Online versions of scientific journals Current user: guest        
Hide Left Menu
Temporary Collection

Customer support
» support service
» FAQ
» help
Abstract of article
Biophysics

 -  Vol. 50, No. 1, January-February 2005, pp. 74-79 Help

[ Previous / Next Abstract | Issue Contents | Bottom of Page ] Delete from Cart Add to Cart Delete from Collection Add to Collection

Product Price:  30.00 USD;  Product Discount:  0.0%;

Full Text: [PDF (61Kb)] |  
 
Stable Isotopes of Mg2+ as Activators of the Suppressed ATP-Generating Function of Mitochondria
D. A. Kuznetsov1, S. E. Arkhangel'skii1, A. G. Berdieva2, A. A. Markaryan2, P. Z. Khasigov2, T. M. Gatagonova2, S. A. Ktsoeva2, and M. A. Orlova3
1Semenov Institute of Chemical Physics, Russian Academy of Sciences, Moscow, 119991 Russia
2Sechenov Moscow Medical Academy, Moscow, 117421 Russia
3Lomonosov Moscow State University, Moscow, 119991 Russia

Received September 16, 2003
in final form June 3, 2004
Key words: myocardial mitochondria, creatine kinase, 1-methylnicotinamide.

The ATP-generating activity of mitochondria and mitochondrial creatine kinase was studied as a function of the isotopy of the magnesium pool of the incubation medium. The objects of investigation were in vitro systems containing preparations of isolated mitochondria and the enzyme from the myocardium of rats given a single injection of 1-methylnicotinamide to a dose of 1/2DL50. It was shown that the presence of paramagnetic cations of the 25Mg isotope leads to significant compensation for the intramitochondrial ATP deficiency caused by suppression of oxidative phosphorylation by 1-methylnicotinamide. This effect is virtually unachievable in systems whose magnesium pool comprises isotopes with zero nuclear spin (24Mg and 26Mg). The restoration of the mitochondrial ATP synthesis under induced inhibition of NAD/NADP-de-pendent reactions by 1-methylnicotinamide involves creatine kinase, whose activity is not suppressed by 1-methylnicotinamide. The high efficiency of restoration of this process is a spin-selective phenomenon and is reached mainly in the presence of 25Mg2+ cations. The significance of the obtained data for further investigation of the mechanisms of regulation of enzymatic catalysis was discussed.

References

  1. O. Okada, S. Telashima, M. Satoh, et al., J. Japan Pharm. Soc. 58, 211 (2000).
  2. A. Velaidi, in Toxic Agents in Biomedical Research, Ed. by R. Sanai and T. Amirkanian (Guilan Press, Rasht-Tehran, 2003), pp. 44–60.
  3. G. Hranic and Z. Milutinovic, Acta Biol. Med. Slovenica 8, 601 (2002).
  4. V. B. Mahajan, K. S. Pai, A. Lau, and D. D. Cunningham, Proc. Natl. Acad. Sci. USA 97, 12062 (2000).
  5. A. L. Buchachenko, J. Phys. Chem. A105, 9995 (2001).
  6. W. E. Jacobus and A. Saks, Arch. Biochem. Biophys. 219, 167 (1982).
  7. L. A. Belousova, T. Y. Lipskaya, V. D. Temple, and A. P. Rostovtsev, in Advances in Myocardiology, Ed. by E. I. Chazov, V. N. Smirnov, and T. S. Dhalla (University Park Press, Baltimore, 1983), pp. 585–595.
  8. A. G. Gornall, C. L. Bardawill, and M. M. David, J. Biol. Chem. 177, 751 (1949).
  9. J. S. Moudy and T. D. Barthelrough, J. Pharm. Chem. 19, 610 (1986).
  10. S. Sobol, A. Conrad, and S. Hebish, Mol. Cell. Biochem. 133/134, 105 (1994).
  11. D. A. Kouznetsov, A. V. Govorkov, N. V. Zavijalov, et al., J. Biochem. Biophys. Methods 13, 53 (1986).
  12. B. Sieliwanowicz, L. Skrob, and A. Mlody, in Mitochondria, Ed. by R. Novotny and K. Bolek (Jagellonski University Press, Krakov, 1990), pp. 109–132.
  13. S. Sobol, A. Konrad, M. Keller, and S. Hebisch, Biochim. Biophys Acta 1100, 27 (1992).
  14. E. J. Davis and L. Lumerg, J. Biol. Chem. 250, 2275 (1975).
  15. D. A. Kuznetsov, M. A. Orlova, A. G. Berdieva, and P. Z. Khasigov, Biomed. Khim. 49, 213 (2003).
  16. K. Lowenhaupt, S. J. Troll, T. Ornelli, et al., Canad. J. Gen. Pathol. 38, 1008 (2003).
  17. L. S. Sarcar and T. Lemke, Biostatistics (Alba Regia, Szeged-Budapest, 1980).
  18. C. B. Grissom, Chem. Rev. 95, 3 (1995).
  19. I. G. Alkoev, M. S. Pashovkina, L. P. Dolgacheva, T. P. Semenova, and V. L. Kalmykov, Radiat. Biol. Radioekol. 42, 322 (2002).
  20. O. J. Lottrell, S. Thaler, and D. O'Neal, Mol. Cell. Pathol. 18, 441 (2003).
  21. K. Hummel, K. Martle, and M. G. Martle, J. Mol. Catal. 54, L1 (1989).
  22. A. L. Buchachenko, Progr. React. Kinet. 13, 164 (1984).
  23. A. L. Buchachenko, Russ. Chem. Rev. 62, 1073 (1993).
  24. A. A. Ivanov, Biofractionation of Carbone Isotopes and Photosynthesis (Turin Polytechnical University Press, Turin-Varese-Milan, 2002).
  25. T. Yu. Lipskaya and M. S. Savchenko, Biokhimiya 68, 82 (2003).
  26. E. J. Calobrese and L. A. Baldwin, Nature 421, 691 (2003).
  27. D. A. Kousnetsov, Neurochem. Res. 12, 751 (1986).
  28. A. L. Buchachenko, D. A. Kousnetsov, and A. V. Shishkov, J. Phys. Chem. A108, 707 (2003).
  29. J. Schlichter, J. Fredrich, M. Parbel, and H. Scheer, J. Chem. Phys. 114, 9638 (2001).
  30. D. A. Kouznetsov and J. J. Brochard, Progr. Mol. Pharmacol. Toxicol. Res. 22, 680 (1999).


PII: S0006350905010100

[ Previous / Next Abstract | Issue Contents | Top of Page ]