Journal of Bioenergetics and Biomembranes

, Volume 34, Issue 5, pp 389–395 | Cite as

Role of Copper in Mitochondrial Biogenesis Via Interaction with ATP Synthase and Cytochrome c Oxidase

Article

Abstract

Animals that are copper deficient have cardiac hypertrophy where there is a dramatic increase in mitochondria. Mitochondrial biogenesis is enhanced in this model and there is an upregulation of mitochondrial transcription factor A (mtTFA) and nuclear respiratory factors 1 and 2 (NRF-1 and NRF-2). While the cuproenzyme, cytochrome c oxidase (CCO), is an attractive candidate to explain the connection between cardiac hypertrophy in copper deficiency and subsequent mitochondrial biogenesis, studies have revealed that ATP synthase may be impacted by copper depletion. NRF-1 and NRF-2 can bind to some of the subunits of both CCO and ATP synthase to regulate gene expression. Furthermore, oxidative phosphorylation appears to occur unaltered in the copper-deficient state. Copper-deficient mitochondria appear to be less sensitive to the inhibitory effect of oligomycin compared to controls. Decreases in the δ subunit protein and β mRNA transcript have been reported for ATP synthase as a function of copper deficiency. The limited data available suggest that copper, either indirectly or directly, alters ATP synthase function.

ATP synthase copper cytochrome c oxidase mitochondrial transcriptional factor A nuclear respiratory factors mitochondria 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

REFERENCES

  1. Archinard, P., Godinot, C., Comte, J., and Gautheron, D. C. (1986). Biochemistry 25, 3397–3404.Google Scholar
  2. Belogrudov, G., Tomich, J. M., and Hatefi, Y. (1996). J. Biol. Chem. 271, 20340–20345.Google Scholar
  3. Bonnikov, G. E., Vinogradova, S. O., and Chernyak, B. V. (1990). FEBS Lett. 266, 83–86.Google Scholar
  4. Chao, J. C., Medeiros, D. M., Atschuld, R. A., and Hohl, C. M. (1993). Life Sci. 104A, 163–168.Google Scholar
  5. Chau, J. C., Medeiros, D. M., Davidson, J., and Shiry, L. (1994). J. Nutr. 124, 789–803.Google Scholar
  6. Chau, C. A., Evans, M. J., and Scarpulla, R. C. (1992). J. Biol. Chem. 267, 6999–7006.Google Scholar
  7. Chen, X., Jennings, D. B., and Medeiros, D. M. (2002). J. Bioenerg. Biomem. 34, 397–406.Google Scholar
  8. Dairaghi, D. J., Shadel, G. S., and Clayton, D. A. (1995). J. Mol. Biol. 249, 11–28.Google Scholar
  9. Davidson, J. A., Medeiros, D. M., and Hamlin, R. L. (1992). J. Nutr. 122, 1566–1575.Google Scholar
  10. Giraud, M. F., and Velours, J. (1997). Eur. J. Biochem. 245, 813–818.Google Scholar
  11. Gomez-Puyou, A., Ayala, G., Muller, U., and Tuena de Gomez-Puyou, M. (1983). J. Biol. Chem. 258, 13673–13679.Google Scholar
  12. Gopalakrishnan, L., and Scarpulla, R. C. (1995). J. Biol. Chem. 270, 18019–18025.Google Scholar
  13. Guerrieri, F., Zanotti, F., Capozza, G., Colaianni, G., Ronchi, S., and Papa, S. (1991). Biochim. Biophys. Acta 1059, 348–354.Google Scholar
  14. Guerrieri, F., Zanotti, F., Che, Y. W., scarfo, R., and Papa, S. (1987). Biochim. Biophys. Acta 892, 284–293.Google Scholar
  15. Gugneja, S., Virbasius, J.V., and Scarpulla, R. C. (1995). Mol. Cell. Biol. 15, 102–111. ATP Synthase, Cytochrome c Oxidase, and Copper 395 Google Scholar
  16. Hopp, J., Gatti, D., Weber, H., and Sebald, W. (1986). Eur. J. Biochem. 155, 259–264.Google Scholar
  17. Klein, G., Satre, M., Dianoux, A. C., and Vignais, P. V. (1980). Biochemistry. 24, 2919–2925.Google Scholar
  18. Jalili, T., Medeiros, D. M., and Wildman, R. E. C. (1996). J. Nutri. 126, 807–816.Google Scholar
  19. LaFontaine, S., Firth, S. D., Camakaris, J., Englezou, A., Theohilos, M. B., Petris, M. J., Howie, M., Lockhart, P. J., Greenoughs, M., Brooks, H., Reddle, R. R., and Mercer, J. F.B. (1998). J. Biol. Chem. 272, 31375–31380.Google Scholar
  20. Lukaski, H. C., Hall, C. B., and Marchello, M. J. (1995). J. Nutr. Biochem. 6, 445–451.Google Scholar
  21. Mao, S., Leone, T. C., Kelly, D. P., and Medeiros, D. M. (2000). J. Nutr. 130, 2143–2150.Google Scholar
  22. Mao, S., and Medeiros, D. M. (2001). Biol. Trace. Elem. Res. 83, 57–68.Google Scholar
  23. Mao, S., Medeiros, D. M., and Wildman, R. E. C. (1998). Biol. Trace Elem. Res. 63, 175–184.Google Scholar
  24. Marin-Garcia, J., and Goldenthal, M. J. (1997). Pediatr. Cardiol. 18, 251–260.Google Scholar
  25. Martin, I., Villena, J. S., Giralt, M., Iglesias, R., Mampel, T., Vinas, O., and Villarroya, F. (1996). Mol. Cell. Biochem. 154, 107–111.Google Scholar
  26. Matz, J. M., Saari, J. T., and Bode, A. M. (1995). J. Nutr. Biochem. 6, 644–652.Google Scholar
  27. McCormick, R. J., Ovecka, G. D., and Medeiros, D. M. (1989). J. Nutr. 119, 1683–1690.Google Scholar
  28. Medeiros, D. M., Bagby, D., Ovecka, G. and McCormick R. (1991a). J. Nutr. 121, 815–824.Google Scholar
  29. Medeiros, D. M., and Beard, J. L. (1998). Proc. Soc. Exp. Biol. Med. 218, 370–375.Google Scholar
  30. Medeiros, D. M., Liao, Z., and Hamlin, R. L. (1991b). J. Nutr. 121, 1026–1034.Google Scholar
  31. Medeiros, D. M., Lin, K. N., Liu, C. F., and Thorne, B. M. (1984). Nutr. Rep. Int. 30, 559–564.Google Scholar
  32. Medeiros, D. M., Shiry, L., Lincoln, A. J., and Prochaska, L. (1993). Biol. Trace Elem. Res. 36, 271–282.Google Scholar
  33. Medeiros, D. M., Shiry, L., and Samelman, T. (1997). Comp. Biochem. Physiol. 117A, 77–87.Google Scholar
  34. Medeiros, D. M., and Wildman, R. E. C. (1997). Proc. Soc. Exp. Biol. Med. 215, 299–313.Google Scholar
  35. Montoya, J., Perez-Martos, A., Garstka, H. L., and Wiesner, R. L. (1997). Mol. Cell. Biochem. 174, 227–230.Google Scholar
  36. Pan, W., Ko, Y. H., and Pedersen, P. L. (1998). Biochemistry 37, 6911–6923.Google Scholar
  37. Papa, S., Xu, T., Gaballo, A., and Zanotti, F. (1999). In Frontiers of Cellular Bioenegetics: Molecular Biology, Biochemistry and Physiopathology (Papa, S., Guerrieri, F., and Tager, J. M., eds.), Plenum, London, UK, pp. 459–486.Google Scholar
  38. Papa, S., Zanotti, F., and Gaballo, A. (2000). J. Bioenerg. Biomemb. 32, 401–411.Google Scholar
  39. Parisi, M. A., Xu, B., and Clayton, D. A. (1993). Mol. Cell. Biol. 13, 1951–1961.Google Scholar
  40. Pedersen, P. L., Ko, Y. H., and Hong, S. (2000a). J. Bioenerg. Biomemb. 32, 325–332.Google Scholar
  41. Pedersen, P. L., Ko, Y. H., and Hong, S. (2000b). J. Bioenerg. Biomemb. 32, 423–432.Google Scholar
  42. Pedersen, P. L., and Amzel, L. M. (1993). J. Biol. Chem. 268, 9937–9940.Google Scholar
  43. Rusinko, N., and Prohaska, J. R. (1995). J. Nutr. 115, 936–943.Google Scholar
  44. Saraste, M. (1999). Science (Washington, DC) 283, 1488–1493.Google Scholar
  45. Tsunoda, S. P., Rodgers, A. J., Aggeler, R., Wilce, M. C., Yoshida, M., and Capaldi, R. A. (2001). Proc. Natl. Acad. Sci. U.S.A. 98, 6560–6564.Google Scholar
  46. Villena, J. A., Vinas, O., Mampel, T., Iglesias, R., Giralt, M., and Villarroya F. (1998). Biochem. J. 331, 121–127.Google Scholar
  47. Virbasius, J.V., and Scarpulla, R. C. (1994). Proc. Natl. Acad. Sci.U.S.A. 91, 1309–1313.Google Scholar
  48. Virbasius, C. A., Virbasius, J. V., and Scarpulla, R. C. (1993). Genes Dev. 7, 2431–2445.Google Scholar
  49. Wildman, R. E. C., Medeiros, D. M., Hamlin, R. L., Stills, H., Jones, D. A., and Bonagura, J. D. (1996). Biol. Tr. El. Res. 55, 55–70.Google Scholar
  50. Wildman, R. E. C., Medeiros, D. M., and Jenkins, J. (1994). Biol. Tr. El. Res. 46, 51–66.Google Scholar
  51. Wu, B. N., Medeiros, D. M., Liu, C. F., and Thorne, B. M. (1984). Nutr. Res. 4, 305–314.Google Scholar
  52. Zanotti, F., Guerrieri, F., Capozza, G., Houstek, J., Runchi, S., and Papa, S. (1988). S Lett. 237, 9–14.Google Scholar

Copyright information

© Plenum Publishing Corporation 2002

Authors and Affiliations

  1. 1.Department of Human NutritionKansas State UniversityManhattan

Personalised recommendations