Role of thiocyanate ion in metallothionein induction and in endogenous distribution of essential elements in the rat liver

Biological Trace Element Research

Volumn 90, Issue 1-3, 2002, Pages 187-202

  Aydin, H Hakan ^a   Çelik, Handan Ak ^a   Ersoz, Biltan ^a  

^a EGE UNIVERSITY SCHOOL OF MEDICINE   (Turkey)

Author keywords

Calcium; Copper; Iron; Magnesium; Manganese; Metallothionein; Thiocyanate; Zinc

Indexed keywords

CALCIUM; COPPER; CYANIDE; HYDROGEN CYANIDE; IRON; MAGNESIUM; MANGANESE; METAL; METALLOTHIONEIN; THIOCYANATE; ZINC;

ANIMAL EXPERIMENT; ARTICLE; CELL FUNCTION; CELL METABOLISM; CONTROLLED STUDY; DRUG BLOOD LEVEL; IN VIVO STUDY; LIVER METABOLISM; MALE; MOLECULAR INTERACTION; NONHUMAN; POLLUTION; RAT; SMOKING; TISSUE DISTRIBUTION;

ANIMALS; CALCIUM; COPPER; ENVIRONMENTAL POLLUTANTS; IRON; LIVER; MAGNESIUM; MALE; MANGANESE; METALLOTHIONEIN; RATS; RATS, WISTAR; THIOCYANATES; ZINC;

ANIMALIA;

EID: 0036964905     PISSN: 01634984     EISSN: None     Source Type: Journal    
DOI: 10.1385/BTER:90:1-3:187     Document Type: Article

References (56)

1. A. A. Newman, ed., Chemistry and Biochemistry of Thiocyanic Acid and Its Derivatives, Academic, Orlando, FL (1975).
2. F. S. Apple, M. C. Lowe, M. K. Gookins, and J. Kloss, Serum thiocyanate concentrations in patients with normal and impaired renal function receiving nitroprusside, Clin. Chem. 42, 1878-1879 (1996).
3. J. Tenovuo, Nonimmunoglobulin defense factors in human saliva, in Human Saliva: Clinical Chemistry and Microbiology, Vol. II, J. Tenovuo, ed., CRC, Boca Raton, FL, pp. 55-91 (1989).
4. J. Hovinen, T. Pettersson-Fernholm, M. Lahti, and J. Vilpo, Role of thiocyanate ion in detoxification of the anticancer agent chlorambucil, Chem. Res. Toxicol., 11, 1377-1381 (1998).
5. H. Rosling, Molecular antropology of cassava cyanogenesis, in The Impact of Plant Molecular Genetics, B. W. S. Soral, ed., Oxford University Press, New York, pp. 338-343 (1996).
6. J. Tor-Agbidye, V. S. Palmer, M. R. Laserev, A. M. Craig, L. L. Blythe, M. I. Sabri, et al., Bioactivation of cyanide to cyanate in sulfur amino acid deficiency: relevance to neurological disease in humans subsisting on cassava, Toxicol. Sci. 50, 228-235 (1999).
7. S. Ripa and R. Ripa, Zinc cellular traffic: physiopathological considerations, Minerva Med. 86, 37-43 (1995).
8. J. H. R. Kägi, Overview of metallothionein, in Methods in Enzymology, Riordan, ed., Academic, New York, pp. 613-626 (1991).
9. J. H. R. Kägi, Evolution, structure, and chemical activity of class I metallothioneins: an overview, in Metallothionein III, K. Y. Suzuki, N. Imura, and M. Kimura, eds., Birkhäuser, Basel, pp. 29-55 (1993).
10. H. H. Aydin, C. Coker, B. Ersoz, and G. Mentes, Distribution of zinc and copper in thiocyanate administrated rats, in Metal Ions in Biology and Medicine, P. H. Collery, P. Bratter, V. Negretti Bratter, and L. Khassanova, eds. John Libbey Eurotext, Paris, pp. 223-227 (1998).
11. A. R. Pettigrew and G. S. Fell, Simplified colorimetric determination of thiocyanate in biological fluids, and its application to investigation of the toxic amblyopias, Clin. Chem. 18, 996-1000 (1972).
12. A. M. Scheuhammer and M. G. Cherian, Quantification of metallothioneins by a silver saturation method, Toxicol. Appl. Pharmacol. 82, 417-425 (1986).
13. O. H. Lowry, N. J. Rosebrough, A. L. Farr, and R. J. Randall, Protein measurement with Folin's phenol reagent, J. Biol. Chem. 193, 265-275 (1951).
14. J. Cha, R. L. Makowiec, J. B. Penney, and A. B. Young, Multiple states of rat brain (RS)-alpha-amino-3 hydroxy-5-methylisoxazole-4-propionic acid receptors as revealed by quantative autoradiography, Mol. Pharmacol. 41, 832-838 (1992).
15. P. S. Spencer, Food toxins, AMPA receptors and motor neuron diseases, Drug Metab. Rev. 31, 561-587 (1999).
16. P. G. Furtmüller, U. Burner, G. Regelsberger, and C. Obinger, Spectral and kinetic studies on theformation of eosinophil peroxidase compound I and Its reaction with halides and thiocyanate, Biochemistry 39, 15,578-15,584 (2000).
17. A. Slungaard and J. R. Mahoney, Jr., Thiocyanate is the major substrate for eosinophil peroxidase in physiologic fluids. Implications for cytotoxicity, J. Biol. Chem. 266, 4903-4910 (1991).
18. M. B. Grisham and E. M. Ryan, Cytotoxic properties of salivary oxidants. Am. J. Physiol. 258, C115-C121 (1990).
19. P. G. Furtmuller, U. Burner, and C. Obinger, Reaction of myeloperoxidase compound I with chloride, bromide- iodide and thiocyanate, Biochemistry 37, 17,923-17,930 (1998).
20. J. R. Milligan, J. A. Aguilera, R. A. Paglinawan, and J. F. Ward, Mechanism of DNA damage by thiocyanate radicals, Int. J. Radiat. Biol. 76, 1305-1314 (2000).
21. Y. Katayama and J. H. Widdicombe, Halide transport in Xenopus oocytes, J. Physiol. 443, 587-599 (1991).
22. B. L. Vallee, Introduction to metallothioneins, in Methods in Enzymology, Metallobiochemistry Part B, J. F. Riordan and B. L. Vallee, eds. vol 205 Academic, San Diego, CA, Vol. 205 pp. 3-7 (1991).
23. B. L. Vallae, Implications and inferences of metallothionein structure, Experientia 52(Suppl 5.), 16 (1987).
24. F. O. Brady, Induction of metallothionein in rats, in Methods in Enzymology, Metallobiochemistry, Part B, J. F. Riordan and B. L. Vallee, eds., Academic, San Diego, CA, Vol. 205, pp 559-566 (1991).
25. K. T. Tamai, E. B. Gralla, L. M. Ellerby, J. S. Valentine, and D. J. Thiele, Yeast and mammalian metallothioneins functionally substitute for yeast copper-zinc superoxide dismutase, Proc. Natl. Acad. Sci. USA 90, 8013-8017 (1993).
26. S. K. De, M. T. McMaster, and G. K. Andrews, Endotoxin induction of murine metallothionein gene expression, J. Biol. Chem. 265, 15,267-15,274 (1990).
27. K. S. Min, Y. Terano, S. Onosaka, and K. Tanaka, Induction of hepatic metallothionein by nonmetallic compounds associated with acute-phase response in inflammation, Toxicol. Appl. Pharmacol. 111, 152-162 (1991).
28. J. W. Bauman, C. Madhu, J. M. McKim, Jr., Y. Liu, and C. D. Klaassen, Induction of hepatic metallothionein by paraquat, Toxicol. Appl. Pharmacol. 117, 233-241 (1992).
29. T. Dalton, R. D. Palmiter, and G. K. Andrews, Transcriptional induction of the mouse metallothionein-I gene in hydrogen peroxide-treated HEPA cells involves a composite major late transcription factor/antioxidant response element and metal response promoter elements. Nucleic Acids Res. 22, 5016-5023 (1994).
30. M. A. Schwarz, J. S. Lazo, J. C. Yalowich, W. P. Allen, M. Whitmore, H. A. Bergonia, et al. Metallothionein protects against the cytotoxic and DNA-damaging effects of nitric oxide, Proc. Natl. Acad. Sci. USA 92, 4452-4456 (1995).
31. B. L. Vallee and K. F. Falchuk, The biochemical basis of zinc physiology, Physiol. Rev. 73, 79-118 (1993).
32. E. H. Fischer and E. W. Davie, Recent excitement regarding metallothionein, Proc. Natl. Acad. Sci. USA 95, 3333-3334 (1998).
33. V. Kalfakakou and T. J. Simons, Anionic mechanisms of zinc uptake across the human red cell membrane, J. Physiol. 421, 485-497 (1990).
34. L. J. Jiang, W. Maret, and B. L. Vallee, The glutathione redox couple modulates zinc transfer from metallothionein to zinc-depleted sorbitol dehydrogenase, Proc. Natl. Acad. Sci. USA 95, 3483-3488 (1998).
35. C. Jacob, W. Maret, and B. L. Vallee, Control of zinc transfer between thionein, metal-lothionein, and zinc proteins, Proc. Natl. Acad. Sci. USA 95, 3489-3494 (1998).
36. C. Askwith and J. Kaplan, Iron and copper transport in yeast and its relevance to human disease, Trends Biochem. Sci. 23, 135-138 (1998).
37. M. D. Harrison, C. E. Jones, M. Solioz, and C. T. Dameron, Intracellular copper routing: the role of copper chaperons, Trends Biochem. Sci. 25, 29-32 (2000).
38. R. A. Pufahl, C. P. Singer, K. L. Peariso, S. J. Lin, P. J. Schmidt, C. J. Fahrni, et al. Metal ion chaperone function of the soluble Cu (1) receptor Atx1, Science 278, 853-856 (1997).
39. S. J. Lin, R. A. Pufahl, A. Dancis, T. V. O'Halloran, and V. C. Culotta, A role for the Saccharomyces cerevisiae ATX1 gene in copper trafficking and iron transport, J. Biol. Chem. 272, 9215-9220 (1997).
40. D. L. Savigni and E. H. Morgan, Transport mechanisms for iron and other transition metals in rat and rabbit erythoid cells, J. Physiol. 508, 837-850 (1998).
41. D. R. Richardson and P. Ponka, The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells, BBA - Rev. Biomembr. 1331, 1-40 (1997).
42. T. A. Rouault and R. D. Klausner, Iron-sulfur clusters as biosensors of oxidants and iron, Trends Biochem. Sci. 21, 174-177 (1996).
43. M. W. Hentze and L. C. Kühn, Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress, Proc. Natl. Acad. Sci. USA 93, 8175-8182 (1996).
44. J. C. Drapier and C. Bouton, Modulation by nitric oxide of metalloprotein regulatory activities, Bioessays 18, 549-556 (1996).
45. N. H. Gehring, M. W. Hentze, and K. Pantopoulos, Inactivation of both RNA binding and aconitase activities of iron regulatory protein-I by quinone-induced oxidative stress, J. Biol. Chem. 274, 6219-6225 (1999).
46. E. Carafoli, Intracellular calcium homeostasis, Annu. Rev. Biochem. 56, 395-433 (1987).
47. N-E. L. Saris, E. Mervaala, H. Karppanen, J. A. Khawaja, and A. Lewenstam, Magnesium: an update on physiological, clinical and analytical aspect. Clin. Chim. Acta 294, 1-26 (2000).
48. R. D. Grubbs and M. E. Maguire, Magnesium as a regulatory cation: critical evaluation. Magnesium 6, 113-127 (1987).
49. P. N. Flatman, Mechanism of magnesium transport, Annu. Rev. Physiol. 53, 259-271 (1991).
50. N. Nelson, Metal ion transporters and homeostasis, EMBO J. 18, 4361-4371 (1999).
51. 2+ required for glycosylation, sorting and endoplasmic reticulum-associated protein degradation. Mol. Biol. Cell 9, 1149-1162 (1998).
52. K. W. Beyenbach, Transport of magnesium across biological membranes, Magnesium Trace Elements 9, 233-254 (1990).
53. A. Romani and A. Scarpa, Regulation of cell magnesium, Arch. Biochem. Biophy. 298, 1-12 (1992).
54. R. J. P. Williams, The biochemistry of sodium, potassium, magnesium and calcium, Q. Rev. Chem. Soc. 24, 331-365 (1970).
55. F. I. Wolf, A. Di Francesco, V. Covacci, and A. Cittadini, cAMP activates magnesium efflux via the Na/Mg antiporter in ascites cells, Biochem. Biophys. Res. Commun. 202, 1209-1214 (1994).
56. V. A. Murphy, K. C. Washwani, Q. R. Smith, and S. I. Rapaport, Saturable transport of manganase (II) across the rat blood-brain barrier, J. Neurochem. 59, 300-306 (1991).