In vitro uptake of glutamate in GLAST- and GLT-1-transfected mutant CHO-K1 cells is inhibited by the ethylmercury-containing preservative thimerosal

Biological Trace Element Research

Volumn 105, Issue 1-3, 2005, Pages 71-86

  Mutkus, Lysette ^a   Aschner, Judy L ^a   Syversen, Tore ^b   Shanker, Gouri ^a   Sonnewald, Ursula ^b   Aschner, Michael ^a  

^a WAKE FOREST SCHOOL OF MEDICINE   (United States)

^b NORWEGIAN UNIVERSITY OF SCIENCE AND TECHNOLOGY   (Norway)

Author keywords

Chinese hamster ovary (CHO) cells; Ethylmercury; Glutamate transport; Thimerosal

Indexed keywords

ASPARTIC ACID; CARRIER PROTEIN; ETHYLMERCURY DERIVATIVE; GLUTAMATE ASPARTATE TRANSPORTER; GLUTAMIC ACID; GLUTAMIC ACID DERIVATIVE; MESSENGER RNA; PRESERVATIVE; THIOMERSAL; UNCLASSIFIED DRUG; VESICULAR GLUTAMATE TRANSPORTER 1;

ANIMAL CELL; ARTICLE; BIOACCUMULATION; CELL MUTANT; CHO CELL; GENE EXPRESSION; GENETIC TRANSFECTION; NONHUMAN; PROTEIN EXPRESSION;

CRICETULUS GRISEUS;

EID: 22444445508     PISSN: 01634984     EISSN: None     Source Type: Journal    
DOI: 10.1385/bter:105:1-3:071     Document Type: Article

References (49)

1. WHO, Environmental Health Criteria 1, Mercury, International Program on Chemical Safety, World Health Organization. Geneva (1976).
2. Swedish Expert Group, Methylmercury in fish, a toxicological epidemiological evaluation of risks, Nord. Hyg. Tidskr. 4, 19-364 (1971).
3. A. Blair, B. Clark, A. Clarke, and P. Wood, Tissue concentrations of mercury after chronic dosing of squirrel monkeys with Thimerosal, Toxicology 3, 171-176 (1975).
4. L. Magos, A. W. Brown, S. Sparrow, E. Bailey, R. T. Snowden, and W. R. Skipp, The comparative toxicology of ethyl- and methylmercury, Arch. Toxicol. 57, 260-267 (1985).
5. L. K. Ball, R. Ball, and R. D. Pratt, An assessment of thimerosal use in childhood vaccines, Pediatrics 107, 1147-1154 (2001).
6. IOM (Institute of Medicine), Immunization Safety Review: Vaccines and Autism, Board on Health Promotion and Disease Prevention (HPDP), Institute of Medicine (IOM), National Academy Press, Washington, DC. Available at http://www.nap.edu/books/030909237X/htm (accessed 2004).
7. M. Hornig, D. Chian, and W. I. Lipkin, Neurotoxic effects of postnatal thimerosal are mouse strain dependent, Mol. Psychiatry 9, 833-845 (2004).
8. J. G. R. Elferink, Thimerosal. A versatile sulfhydryl reagent, calcium mobilizer, and cell function modulating agent, Gen. Pharmacol. 33, 1-6 (1999).
9. W. H. Hughes, A physiochemical rationale for the biological activity of mercury and its compounds, Ann. NY Acad. Sci. 65, 454-460 (1957).
10. D. R. Curtis, A. W. Duggan, and G. A. Johnston, The inactivation of extracellularly administered amino acids in the feline spinal cord, Exp. Brain Res. 10, 447-462 (1970).
11. E. C. Foulkes, Nature of inhibition of renal aspartate reabsorption in experimental Fanconi syndrome, Toxicol. Appl. Pharmacol. 71, 445-450 (1983).
12. T. W. Clarkson, The biological properties and distribution of mercury, Biochem. J. 130, 61P-63P (1972).
13. 2+ concentration of rat cerebellar neurons, Toxicology 195, 77-84 (2004).
14. T. Storck, S. Schulte, K. Hofmann, and W. Stoffel, Structure, expression, and functional analysis of a Na(+)-dependent glutamate/aspartate transporter from rat brain, Proc. Natl. Acad. Sci. USA 89, 10,955-10,959 (1992).
15. G. Pines, N. C. Danbolt, M. Bjoras, et al., Cloning and expression of a rat brain L-glutamate transporter, Nature 360, 464-467 (1992).
16. Y. Kanai and M. A. Hediger, Primary structure and functional characterization of a high-affinity glutamate transporter, Nature 360, 467-471 (1992).
17. W. A. Fairman and S. G. Amara, Functional diversity of excitatory amino acid transporters: ion channel and transport modes, Am. J. Physiol. 277, F481-F486 (1999).
18. J. L. Arriza, S. Eliasof, M. P. Kavanaugh, and S. G. Amara, Excitatory amino acid transporter 5, a retinal glutamate transporter coupled to a chloride conductance, Proc. Natl. Acad. Sci. USA 94, 4155-1160 (1997).
19. Y. Kanai, Family of neutral and acidic amino acid transporters: molecular biology, physiology and medical implications, Curr. Opin. Cell. Biol. 9, 565-572 (1997).
20. O. Haugeto, K. Ullensvang, L. M. Levy, et al., Brain glutamate transporter proteins from homomultimers, J. Biol. Chem. 271, 27,715-27,722 (1996).
21. N. C. Danbolt, G. Pines, and B. I. Kanner, Purification and reconstitution of the sodium-and potassium-coupled glutamate transport glycoprotein from rat brain, Biochemistry 29, 6734-6740 (1990).
22. K. D. Sims, and M. B. Robinson, Expression patterns and regulation of glutamate transporters in the developing and adult nervous system, Crit. Rev. Neurobiol. 13, 169-197 (1999).
23. K. P. Lehre, L. M. Levy, O. P. Ottersen, J. Storm-Mathisen, and N. C. Danbolt, Differential expression of two glial glutamate transporters in the rat brain: quantitative and immunocytochemical observations, J. Neurosci. 15, 1835-1853 (1995).
24. J. D. Rothstein, L. Martin, A. I. Levey et al., Localization of neuronal and glial glutamate transporters, Neuron 13, 713-725 (1994).
25. R. Torp, D. Lekieffre, L. M. Levy, et al., Reduced postischemic expression of a glial glutamate transporter, GLT1 in the rat hippocampus, Exp. Brain Res. 103, 51-58 (1995).
26. A. E. Fray, P. G. Ince, S. J. Banner, et al., The expression of the glial glutamate transporter protein EAAT2 in motor neuron disease: and immunohistochemical study, Eur. J. Neurosci. 10, 2481-2489 (1998).
27. S. Sasaki, T. Komori, and M. Iwata, Excitatory amino acid transporter 1 and 2 immunoreactivity in the spinal cord in amyotrophic lateral sclerosis, Acta Neuropathol. (Berlin) 100, 138-144 (2000).
28. B. Meldrum and J. Garthwaite, Excitatory amino acid neurotoxicity and neurodegenerative disease, Trends Pharmacol. Sci. 11, 379-387 (1990).
29. M. Aschner, N. B. Eberle, K. Miller, and H. K. Kimelberg, Interactions of methylmercury with rat primary astrocyte cultures: inhibition of rubidium and glutamate uptake and induction of swelling, Brain Res. 530, 245-250 (1990).
30. 2 and methylmercury in astrocytes: selectivity and reversibility, J. Neurochem. 53, 1228-1237 (1989).
31. J. Albrecht, M. Talbot, H. K. Kimelbere, and M. Aschner, M, The role of sulfhydryl groups and calcium in the mercuric chloride-induced inhibition of glutamate uptake in rat primary astrocyte cultures, Brain Res. 607, 249-254 (1993).
32. R. P. Igo and J. F. Ash, New mutations and phenotypes associated with glutamate and aspartate transport in Chinese Hamster ovary (CHO-K1) cells, Somat. Cell. Mol. Genet. 22, 87-103 (1996).
33. O. J. Birot, A. Peinnequin, N. Simler, Hv. H. Cuyck-Gandre, R. Hamel, and X. A. Bigard, Vascular endothelial growth factor expression in heart of rats exposed to hypobaric hypoxia: Differential response between mRNA and protein, J. Cell Physiol. 200, 107-115 (2004).
34. 2) inhibits the in vitro uptake of glutamate in GLAST and GLT-1 transfected mutant CHO-K1 cells. Biol. Trace Element Res., in press (2005).
35. S. Duan, C. M. Anderson, B. A. Stein, and R. A. Swanson, Glutamate induces rapid upregulation of astrocyte glutamate transport and cell-surface expression of GLAST, J. Neurosci. 19, 10,193-10,200 (1999).
36. Y. Qian, A. Galli, S. Ramamoorthy S. Risso, L. J. DeFelice, and R. D. Blakely, Protein kinase C activation regulates human serotonin transporters in HEK-293 cells via altered cell surface expression, J. Neurosci. 17, 45-57 (1997).
37. K. E. Davis, D. J. Straff, E. A. Weinstein, et al., Multiple signaling pathways regulate cell surface expression and activity of the excitatory amino acid carrier 1 subtype of Glu transporter in C6 glioma, J. Neurosci. 18, 2475-2485 (1998).
38. T. W. Clarkson, The toxicology of mercury, Crit. Rev. Clin. Lab. Sci. 34, 369-403 (1997).
39. L. Kwock, Sulfhydryl group involvement in the modulation of neutral amino acid transport in thymocyte membrane vesicles, J. Cell Physiol. 106, 279-282 (1981).
40. T. C. Chiles and M. S. Kilberg, System A transport activity in normal rat hepatocytes and transformed liver cells: substrate protection from inactivation by sulfhydryl-modifying reagents, J. Cell Physiol. 129, 321-328 (1986).
41. J. L. Webb, Mercurials, in Enzyme and Metabolic Inhibitors, J. L. Webb, ed., Academic, New York, Vol. 2, pp. 729-1070 (1966).
42. V. Petronilli, P. Costantini, L. Scorrano, R. Colonna, S. Passamonti, and P. Bernardi, The voltage sensor of the mitochondrial permeability transition pore is tuned by the oxidation-reduction state of vicinal thiols. Increase of the gating potential by oxidants and its reversal by reducing agents, J. Biol. Chem. 269, 16,638-16,642 (1994).
43. Z. H. Pan, R. Bahring, R., Grantyn, and S. A. Lipton, Differential modulation by sulfhydryl redox agents and glutathione of GABA- and glycine-evoked currents in rat retinal ganglion cells, J. Neurosci. 15, 1384-1391 (1995).
44. R. P. Seal and S. G. Amara, A reentrant loop domain in the glutamate carrier EAAT1 participates in substrate binding and translocation, Neuron 21, 1487-1498 (1998).
45. M. Grunewald, A. Bendahan, and B. I. Kanner, Biotinylation of single cysteine mutant of the glutamate transporter GLT-1 from rat brain reveals its unusual topology, Neuron 21, 623-632 (1998).
46. R. Zarbiv, M. Grunewald, M. P. Kavanaugh, and V. I. Kanner, Cysteine scanning of the surroundings of an alkali-ion binding site of the glutamate transporter GLT-1 reveals a conformationally sensitive residue, J. Biol. Chem. 273, 14,231-14,237 (1998).
47. D. Trotti, B. L. Rizzini, D. Rossi, et al., Neuronal and glial glutamate transporters possess and SH-based redox regulatory mechanism, Eur. J. Neurosci. 9, 1236-1243 (1997).
48. D. Trotti, N. C. Danbolt, and A. Volterra, Glutamate transporters are oxidant-vulnerable: a molecular link between oxidative and excitotoxic neurodegeneration? Trends Pharmacol. Sci. 8, 328-334 (1998).
49. N. Zerangue and M. P. Kavanaugh, Flux coupling in a neuronal glutamate transporter, Nature 383, 634-637 (1996).