. 391–402, 2009. View at Publisher · View at Google Scholar · View at Scopus
  207. L. Trasande, P. J. Landrigan, and C. Schechter, “Public health and economic consequences of methyl mercury toxicity to the developing brain,” Environmental Health Perspectives, vol. 113, no. 5, pp. 590–596, 2005. View at Publisher · View at Google Scholar · View at Scopus
  208. L. D. Hylander and M. E. Goodsite, “Environmental costs of mercury pollution,” Science of the Total Environment, vol. 368, no. 1, pp. 352–370, 2006. View at Publisher · View at Google Scholar · View at Scopus
  209. J. J. Wirth and R. S. Mijal, “Adverse effects of low level heavy metal exposure on male reproductive function,” Systems Biology in Reproductive Medicine, vol. 56, no. 2, pp. 147–167, 2010. View at Publisher · View at Google Scholar
  210. L. Jarup, “Hazards of heavy metal contamination,” British Medical Bulletin, vol. 68, no. 1, pp. 167–182, 2003. View at Publisher · View at Google Scholar
  211. B. H. Robinson, “E-waste: an assessment of global production and environmental impacts,” Science of the Total Environment, vol. 408, no. 2, pp. 183–191, 2009. View at Publisher · View at Google Scholar · View at Scopus
  212. G. Zheng, X. Xu, K. Wu, T. A. Yekeen, and X. Huo, “Association between lung function in school children and exposure to three transition metals from an e-waste recycling area,” Journal of Exposure Science and Environmental Epidemiology, vol. 23, pp. 67–72, 2013. View at Publisher · View at Google Scholar
  213. S.-R. Lim, D. Kang, O. A. Ogunseitan, and J. M. Schoenung, “Potential environmental impacts from the metals in incandescent, compact fluorescent lamp (CFL), and light-emitting diode (LED) bulbs,” Environmental Science and Technology, vol. 47, no. 2, pp. 1040–1047, 2013.
  214. Y. Liu, C. Wen, and X. Liu, “China’s food security soiled by contamination,” Science, vol. 339, pp. 1382–1383, 2013.