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Neurochemical Journal

, Volume 12, Issue 1, pp 33–40 | Cite as

Melatonin Modulates Phosphorylation of 2′,3′-Cyclic Nucleotide-3′-Phosphodiesterase in the Presence of Protoporphyrin IX in the Brain Mitochondria of Rats during the Functioning of the Non-Specific Mitochondrial Pore

  • O. V. Krestinina
  • Yu. L. Baburina
  • I. V. Odinokova
  • T. S. Azarashvili
  • V. S. Akatov
Experimental Articles
  • 14 Downloads

Abstract

Melatonin (N-acetyl-5-methoxytryptamine), a neuroendocrine hormone of the pineal gland, participates in the modulation of the mitochondrial nonspecific pore (mitochondrial permeability transition pore, mPTP). According to the results we obtained, protoporphyrin IX (PPIX, a ligand of the TSPO translocator protein) induces the opening of the mPTP in brain mitochondria; melatonin slows the induction of the mPTP in rat brain mitochondria incubated with PPIX. Induction of the mPTP activates protein kinases/protein phosphatases that are involved in the regulation of protein phosphorylation. The TSPO modulates protein phosphorylation; in the presence of PPIX, the phosphorylation of 2′,3′-cyclic nucleotide-3′-phosphodiesterase (CNPase) increases. Here, we showed an increase in the degree of phosphorylation of CNPase in PPIX-treated rat brain mitochondria, a melatonin-induced decrease in level of CNPase phosphorylation in mitochondria incubated with PPIX; hence, we propose that melatonin participates in TSPOmodulated protein phosphorylation.

Keywords

melatonin rat brain mitochondria protein phosphorylation protoporphyrin IX non-specific permeability pore 2′,3′-cyclic nucleotide-3′-phosphodiesterase (CNPase) 

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References

  1. 1.
    Falcon, J., Besseau, L., Fuentes, M., Sauzet, S., Magnanou, E., and Boeuf, G., Ann. NY: Acad. Sci., 2009, vol. 1163, pp. 101–111.CrossRefGoogle Scholar
  2. 2.
    Tan, D.-X., Manchester, L.C., Hardeland, R., Lopez-Burillo, S., Mayo, J.C., Sainz, R.M., and Reiter, R.J., J. Pineal Res., 2003, vol. 34, pp. 75–78.CrossRefPubMedGoogle Scholar
  3. 3.
    Tan, D.X., Poeggeler, B., Reiter, R.J., Chen, L.D., Chen, S., Manchester, L.C., and Barlowwalden, L.R., Cancer Lett., 1993, vol. 70, pp. 65–71.CrossRefPubMedGoogle Scholar
  4. 4.
    Menendez-Pelaez, A. and Reiter, R.J., J. Pineal Res., 1993, vol. 15, pp. 59–69.CrossRefPubMedGoogle Scholar
  5. 5.
    Lopez, A., Garcia, J.A., Escames, G., Venegas, C., Ortiz, F., Lopez, L.C., and Acuna-Castroviejo, D., J. Pineal Res., 2009, vol. 46, pp. 188–198.CrossRefPubMedGoogle Scholar
  6. 6.
    Acuna-Castroviejo, D., Escames, G., Leon, J., Carazo, A., and Khaldy, H., Adv. Exp. Med. Biol., 2003, vol. 527, pp. 549–557.CrossRefPubMedGoogle Scholar
  7. 7.
    Castroviejo, D.A., Lopez, L.C., Escames, G., Lopez, A., Garcia, J.A., and Reiter, R.J., Curr. Top. Med. Chem., 2011, vol. 11, pp. 221–240.CrossRefGoogle Scholar
  8. 8.
    Acuna-Castroviejo, D., Escames, G., Rodriguez, M.I., and Lopez, L.C., Front. Biosci.-Landmrk, 2007, vol. 12, pp. 947–963.CrossRefGoogle Scholar
  9. 9.
    Martin, M., Macias, M., Escames, G., Reiter, R.J., Agapito, M.T., Ortiz, G.G., and Acuna-Castroviejo, D., J. Pineal Res., 2000, vol. 28, pp. 242–248.CrossRefPubMedGoogle Scholar
  10. 10.
    Petrosillo, G., Colantuono, G., Moro, N., Ruggiero, F.M., Tiravanti, E., Di Venosa, N., Fiore, T., and Paradies, G., Am. J. Physiol. Heart Circ. Physiol., 2009, vol. 297, pp. H1487–1493.CrossRefPubMedGoogle Scholar
  11. 11.
    Jou, M.J., J. Pineal Res., 2011, vol. 50, pp. 427–435.CrossRefPubMedGoogle Scholar
  12. 12.
    Di Lisa, F. and Bernardi, P., Cardiovasc. Res., 2005, vol. 66, pp. 222–232.CrossRefPubMedGoogle Scholar
  13. 13.
    Krestinina, O.V., Baburina, Y.L., and Azarashvili, T.S., Biol. Membrany, 2014, vol. 31, pp. 95–103.CrossRefGoogle Scholar
  14. 14.
    Lim, S., Smith, K.R., Lim, S.T., Tian, R., Lu, J., and Tan, M., Cell Biosci., 2016, vol. 6, p.25.Google Scholar
  15. 15.
    Azarashvili, T., Krestinina, O., Odinokova, I., Evtodienko, Y., and Reiser, G., Cell Calcium, 2003, vol. 34, pp. 253–259.CrossRefPubMedGoogle Scholar
  16. 16.
    Azarashvili, T., Krestinina, O., Galvita, A., Grachev, D., Baburina, Y., Stricker, R., Evtodienko, Y., and Reiser, G., Am. J. Physiol. Cell Physiol., 2009, vol. 296, pp. C1428–C1439.CrossRefPubMedGoogle Scholar
  17. 17.
    Azarashvili, T., Krestinina, O., Galvita, A., Grachev, D., Baburina, Y., Stricker, R., and Reiser, G., J. Bioenerg. Biomembr., 2014, vol. 46, pp. 135–145.CrossRefPubMedGoogle Scholar
  18. 18.
    Azarashvili, T., Grachev, D., Krestinina, O., Evtodienko, Y., Yurkov, I., Papadopoulos, V., and Reiser, G., Cell Calcium, 2007, vol. 42, pp. 27–39.CrossRefPubMedGoogle Scholar
  19. 19.
    McEnery, M.W., Snowman, A.M., Trifiletti, R.R., and Snyder, S.H., Proc. Natl. Acad. Sci. U.S.A., 1992, vol. 89, pp. 3170–3174.CrossRefPubMedPubMedCentralGoogle Scholar
  20. 20.
    Pastorino, J.G., Simbula, G., Gilfor, E., Hoek, J.B., and Farber, J.L., J. Biol Chem., 1994, vol. 269, pp. 31041–31046.PubMedGoogle Scholar
  21. 21.
    Azarashvili, T., Krestinina, O., Yurkov, I., Evtodienko, Y., and Reiser, G., J. Neurochem., 2005, vol. 94, pp. 1054–1062.CrossRefPubMedGoogle Scholar
  22. 22.
    Krestinina, O., Azarashvili, T., Baburina, Y., Galvita, A., Grachev, D., Stricker, R., and Reiser, G., Neurochem. Int., 2015, vol. 80, pp. 41–50.CrossRefPubMedGoogle Scholar
  23. 23.
    Baburina, Y., Odinokova, I., Azarashvili, T., Akatov, V., Lemasters, J.J., and Krestinina, O., BBA-Biomembr., 2017, vol. 1859, pp. 94–103.CrossRefGoogle Scholar
  24. 24.
    Brydon, L., Roka, F., Petit, L., de Coppet, P., Tissot, M., Barrett, P., Morgan, P.J., Nanoff, C., Strosberg, A.D., and Jockers, R., Mol. Endocrinol., 1999, vol. 13, pp. 2025–2038.CrossRefPubMedGoogle Scholar
  25. 25.
    Niles, L.P. and Hashemi, F., Cell Mol. Neurobiol., 1990, vol. 10, pp. 553–558.CrossRefPubMedGoogle Scholar
  26. 26.
    Morgan, P.J., Barrett, P., Howell, H.E., and Helliwell, R., Neurochem. Int., 1994, vol. 24, pp. 101–146.CrossRefPubMedGoogle Scholar
  27. 27.
    Chan, A.S., Lai, F.P., Lo, R.K., Voyno-Yasenetskaya, T.A., Stanbridge, E.J., and Wong, Y.H., Cell. Signal., 2002, vol. 14, pp. 249–257.CrossRefPubMedGoogle Scholar
  28. 28.
    Schuster, C., Williams, L.M., Morris, A., Morgan, P.J., and Barrett, P., J. Neuroendocrinol., 2005, vol. 17, pp. 170–178.CrossRefPubMedGoogle Scholar
  29. 29.
    Petrosillo, G., Moro, N., Paradies, V., Ruggiero, F.M., and Paradies, G., J. Pineal Res., 2010, vol. 48, pp. 340–346.CrossRefPubMedGoogle Scholar
  30. 30.
    Krestinina, O.V., Kruglov, A.G., Grachev, D.E., Baburina, Y.L., Evtodienko, Y.V., Moshkov, D.A., Santalova, I.M., and Azarashvili, T.S., Biol. Membrany, 2010, vol. 27, pp. 177–183.Google Scholar
  31. 31.
    Reiser, G., Kunzelmann, U., Steinhilber, G., and Binmoller, F.J., Neurochem. Res., 1994, vol. 19, pp. 1479–1485.CrossRefPubMedGoogle Scholar
  32. 32.
    Afonso, S., Vanore, G., and Batlle, A., Free Radic. Res., 1999, vol. 31, pp. 161–170.CrossRefPubMedGoogle Scholar
  33. 33.
    Krestinina, O.V., Grachev, D.E., Odinokova, I.V., Reiser, G., Evtodienko, Y.V., and Azarashvili, T.S., Biochemistry (Moscow), 2009, vol. 74, pp. 421–429.CrossRefGoogle Scholar
  34. 34.
    Krestinina, O.V., Cand. Sc. (Biol.) Dissertation, Pushchino: ITEB RAN, 2005.Google Scholar
  35. 35.
    McEnery, M.W., Dawson, T.M., Verma, A., Gurley, D., Colombini, M., and Snyder, S.H., J. Biol. Chem., 1993, vol. 268, pp. 23289–23296.PubMedGoogle Scholar
  36. 36.
    Baburina, Y., Azarashvili, T., Grachev, D., Krestinina, O., Galvita, A., Stricker, R., and Reiser, G., Neurochem. Int., 2015, vol. 90, pp. 46–55.CrossRefPubMedGoogle Scholar
  37. 37.
    Krestinina, O.V, Odinokova, I.V., Baburina, Yu.L., and Azarashvili, T.S., Biol. Membr., 2017, vol. 34, pp. 42–47.Google Scholar
  38. 38.
    Myllykoski, M., Itoh, K., Kangas, S.M., Heape, A.M., Kang, S.U., Lubec, G., Kursula, I., and Kursula, P., J. Neurochem., 2012, vol. 123, pp. 515–524.CrossRefPubMedGoogle Scholar
  39. 39.
    Myllykoski, M., Seidel, L., Muruganandam, G., Raasakka, A., Torda, A.E., and Kursula, P., Brain Res., 2016, vol. 1641, pt. A, pp. 64–78.CrossRefPubMedGoogle Scholar
  40. 40.
    Baburina, Y.L., Gordeeva, A.E., Moshkov, D.A., Krestinina, O.V., Azarashvili, A.A., Odinokova, I.V., and Azarashvili, T.S., Biochemistry (Moscow), 2014, vol. 79, pp. 555–565.CrossRefGoogle Scholar
  41. 41.
    Baburina, Y., Odinokova, I., Azarashvili, T., Akatov, V., Lemasters, J.J., and Krestinina, O., Biochim. Biophys. Acta, 2017, vol. 1859, pp. 94–103.CrossRefPubMedGoogle Scholar
  42. 42.
    de Faria, Poloni J., Feltes, B.C., and Bonatto, D., Funct. Integr. Genomics, 2011, vol. 11, pp. 383–388.CrossRefGoogle Scholar
  43. 43.
    Williams, L.M., Drew, J.E., Bunnett, N.W., Grady, E., Barrett, P., Abramovich, D.R., Morris, A., and Slater, D., J. Neuroendocrinol., 2001, vol. 13, pp. 94–101.CrossRefPubMedGoogle Scholar
  44. 44.
    Sprinkle, T.J., Crit. Rev. Neurobiol., 1989, vol. 4, pp. 235–301.PubMedGoogle Scholar
  45. 45.
    Leung, A.W. and Halestrap, A.P., Biochim. Biophys. Acta, 2008, vol. 1777, pp. 946–952.CrossRefPubMedGoogle Scholar

Copyright information

© Pleiades Publishing, Ltd. 2018

Authors and Affiliations

  • O. V. Krestinina
    • 1
    • 2
  • Yu. L. Baburina
    • 1
  • I. V. Odinokova
    • 1
  • T. S. Azarashvili
    • 1
  • V. S. Akatov
    • 1
  1. 1.Institute of Theoretical and Experimental BiophysicsRussian Academy of SciencesPushchinoRussia
  2. 2.Pushchino, Moscow oblastRussia

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