The dual personality of ionic copper in biology

Journal of Inclusion Phenomena and Macrocyclic Chemistry

Volumn 65, Issue 1, 2009, Pages 165-170

  Cuillel, Martine ^a,b,c  

^a CEA GRENOBLE   (France)

^b CNRS   (France)

^c UNIV GRENOBLE ALPES   (France)

Author keywords

Biology; Copper; Homeostasis; Toxicity

Indexed keywords

EID: 76349094102     PISSN: 09230750     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10847-009-9636-4     Document Type: Article

References (29)

1. Peña, M. M., Lee, J., Thiele, D. J.: A delicate balance: homeostatic control of copper uptake and distribution. J. Nutr. 129, 1251-1260 (1999).
2. Frausto da Silva, J. J. R., Williams, R. J. P.: The Biological Chemistry of the Elements. Clarendon Press, Oxford (2001).
3. Rensing, C., Grass, G.: Escherichia coli mechanisms of copper homeostasis in a changing environment. FEMS Microbiol. Rev. 27, 197-213 (2003).
4. Cotton, F. A., Wilkinson, G.: Advanced Inorganic Chemistry. Wiley, New York (1987).
5. Huheey, J. E., Keiter, E. A., Keiter, R. L.: Inorganic Chemistry: Principles of Structure and Reactivity. Harper Collins College, New York (1993).
6. Karlin, S., Zhu, Z. Y., Karlin, K. D.: The extended environment of mononuclear metal centers in protein structures. Proc. Natl. Acad. Sci. USA. 94, 14225-14230 (1997).
7. Koch, K. A., Peña, M. M., Thiele, D. J.: Copper-binding motifs in catalysis, transport, detoxification and signaling. Chem. Biol. 4, 549-560 (1997).
8. Solomon, E. I., Sundaram, U. M., Machonkin, T. E.: Multicopper oxidases and oxygenases. Chem. Rev. 96, 2563-2606 (1996).
9. Hornstra, I. K., Birge, S., Starcher, B., Bailey, A. J., Mecham, R. P., et al.: Lysyl oxidase is required for vascular and diaphragmatic development in mice. J. Biol. Chem. 278, 14387-14393 (2003).
10. Czyzyk, T. A., Ning, Y., Hsu, M. S., Peng, B., Mains, R. E., et al.: Deletion of peptide amidation enzymatic activity leads to edema and embryonic lethality in the mouse. Dev. Biol. 287, 301-313 (2005).
11. Vulpe, C. D., Kuo, Y. M., Murphy, T. L., Cowley, L., Askwith, C., et al.: Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse. Nat. Genet 21, 195-199 (1999).
12. Sarkar, B.: Metal replacement in DNA-binding zinc finger proteins and its relevance to mutagenicity and carcinogenicity through free radical generation. Nutrition 11, 646-649 (1995).
13. De Feo, C. J., Aller, S. G., Siluvai, G. S., Blackburn, N. J., Unger, V. M.: Three-dimensional structure of the human copper transporter hCTR1. Proc Natl. Acad. Sci. USA 106, 4237-4242 (2009).
14. De Rome, L., Gadd, G. M.: Measurement of copper uptake in Saccharomyces cerevisiae using a Cu2+ -selective electrode. FEMS Microbiol. Lett. 43, 283-287 (1987).
15. Labbé, S., Zhu, Z., Thiele, D. J.: Copper-specific transcriptional repression of yeast genes encoding critical components in the copper transport pathway. J. Biol. Chem. 272, 15951-15958 (1997).
16. Kuo, Y. M., Gybina, A. A., Pyatskowit, J. W., Gitschier, J., Prohaska, J. R.: Copper transport protein (Ctr1) levels in mice are tissue specific and dependent on copper status. J. Nutr. 136, 21-26 (2006).
17. Finney, L. A., O'Halloran, T. V.: Transition metal speciation in the cell: insights from the chemistry of metal ion receptors. Science 300, 931-936 (2003).
18. Calderone, V., Dolderer, B., Hartmann, H. J., Echner, H., Luchinat, C., et al.: The crystal structure of yeast copper thionein: the solution of a long-lasting enigma. Proc. Natl. Acad. Sci. USA. 102, 51-56 (2005).
19. Rae, T. D., Schmidt, P. J., Pufahl, R. A., Culotta, V. C., O'Halloran, T. V.: Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase. Science 284, 805-808 (1999).
20. Glerum, D. M., Shtanko, A., Tzagoloff, A.: Characterization of COX17, a yeast gene involved in copper metabolism and assembly of cytochrome oxidase. J. Biol. Chem. 271, 14504-14509 (1996).
21. Horng, Y. C., Cobine, P. A., Maxfield, A. B., Carr, H. S., Winge, D. R.: Specific copper transfer from the Cox17 metallochaperone to both Sco1 and Cox11 in the assembly of yeast cytochrome C oxidase. J. Biol. Chem. 279, 35334-35340 (2004).
22. 2-terminal domain of the Wilson's disease protein and regulates its catalytic activity. J. Biol. Chem. 277, 27953-27959 (2002).
23. Lin, S. J., Pufahl, R. A., Dancis, A., O'Halloran, T. V., Culotta, V. C.: A role for the Saccharomyces cerevisiae ATX1 gene in copper trafficking and iron transport. J. Biol. Chem. 272, 9215-9220 (1997).
24. Morin, I., Gudin, S., Mintz, E., Cuillel, M.: Dissecting the role of the N-terminal metal-binding domains in activating the yeast copper ATPase in vivo. Febs. J. (2009) (in press).
25. La Fontaine, S., Mercer, J. F.: Trafficking of the copper-ATPases, ATP7A and ATP7B: role in copper homeostasis. Arch. Biochem. Biophys. 463, 149-167 (2007).
26. Mercer, J. F.: The molecular basis of copper-transport diseases. Trends Mol. Med. 7, 64-69 (2001).
27. Sarkar, B.: Early copper histidine therapy in classic Menkes disease. Ann. Neurol. 41, 134-136 (1997).
28. Gitlin, J. D.: Wilson disease. Gastroenterology 125, 1868-1877 (2003).
29. Gaggelli, E., Kozlowski, H., Valensin, D., Valensin, G.: Copper homeostasis and neurodegenerative disorders (Alzheimer's, prion, and Parkinson's diseases and amyotrophic lateral sclerosis). Chem. Rev. 106, 1995-2044 (2006).