Thiosulfoxide (Sulfane) sulfur: New chemistry and new regulatory roles in biology

Molecules

Volumn 19, Issue 8, 2014, Pages 12789-12813

  Toohey, John I ^a   Cooper, Arthur J L ^b  

^a Cytoregulation Research   (Canada)

^b NEW YORK MEDICAL COLLEGE   (United States)

Author keywords

Cystamine; Cystathionine lyase ( cystathionase); Garlic; Glutathione persulfide; Hydrogen sulfide; Mercaptoethanol; Perseleno selenium; Persulfide; Sulfane sulfur; Thioglycerol

Indexed keywords

ANTIOXIDANT; SULFOXIDE;

ANIMAL; BIOSYNTHESIS; CHEMISTRY; HUMAN; METABOLISM; OXIDATION REDUCTION REACTION;

ANIMALS; ANTIOXIDANTS; BIOSYNTHETIC PATHWAYS; HUMANS; OXIDATION-REDUCTION; SULFOXIDES;

EID: 84906657542     PISSN: None     EISSN: 14203049     Source Type: Journal    
DOI: 10.3390/molecules190812789     Document Type: Review

References (126)

1. Kutney, G.W.; Turnbull, K. Compounds containing the S=S bond. Chem. Rev. 1982, 82, 333-357.
2. Noury, S.; Silvi, B: Gillespie, R.J. Chemical bonding in hypervalent molecules: Is the octet rule relevant? Inorg. Chem. 2002, 41, 2164-2172.
3. Nishimoto, A.; Yang, D.Y. Hypervalency in sulfur? Ab initio and DFT studies of the structures of thiosulfate and related sulfur oxyanions. Sulfur Lett. 2003, 26, 171-180.
4. 4. Inorg. Chem. 2012, 51, 8607-8616.
5. 2. J. Chem. Soc. Dalton Trans. 1991, 2395-2398.
6. 2SS, and the related transition states. J. Am. Chem. Soc. 1997, 119, 1990-1996.
7. Roos, G.; Messens, J. Protein sulfenic acid formation: From cellular damage to redox regulation. Free Radic. Biol. Med. 2011, 51, 314-326.
8. Laxman, S.; Sutter, B.M.; Wu, X.; Kumar, S.; Guo, X.; Trudgian, D.C.; Mirzaei, H.; Tu, B.P. Sulfur amino acids regulate translational capacity and metabolic homeostasis through modulation of tRNA thiolation. Cell 2013, 154, 416-429.
9. Mendel, R.R. The molybdenum cofactor. J. Biol. Chem. 2013, 288, 13165-13172.
10. L'vov, N.P.; Nosikov, A.N.; Antipov, A.N. Tungsten-containing enzymes. Biochemistry (Mosc.) 2002, 67, 196-200.
11. Fanger, M.W.; Hart, D.A.; Wells, J.V.; Nisonoff, A. Enhancement by reducing agents of the transformation of human and rabbit peripheral lymphocytes. J. Immunol. 1970, 105, 1043-1045.
12. Click, R.E.; Benck, L.; Alter, B.J. Enhancement of antibody synthesis in vitro by mercaptoethanol. Cell. Immunol. 1972, 3, 156-160.
13. Heber-Katz, E.; Click, R.E. Immune responses in vitro. Role of mercaptoethanol in the mixed leukocyte reaction. Cell. Immunol. 1972, 5, 410-418.
14. Goodman, M.G.; Weigle, W.O. Nonspecific activation of murine lymphocytes. 1. Proliferation and polyclonal activation induced by 2-mercaptoethanol and α-thioglycerol. J. Exp. Med. 1977, 145, 473-488.
15. Broome, J.D.; Jeng, M.W. Promotion of replication in lymphoid cells by specific thiols and disulfides. J. Exp. Med. 1973, 138, 574-592.
16. Toohey, J.I. Sulfhydryl dependence in primary explant hematopoietic cells; inhibition of growth in vitro with vitamin B12 compounds. Proc. Nat. Acad. Sci. USA 1975, 72, 73-77.
17. Toohey, J.I. Persulfide sulfur is a growth factor for cells defective in sulfur metabolism. Biochem. Cell Biol. 1986, 64, 758-765.
18. Toohey, J.I. Macrophages and methylthio groups in lymphocyte proliferation. J. Supramol. Struct. 1981, 17, 11-25.
19. Costa, M.T.; Wolf, A.M.; Giarnieri, D. Cleavage of cystine by cystathionase. Enzymologia 1972, 43, 271-279.
20. Cavallini, D.; de Marco, C.; Mondovi, B. Cleavage of cystine by a pyridoxal model. Arch. Biochem. Biophys. 1960, 87, 281-287.
21. Cooper, A.J.L.; Pinto, J.T. Aminotransferase, L-amino acid oxidase and β-lyase reactions involving L-cysteine S-conjugates found in allium extracts: Relevance to biological activity? Biochem. Pharmacol. 2005, 69, 209-220.
22. Cooper, A.J.L.; Pinto, J.T. Cysteine S-conjugate β-lyases. Amino Acids 2006, 30, 1-15.
23. De Marco, C.; Coletta, M.; Mondovi, B. Transulfuration reactions coupled to enzymic oxidation of cystamine. Ital. J. Biochem. 1960, 9, 77-84.
24. Roy, A.B.; Trudinger, P.A. The Biochemistry of Inorganic Compounds of Sulphur; Cambridge University Press: Cambridge, UK, 1970; pp. 20-34.
25. Toohey, J.I. Methylthioadenosine nucleoside phosphorylase deficiency in methylthio-dependent murine cells. Biochem. Biophys. Res. Commun. 1978, 83, 27-35.
26. Livingston, D.M.; Fergson, C.; Gollogly, R.; Lazarus, H. Accumulation of cystine auxotrophic thymocytes accompanying type C viral leukemogenesis in the mouse. Cell 1976, 7, 41-47.
27. Bertino, J.R.; Waud, W.R.; Parker, W.B.; Lubin, M. Targeting tumors that lack methythioadenosine phosphorylase (MTAP) activity. Current strategies. Cancer Biol. Ther. 2011, 11, 1-6.
28. Della Ragione, F.; Oliva, A.; Palumbo, R.; Russo, G.; Gragnaniello, V.; Zappia, V. Deficiency of 5'-deoxy-5'-methylthioadenosine phosphorylase activity in malignancy; Absence of the protein in human enzyme-deficient cell lines. Biochem. J. 1992, 281, 533-538.
29. Click, R.E. A Review: Alteration of in vitro reproduction processes by thiols - Emphasis on 2-mercaptoethanol. J. Reprod. Dev. 2014, doi:10.1262/jrd.2014-055.
30. Okada, M.; Oka, M.; Yoneda, Y. Effective culture conditions for the induction of pluripotent stem cells. Biochim. Biophys. Acta 2010, 1800, 956-963.
31. Click, R.E. Review: 2-mercaptoethanol alteration of in vitro immune functions of species other than murine. J. Immunol. Methods 2014, 402, 1-8.
32. Toohey, J.I. Sulfur metabolism in AIDS: Cystamine as an anti-HIV agent. AIDS Res. Hum. Retrov. 2009, 25, 1057-1060.
33. Bergamini, A.; Capozzi, M.; Ghibelli, L.; Dini, L.; Salanitro, A.; Milanese, G.; Wagner, T.; Beninati, S.; Pesce, C.D.; Amici, C.; et al. Cystamine potently suppresses in vitro HIV replication in acutely and chronically infected human cells. J. Clin. Investig. 1994, 93, 2251-2257.
34. Ho, W.; Zhu, X.; Song, L.; Lee, H.; Cutilli, J.R.; Douglas, S.D. Cystamine inhibits HIV type I replication in cells of macrocyte/macrophage and T cell lineages. AIDS Res. Hum. Retrov. 1995, 11, 451-459.
35. Gibrat, C.; Cicchetti, F. Potential of cystamine and cysteamine in the treatment of neurodegenerative diseases. Prog. Neuropsychopharmacol. Biol. Psychiatry 2011, 35, 380-389.
36. Wasserman, T.H.; Brizel, D.M. The role of amifostine as a radioprotector. Oncology (Williston Park) 2001, 15, 1349-1354.
37. Murley, J.S.; Kataoka, Y.; Baker, K.L.; Diamond, A.M.; Morgan, W.F.; Grdina, D.J. Manganese superoxide dismutase (SOD2)-mediated delayed radioprotection induced by the free thiol form of amifostine and tumor necrosis factor α. Radiat. Res. 2007, 167, 465-474.
38. Click, R.E. Obesity, longevity, quality of life: Alteration by dietary 2-mercaptoethanol. Virulence 2010, 1, 509-515.
39. Heidrick, M.; Hendricks, L.C.; Cook, D.E. Effect of dietary 2-mercaptoethanol on the life span, immune system, tumor incidence and lipid peroxidation damage in spleen lymphocytes of ageing BC3F1 mice. Mech. Ageing Dev. 1984, 31, 341-356.
40. Click, R.E. Dietary supplemented 2-mercaptoethanol prevents spontaneous and delays virally-induced murine mammary tumorigenesis. Cancer Biol. Ther. 2013, 14, 521-526.
41. Harman, D. Prolongation of the normal lifespan and inhibition of spontaneous cancer by antioxidants. J. Gerontol. 1961, 16, 247-254.
42. Toohey, J.I. Sulphane sulphur in biological systems: A possible regulatory role. Biochem. J. 1989, 264, 625-632.
43. Mueller, E.G. Trafficking in persulfides: Delivering sulfur in biosynthetic pathways. Nat. Chem. Biol. 2006, 2, 185-194.
44. Kessler, D. Enzymatic activation of sulfur for incorporation into biomolecules in prokaryotes. FEMS Microbiol. Rev. 2006, 30, 825-840.
45. Bayan, L.; Koulivand, P.H.; Gorji, A. Garlic: A review of potential therapeutic effects. Avicenna J. Phytomed. 2014, 4, 1-14.
46. Cerella, C.; Dicato, M.; Jacob, C.; Diederich, M. Chemical properties and mechanisms determining the anti-cancer action of garlic-derived organic sulfur compounds. Anticancer Agents Med. Chem. 2011, 11, 267-271.
47. Thomson, M.; Ali, M. Garlic [Allium sativum]: A Review of its potential use as an anti-cancer agent. Curr. Cancer Drug Targets 2003, 3, 67-81.
48. Ray, B.; Chauhan, N.B.; Lahiri, D.K. The "aged garlic extract:" (AGE) and one of its active ingredients S-allyl-L-cysteine (SAC) as potential preventive and therapeutic agents for Alzheimer's disease. Curr. Med. Chem. 2011, 18, 3306-3313.
49. Padiya, R.; Banerjee, S.K. Garlic as an anti-diabetic agent: Recent progress and patent reviews. Recent Pat. Food Nutr. Agric. 2013, 5, 105-127.
50. Ried, K.; Toben, C.; Fakler, P. Effect of garlic on serum lipids: An updated meta-analysis. Nutr. Rev. 2013, 71, 282-299.
51. Borek, C. Garlic reduces dementia and heart-disease risk. J. Nutr. 2006, 136, S810-S812.
52. Amagase, H. Clarifying the real bioactive constituents of garlic. J. Nutr. 2006, 136, S716-S725.
53. Li, L.; Sun, T.; Tian, J.; Yang, K.; Yi, K.; Zhang, P. Garlic in clinical practice: An evidence-based overview. Crit. Rev. Food Sci. Nutr. 2013, 53, 670-681.
54. Martelli, A.; Testai, L.; Breschi, M.C.; Blandizzi, C.; Virdis, A.; Taddei, S.; Calderone, V. Hydrogen sulphide: Novel opportunity for drug discovery. Med. Res. Rev. 2012, 32, 1093-1130.
55. 2S. Chem. Res. Toxicol. 2012, 25, 1609-1615.
56. Toohey, J.I. Sulfur signaling; is the agent sulfide or sulfane? Anal. Biochem. 2011, 413, 1-7.
57. 2S to protein thiol oxidation. Antioxid. Redox. Signal. 2013, 19, 1749-1765.
58. Ida, T.; Sawa, T.; Ihara, H.; Tsuchiya, Y.; Watanabe, Y.; Kugamai, Y.; Suematsu, M.; Motohashi, H.; Fujii, S.; Matsunaga, T.; et al. Reactive cysteine persulfides and S-polythiolation regulate oxidative stress and redox signaling. Proc. Natl. Acad. Sci. USA 2014, 111, 7606-7611.
59. 2-dependent manner. Am. J. Heart Circ. Physiol. 2007, 292, H1963-H1960.
60. Olson, K.R.; Forgan, L.G.; Dombkowski, R.A.; Forster, M.E. Oxygen dependency of hydrogen sulfide-mediated vasoconstriction in cyclostome aortas. J. Exp. Biol. 2008, 211, 2205-2213.
61. 2S signaling through protein sulfhydration and beyond. Nat. Rev. Mol. Cell Biol. 2012, 13, 499-507.
62. 2S to sulfane sulfur. Nat. Rev. Mol. Cell Biol. 2013, 13, 803.
63. Sparatore, A.; Santus, G.; Giustarini, D.; Rossi, R.; del Soldato, P. Therapeutic potential of new hydrogen sulfide-releasing hybrids. Expert Rev. Clin. Pharmacol. 2011, 4, 109-121.
64. Cava, M.P.; Levinson, M.I. Thionation reactions of Lawesson's reagents. Tetrahedron 1985, 41, 5061-5087.
65. Zhang Y.; Munday, M. Dithiolethiones for cancer chemoprevention: Where do we stand? Mol. Cancer Ther. 2008, 7, 3470-3479.
66. Kimura, Y.; Mikami, Y.; Osumi, K.; Tsugane, M.; Oka, J.; Kimura, H. Polysulfides are possible H2S-derived signaling molecules in rat brain. FASEB J. 2013, 27, 2451-2457.
67. Höfle, G.; Baldwin, J.E. Thiosufoxides. The intermediates in rearrangement and reduction of allylic disulfides. J. Am. Chem. Soc. 1971, 93, 6307-6308.
68. Meister, A.; Fraser, P.; Tice, S.V. Enzymatic desulfuration of β-mercaptopyruvate to pyruvate. J. Biol. Chem. 1954, 206, 561-575.
69. Kearney, E.B.; Singer, T.P. Enzymic transformation of L-cysteinesulfinic acid. Biochim. Biophys. Acta 1953, 11, 276-283.
70. Nicolet, B.H. The mechanism of sulfur lability in cysteine and its derivatives. Some thioethers readily split by alkali. J. Am. Chem. Soc. 1931, 53, 3066-3072.
71. Hofmann, K.; Bucher, P.; Kajava, A.V. A model of Cdc25 phosphatase catalytic domain and Cdk-interaction surface based on the presence of a rhodanese homology domain. J. Mol. Biol. 1998, 282, 195-208.
72. Yamanishi, T.; Tuboi, S. The mechanism of the L-cystine cleavage reaction catalyzed by rat liver β-cystathionase. J. Biochem. 1981, 89, 1913-1921.
73. Jarabak, R.; Westley, J. Serum albumin and cyanide detoxication. Kinetic characterization of a reactive albumin-sulfur complex. J. Biol. Chem. 1986, 261, 10793-10796.
74. Cipollone, R.; Acsenzi, P.; Visca, P. Common themes and variations in the rhodanese superfamily. IUBMB Life 2007, 59, 51-59.
75. Bordo, D.; Bork, P. The rhodanese/Cdc25 phosphatase superfamily. Sequence-structure-function relations. EMBO Rep. 2002, 3, 741-746.
76. You, Z.; Cao, X.; Taylor, A.B.; Hart P.J.; Levine, R.L. Characterization of a covalent polysulfane bridge in Cu-Zn superoxide dismutase. Biochemistry 2010, 49, 1191-1198.
77. Nielsen, R.W.; Tachibana, C.; Hansen, N.E.; Winther, J.R. Trisulfides in proteins. Antiox. Redox. Signal. 2011, 15, 67-75.
78. Gu, S.; Wen, D.; Weinreb, P.H.; Sun, Y.; Zhang, L.; Foley, S.F.; Kshirsagar, R.; Evans, D.; Mi, S.; Meier, W.; et al. Characterization of trisulfide modifications in antibodies. Anal. Biochem. 2010, 400, 89-98.
79. Knowles, L.M.; Milner, J.A. Diallyl disulfide inhibits p34(Cdc2) kinase activity through changes in complex formation and phosphorylation. Carcinogenesis 2000, 21, 1129-1134.
80. Krishnan, N.; Fu, C.; Pappin, D.; Tonks, N.K. H2S-induced sulfhydration of PTP1B and its role in the endoplasmic reticulum stress response. Sci. Signal. 2011, 4, ra86.
81. Chen, S.S.; Walgate, J.H.; Duerre, J.A. Oxidative deamination of sulfur amino acids by bacterial and snake venom L-amino acid oxidase. Arch. Biochem. Biophys. 1971, 146, 54-63.
82. Cooper, A.J.L.; Meister, A. Enzymatic oxidation of L-homocysteine. Arch. Biochem. Biophys. 1985, 239, 556-566.
83. Zheng, L.; White, R.H.; Cash, V.L.; Dean, D.R. Mechanism for the desulfuration of L-cysteine by the nifS gene product. Biochemistry 1994, 33, 4714-4720.
84. Marelja, Z.; Mullick Chowdhury, M.; Dosche, C.; Hille, C.; Baumann, O.; Löhmannsröben, H.G.; Leimkuhler, S. The L-cysteine desulfurase NFS1 is localized in the cytosol where it provides the sulfur for molybdenum cofactor biosynthesis in humans. PLoS One 2013, 8, e60869.
85. Hidese, R.; Mihara, H.; Esaki, N. Bacterial cysteine desulfurases; versatile key players in biosynthetic pathways of sulfur-containing biofactors. Appl. Microbiol. Biotechnol. 2011, 91, 47-61.
86. Cooper, A.J.L.; Krasnikov, B.F.; Niatsetskaya, Z.V.; Pinto, J.T.; Callery, P.S.; Villar, M.T.; Artigues, A.; Bruschi, S.A. Cysteine S-conjugate β-lyases: Important roles in the metabolism of naturally occurring sulfur and selenium-containing compounds, xenobiotics and anticancer agents. Amino Acids 2011, 41, 7-27.
87. Buckberry, L.D.; Patel, R.; Hollingworth, L.; Teesdale-Spittle, P.H. Cysteine conjugate β-lyase activity of amino acid decarboxylases. Biochem. Soc. Trans. 1998, 26, S269.
88. Blom, HJ.; Boers, G.H.J.; van den Elzen, J.P.; Gahl, W.A.; Tangerman, A. Transamination of methionine in humans. Clin. Sci. 1989, 76, 43-49.
89. Tomisawa, H.; Ichimoto, N.; Ichihara, S.; Fukazawa, H. Involvement of cystathionase in the formation of alkane-thiols from corresponding cysteine conjugates. Xenobiotica 1988, 18, 1029-1037.
90. Wróbel, M.; Ubuka, T.; Yao, W.B.; Abe, T. L-Cysteine metabolism in guinea pig and rat tissues. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 1997, 116, 223-226.
91. Nagahara, N.; Sawada, N. The mercaptopyruvate pathway in cysteine catabolism: A physiologic role and related disease of the multifunctional 3-mercaptopyruvate sulfurtransferase. Curr. Med. Chem. 2006, 13, 1219-1230.
92. Devalier-Klutchko, C.; Flavin, M. Role of Bacterial cystathionine β-cleavage enzyme in disulfide decomposition. Biochim. Biophys. Acta 1965, 99, 371-375.
93. Flavin, M.; Slaughter, C. β-Cystathionase (Neurospora). Methods Enzymol. 1962, 5, 433-439.
94. Malloy, M.H.; Rassin, D.K.; Gaull, G.E. Plasma cyst(e)ine in homocyst(e)inemia. Am. J. Clin. Nutr. 1981, 34, 2619-2621.
95. Wilcken, D.E.L.; Gupta, V.J. Cysteine-homocysteine mixed disulphide: Differing plasma concentrations in normal men and women. Clin. Sci. 1979, 57, 211-215.
96. Schneider, J.A.; Bradley, K.H.; and Seegmiller, J.E. Identification and measurement of cysteine-homocysteine mixed disulfide in plasma. J. Lab. Clin. Med. 1968, 71, 122-125.
97. Wróbel, M.; Lewandowska, I.; Bronowicka-Adamska, P.; Paszewski, A. The level of sulfane sulfur in the fungus Aspergillus nidulans wild type and mutant strains. Amino Acids 2009, 37, 565-571.
98. Toohey, J.I. Vitamin B12 and methionine synthesis: A critical review: Is nature's most beautiful cofactor misunderstood? Biofactors 2006, 26, 45-57.
99. Thomas, T.; Thomas, T.J. Polyamines in cell growth and cell death: Molecular mechanisms and therapeutic applications. Cell. Mol. Life Sci. 2001, 58, 244-258.
100. Gaull, G.; Sturman, J.A.; Räihä, N.C. Development of mammalian sulfur metabolism: Absence of cystathionase in human fetal tissues. Pediatr. Res. 1972, 6, 538-547.
101. Levonin, A.; Lapatto, R.; Saksela, M.; Raivio, K.O. Human cystathionine β-lyase: Developmental and in vitro expression of two isoforms. Biochem. J. 2000, 347, 291-295.
102. Colín-González, A.L.; Santana, R.A.; Silva-Islas, C.A.; Chánez-Cárdenas, M.E.; Santamaría, A.; Maldonado, P.D. The antioxidant mechanisms underlying the aged garlic extract- and S-allylcysteine-induced protection. Oxid. Med. Cell. Longev. 2012, 2012, 907162.
103. Sun, W.H.; Liu, F.; Chen, Y.; Zhu, Y.C. Hydrogen sulfide decreases the levels of ROS by inhibiting mitochondrial complex IV and increasing SOD Activities in cardiomyocytes under ischemia/reperfusion. Biochem. Biophys. Res. Commun. 2012, 421, 164-169.
104. Iciek, M.; Kwiecień, I.; Chwatko, G.; Sokołowska- Jeżewicz, M.; Kowalczyk-Pachel, D.; Rokita, H. The effects of garlic-derived sulfur compounds on cell proliferation, caspase 3 activity, thiol levels and anaerobic sulfur metabolism in human hepatoblastoma HepG2 cells. Cell. Biochem. Funct. 2012, 30, 198-204.
105. Fontecave, M.; Iron-sulfur clusters: Ever-expanding roles. Nat. Chem. Biol. 2006, 2, 171-174.
106. Frey, P.A.; Hegeman, A.D.; Ruzicka, F.J. The radical SAM superfamily. Crit. Rev. Biochem. Mol. Biol. 2008, 43, 63-68.
107. Hänzelmann, P.; Schindelin, H. Crystal structure of the S-adenosylmethionine-dependent enzyme MoaA and its implications for molybdenum cofactor deficiency in humans. Proc. Nat. Acad. Sci. USA 2004, 101, 12870-12875.
108. 0-containing impurities in commercial samples of oxidized glutathione and their catalytic effect in the reduction of cytochrome c. Biochem. Biophys. Res. Commun. 1971, 42, 730-738.
109. Prütz, W.A. Reduction of resazurin by glutathione activated by sulfanes and selenite. J. Chem. Soc. 1994, 14, 1639-1640.
110. Bloem, E.; Haneklaus, S.; Schnug, E. Significance of sulfur compounds in the protection of plants against pests and diseases. J. Plant Nutr. 2005, 28, 763-784.
111. Cooper, R.M.; Williams, J.S. Elemental sulphur as an induced antifungal substance in plant defense. J. Exp. Bot. 2004, 55, 1947-1953.
112. Nwachukwu, I.D.; Slusarenko, A.J.; Gruhlke, M.C. Sulfur and sulfur compounds in plant defense. Nat. Prod. Commun. 2012, 7, 395-400.
113. Fairweather-Tait, S.J.; Bao, Y.; Broadley, M.R.; Collings, R.; Ford, D.; Hesketh, J.E.; Hurst, R. Selenium in health and disease. Antioxid. Redox Signal. 2011, 14, 1338-1367.
114. Stadtman, T.C. Selenoproteins - Tracing the role of a trace element in protein function. PLoS Biol. 2005, 3, e421.
115. Ganther, H.E. Selenotrisulfides. Formation by the reaction of thiols with selenious acid. Biochemsitry 1968, 7, 2898-2905.
116. Ogasawara, Y.; Lacourciere, G.; Stadtman, T.C. Formation of a selenium-substituted rhodanese by reaction with selenite and glutathione: Possible role of a protein pereselenide in a selenium delivery system. Proc. Nat. Acad. Sci. USA 2001, 98, 9494-9498.
117. Burk, R.F.; Hill, K.E.; Motley, A.K. Selenoprotein metabolism and function: Evidence for more than one function for selenoprotein P. J. Nutr. 2003, 133, 1517S-1520S.
118. MacFarquhar, J.K.; Broussard, D.L.; Melstrom, P.; Hutchinson, R.; Wolkin, A.; Martin, C.; Burk, R.F.; Dunn, J.R.; Green, A.L.; Hammond, R.; et al. Acute selenium toxicity associated with a dietary supplement. Arch. Intern. Med. 2010, 170, 256-261.
119. Aldosary, B.M.; Sutter, M.E.; Schwartz, M.; Morgan, B.W. Case series of selenium toxicity from a nutritional supplement. Clin. Toxicol. 2012, 50, 57-64.
120. Yang, G.Q.; Wang, S.Z.; Zhou, R.H.; Sun, S.Z. Endemic seleniun intoxication of humans in china. Am. J. Clin. Nutr. 1983, 37, 872-881.
121. Desta, B.; Maldonado, G.; Reid, H.; Puschner, B.; Maxwell, J.; Agasan, A.; Humphreys, L.; Holt, T. Acute selenium toxicosis in polo ponies. J. Vet. Diagn. Investig. 2011, 23, 623-628.
122. Brozmanová, J.; Mániková, D.; Vlčková, V.; Chovanec, M. Selenium: A double-edged sword for defense and offence in cancer. Arch. Toxicol. 2010, 84, 919-938.
123. Song, G.; Zhang, Z.; Wen, L.; Chen, C.; Shi, Q.; Zhang, Y.; Ni, J.; Liu, Q. Selenomethionine ameliorates cognitive decline, reduces tau hyperphosphorylation, and reverses synaptic deficit in the triple transgenic mouse model of Alzheimer's disease. J. Alzheimer's Dis. 2014, 41, 85-99.
124. Bellinger, F.P.; He, Q.P.; Bellinger, M.T.; Lin, Y.; Raman, A.V.; White, L.R.; Berry, M.J. Association of selenoprotein P with Alzheimer's pathology in human cortex. J. Alzheimer's Dis. 2008, 15, 465-472.
125. Levander, O.A.; Moris, V.C.; Higgs, D.J. Selenium as a catalyst for the reduction of cytochrome c by glutathione. Biochemistry 1973, 12, 4591-4595.
126. Rhead, W.J.; Schrauzer, G.N. The selenium catalyzed reduction of methylene blue by thiols. Bioinorg. Chem. 1974, 3, 225-242.