Advertisement

Effects of Myocardial Ischemia and Long Chain Acyl CoA on Mitochondrial Adenine Nucleotide Translocator

  • D. J. Paulson
  • A. L. Shug

Abstract

The synthesis of ATP occurs predominantly within mitochondria through the process of oxidative phosphorylation, and the consumption of ATP occurs in the cytosol through a variety of energy-consuming reactions (1). These processes are separated by the inner mitochondrial membrane, but are linked through a specific transport protein, adenine nucleotide translocator, which transfers ATP out of the mitochondria in exchange for cytosolic ADP (2). This transport protein is specific for ATP and ADP only; AMP, GTP and GDP are not transported (3). The magnesium complexes of ATP and ADP are also inactive (4). The rate of adenine nucleotide transport is very rapid and requires short time intervals and low temperatures or specialized sophisticated equipment to measure transport kinetics (5, 6). In beef heart mitochondria, the extrapolated rate of adenine nucleotide translocater at 37° is 1800 µmoles/g protein (6). The transport of ATP and ADP is not an energy-consuming process (4). It will occur in uncoupled mitochondria but then ADP and ATP are translocated in both directions. In energized states, there is a preferential uptake of ADP and efflux of ATP.

Keywords

Creatine Kinase Adenine Nucleotide Mitochondrial Matrix Adenine Nucleotide Translocator Mitochondrial Creatine Kinase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Lehninger, A.L. (1972): Biochemistry, Worth, New York.Google Scholar
  2. 2.
    Klingenberg, M. (1976): IN The Enzymes of Biological Membranes: Membrane Transport, Vol. 3, (ed.) M. Anthony, Plenum Press, New York, p. 363.Google Scholar
  3. 3.
    Pfaff, E., & Klingenberg, M. (1968): Eur. J. Biochem. 6: 66.PubMedCrossRefGoogle Scholar
  4. 4.
    Klingenberg, M., & Heldt, H.W. (1982): IN Metabolic Compartmentation, (ed.) H. Sies, Academic Press, London, p. 101.Google Scholar
  5. 5.
    Heldt, H.W., & Klingenberg, M. (1968): Eur. J. Biochem. 4: 1.PubMedCrossRefGoogle Scholar
  6. 6.
    Klingenberg, M., Grebe, K., & Appel, M. (1982): Eur. J. Biochem. 126: 263.PubMedCrossRefGoogle Scholar
  7. 7.
    Vignais, P.V. (1976): Biochim. Biophys. Acta 456: 1.PubMedGoogle Scholar
  8. 8.
    Groen, A.K., Wanders, R.J.A., Westerhoff, H.V., Van der Meer, R., & Tager, J.M. (1982): J. Biol. Chem. 257: 2754.PubMedGoogle Scholar
  9. 9.
    Wilson, D.F., Nelson, D., & Erecinska, M. (1982): FEBS Lett. 143: 228.PubMedCrossRefGoogle Scholar
  10. 10.
    Wilson, D.F., & Owen, C. (1973): Biochem. Biophys. Res. Commun. 53: 326.PubMedCrossRefGoogle Scholar
  11. 11.
    Van der Meer, R., Westerhoff, H.V., & Van Dam, K. (1980): Biochim. Biophys. Acta 591: 488.PubMedCrossRefGoogle Scholar
  12. 12.
    Bessman, S.P., & Geiger, P.J. (1981): Science 211: 448.PubMedCrossRefGoogle Scholar
  13. 13.
    Jacobs, H., Heldt, H.W., & Klingenberg, M. (1964): Biochem. Biophys. Res. Commun. 16: 516.PubMedCrossRefGoogle Scholar
  14. 14.
    Jacobus, W.E., & Lehninger, A.L. (1973): J. Biol. Chem. 248: 4803.PubMedGoogle Scholar
  15. 15.
    Yang, W.C.T., Geiger, P.J., Bessman, S.P., Borrebaek, B. (1977): Biochem. Biophys. Res. Commun. 76: 882.PubMedCrossRefGoogle Scholar
  16. 16.
    Saks, V.A., Kupriyanov, V.V., Elizarova, G.V., & Jacobus, W.E. (1980): J. Biol. Chem. 255: 755.PubMedGoogle Scholar
  17. 17.
    Jacobus, W.E., & Saks, V.A. (1982): Arch. Biochem. Biophys. 219: 167.PubMedCrossRefGoogle Scholar
  18. 18.
    Erickson-Viitanen, S., Viitanen, P., Geiger, P.J., Yang, W.C.T., & Bessman, S.P. (1982): J. Biol. Chem. 257: 14395.PubMedGoogle Scholar
  19. 19.
    Moreadith, R.W., & Jacobus, W.E. (1982): J. Biol. Chem. 257: 899.PubMedGoogle Scholar
  20. 20.
    Saks, V.A., Chernousova, G.B., Gukovsky, D.E., Smirnov, V.N., & Chazov, E.I. (1975): Eur. J. Biochem. 57: 273.PubMedCrossRefGoogle Scholar
  21. 21.
    Saks, V.A., Lipina, N.V., Smirnov, V.N., & Chazov, E.I. (1976): Arch. Biochem. Biophys. 173: 34.PubMedCrossRefGoogle Scholar
  22. 22.
    Altshuld, R.A., & Brierly, G.P. (1977): J. Mol. Cell. Cardiol. 9: 875.CrossRefGoogle Scholar
  23. 23.
    Borrebaek, B. (1980): Arch. Biochem. Biophys. 203: 827.PubMedCrossRefGoogle Scholar
  24. 24.
    Erickson-Viitanen, S., Geiger, P.J., Viitanen, P., & Bessman, S.P. (1982): J. Biol. Chem. 257: 14405.PubMedGoogle Scholar
  25. 25.
    Klingenberg, M., & Rottenberg, H. (1977): Eur. J. Biochem. 73: 125.PubMedCrossRefGoogle Scholar
  26. 26.
    Pfaff, E., Heldt, H.W., & Klingenberg, M. (1969): Eur. J. Biochem. 10: 484.PubMedCrossRefGoogle Scholar
  27. 27.
    Vignais, P.V., Vignais, P.M., Lauquin, G., & Morel, F. (1973): Biochimie (Paris) 55: 763.Google Scholar
  28. 28.
    Barbour, R.L., & Chan, S.H.P. (1981): J. Biol. Chem. 256: 1940.PubMedGoogle Scholar
  29. 29.
    Shug, A., Lerner, E., Elson, C., & Shrago, E. (1971): Biochem. Biophys. Res. Commun. 43: 557.Google Scholar
  30. 30.
    Pande, S.V., & Blanchaer, M.C. (1971): J. Biol. Chem. 246: 402.PubMedGoogle Scholar
  31. 31.
    Harris, R.A., Farmer, B., & Ozawa, T. (1972): Arch. Biochem. Biophys. 150: 199.PubMedCrossRefGoogle Scholar
  32. 32.
    Barbour, R.L., & Chan, S.H.P. (1979): Biochem. Biophys. Res. Commun. 89: 1169.CrossRefGoogle Scholar
  33. 33.
    Chua, B.H., & Shrago, E. (1977): J. Biol. Chem. 252: 6711.PubMedGoogle Scholar
  34. 34.
    Klingenberg, M. (1977): Eur. J. Biochem. 76: 553.PubMedCrossRefGoogle Scholar
  35. 35.
    Lauquin, G.J.M., Villiers, C., Michejda, J.W., Hryniewiecka, L.V., & Vignais, P.V. (1977): Biochim. Biophys. Acta 460: 331.PubMedCrossRefGoogle Scholar
  36. 36.
    La Noue, K.F., Watts, J.A., & Koch, CD. (1981): Am. J. Physiol. 241: H663.Google Scholar
  37. 37.
    Morel, F., Lauquin, G., Lunardi, J., Duszyński, J., & Vignais, P.V. (1974): FEBS Lett. 39: 133.PubMedCrossRefGoogle Scholar
  38. 38.
    Neely, J.R., Liebermeister, H., Battersby, E.J., & Morgan, H.E. (1967): Am. J. Physiol. 212: 804.PubMedGoogle Scholar
  39. 39.
    Adams, H. (1965): IN Methods of Enzymatic Analysis, (ed) H.H. Bergmeyer, Academic Press, New York, p. 573.Google Scholar
  40. 40.
    Stanley, P.E., & Williams, S.O. (1969): Anal. Biochem. 29: 381.PubMedCrossRefGoogle Scholar
  41. 41.
    Veloso, D., & Veech, R.L. (1974): Anal. Biochem. 62: 449.PubMedCrossRefGoogle Scholar
  42. 42.
    Keleti, G., & Lederer, W.H. (1974): IN Handbook of Micro-Methods for Biological Sciences, Van Niehand Reinhold, New York, p. 86.Google Scholar
  43. 43.
    Shug, A.L., Thomsen, J.D., Folts, J.D., Bittar, N., Klein, M.I., Koke, J.R., & Huth, P.J. (1978): Arch. Biochem. Biophys. 187: 25.PubMedCrossRefGoogle Scholar
  44. 44.
    Whitmer, J.T., Idell-Wetiger, J.A., Rovetto, M.J., & Neely, J.R. (1978): J. Biol. Chem. 253: 4305.PubMedGoogle Scholar
  45. 45.
    Idell-Wenger, J.A., Grotyohann, L.W., & Neely, J.R. (1978): J. Biol. Chem. 253: 4310.PubMedGoogle Scholar
  46. 46.
    Powell, G.L., Grothusen, J.R., Zimmerman, J.K., Evans, C.A., & Fish, W.W. (1981): J. Biol. Chem. 256: 12740.PubMedGoogle Scholar
  47. 47.
    Fritz, I.B., & Marquis, N.R. (1965): Proc. Natl. Acad. Sci. USA 54: 1226.PubMedCrossRefGoogle Scholar
  48. 48.
    Heldt, H.W., Jacobs, H., & Klingenberg, M. (1965): Biochem. Biophys. Res. Commun. 18: 174.Google Scholar
  49. 49.
    Vignais, P.V., Vignais, P.M., & Defayl, G. (1973): Biochemistry 12: 1508.PubMedCrossRefGoogle Scholar
  50. 50.
    Bremer, J., & Norum, K.R. (1967): J. Biol. Chem. 252: 1744.Google Scholar
  51. 51.
    Neely, J.R., & Morgan, U.E. (1974): Ann. Rev. Physiol. 36: 413.CrossRefGoogle Scholar
  52. 52.
    Folts, J.D., Shug, A.L., Koke, J.R., & Bittar, N. (1978): Am. J. Cardiol. 41: 1209.PubMedCrossRefGoogle Scholar
  53. 53.
    Liedtke, A.J., Nellis, S.H., & Whitesell, L.F. (1981): Circ. Res. 48: 859.PubMedGoogle Scholar
  54. 54.
    Suzuki, Y., Kamikawa, T., Kobayashi, A., Musumura, Y., & Yamazaki, N. (1981): Jap. Cire. J. 45: 687.CrossRefGoogle Scholar
  55. 55.
    Halperin, M.L., Robinson, B.H., & Fritz, I.B. (1972): Proc. Natl. Acad. Sci. USA 69: 1003.PubMedCrossRefGoogle Scholar
  56. 56.
    Woldegiorgis, G., Yousufzai, S.Y.K., & Shrago, E. (1982): J. Biol. Chem. 257: 14783.PubMedGoogle Scholar
  57. 57.
    Pearson, D.J., & Tubbs, R.K. (1967): Biochem. J. 105: 953.PubMedGoogle Scholar
  58. 58.
    Feuvray, D., Idell-Wenger, J.A., & Neely, J.R. (1979): Circ. Res. 44: 322.PubMedGoogle Scholar
  59. 59.
    Burlington, R.F., & Shug, A.L. (1981): Comp. Biochem. Physiol. 68: 431.CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1984

Authors and Affiliations

  • D. J. Paulson
    • 1
    • 2
  • A. L. Shug
    • 1
    • 2
  1. 1.Metabolic Research Lab WilliamS. Middleton Memorial Veterans HospitalMadisonUSA
  2. 2.Department of NeurologyUniversity of WisconsinMadisonUSA

Personalised recommendations