Abstract
The content and distribution of myelin basic protein (MBP) isoforms (17 and 21.5 kDa) as well as 2′,3′-cyclic nucleotide-3′-phosphodiesterase (CNPase) were determined in mitochondrial fractions (myelin fraction, synaptic and non-synaptic mitochondria) obtained after separation of brain mitochondria by Percoll density gradient. All the fractions could accumulate calcium, maintain membrane potential, and initiate the opening of the permeability transition pore (mPTP) in response to calcium overloading. Native mitochondria and structural contacts between membranes of myelin and mitochondria were found in the myelin fraction associated with brain mitochondria. Using Western blot, it was shown that addition of myelin fraction associated with brain mitochondria to the suspension of liver mitochondria can lead to binding of CNPase and MBP, present in the fraction with liver mitochondria under the conditions of both closed and opened mPTP. However, induction of mPTP opening in liver mitochondria was prevented in the presence of myelin fraction associated with brain mitochondria (Ca2+ release rate was decreased 1.5-fold, calcium retention time was doubled, and swelling amplitude was 2.8-fold reduced). These results indicate possible protective properties of MBP and CNPase.
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Abbreviations
- CNPase:
-
2′,3′-cyclic nucleotide-3′-phosphodiesterase
- MBP:
-
myelin basic protein
- MFAM:
-
myelin fraction associated with mitochondria
- mPTP:
-
mitochondrial permeability transition pore
- PLP:
-
proteolipid protein
References
Gorman, A. M. (2008) J. Cell Mol. Med., 12, 2263–2280.
Calabrese, V., Scapagnini, G., Giuffrida Stella, A. M., Bates, T. E., and Clark, J. B. (2001) Neurochem. Res., 26, 739–764.
Aliev, G., Palacios, H. H., Walrafen, B., Lipsitt, A. E., Obrenovich, M. E., and Morales, L. (2009) Int. J. Biochem. Cell Biol., 41, 1989–2004.
Kolehmainen, E., Knip, M., and Leppaluoto, J. (1990) Acta Physiol. Scand., 139, 493–501.
Kolehmainen, E. (1996) J. Neurol. Sci., 141, 19–26.
Kolehmainen, E., and Sormunen, R. (1998) Pancreas, 16, 176–188.
Baburina, Yu. L., Krestinina, O. V., and Azarashvili, T. S. (2013) Neurochem. J., 7, 1–15.
Huttemann, M., Zhang, Z., Mullins, C., Bessert, D., Lee, I., Nave, K. A., Appikatla, S., and Skoff, R. P. (2009) Neuro, 1.
Azarashvili, T., Krestinina, O., Galvita, A., Grachev, D., Baburina, Y., Stricker, R., Evtodienko, Y., and Reiser, G. (2009) Am. J. Physiol. Cell Physiol., 296, 1428–1439.
Ghandour, M. S., Feutz, A. C., Jalabi, W., Taleb, O., Bessert, D., Cypher, M., Carlock, L., and Skoff, R. P. (2002) Glia, 40, 300–311.
Knapp, P. E. (1996) Dev. Neurosci., 18, 297–308.
Laursen, R. A., Samiullah, M., and Lees, M. B. (1983) FEBS Lett., 161, 71–74.
Azarashvili, T. S., Tyynela, J., Odinokova, I. V., Grigorjev, P. A., Baumann, M., Evtodienko, Y. V., and Saris, N. E. (2002) J. Bioenerg. Biomembr., 34, 279–284.
Azarashvily, T. S., Tyynela, J., Baumann, M., Evtodienko, Y. V., and Saris, N. E. (2000) Biochem. Biophys. Res. Commun., 270, 741–744.
Krestinina, O. V., Grachev, D. E., Odinokova, I. V., Reiser, G., Evtodienko, Y. V., and Azarashvili, T. S. (2009) Biochemistry (Moscow), 74, 421–429.
Azarashvili, T., Odinokova, I., Bakunts, A., Ternovsky, V., Krestinina, O., Tyynela, J., and Saris, N. E. (2014) Cell Calcium, 55, 69–77.
Bonora, A., Bononi, M. E., De, C., Giorgi, M., Lebiedzinska, S., Marchi, S., Patergnani, A., Rimessi, J. M., Suski, A., Wojtala, M. R., Wieckowski, G., Kroemer, L., and Galluzzi, P. (2013) Cell Cycle, 12, 674–683.
Krestinina, O., Makarov, P., Baburina, Yu., Gordeeva, A., and Azarashvili, T. (2013) Neurochem. J., 7, 284–290.
Sims, N. R. (1990) J. Neurochem., 55, 698–707.
Laemmli, U. K. (1970) Nature, 227, 680–685.
Krestinina, O. V., Kruglov, A. G., Grachev, D. E., Baburina, Yu. L., Evtodienko, Yu. V., Moshkov, D. A., Santalova, I. M., and Azarashvili, T. S. (2010) Biochemistry (Moscow), Ser. A: Membrane and Cell Biology, 4, 180–186.
Azarashvili, T., Baburina, Y., Grachev, D., Krestinina, O., Evtodienko, Y., Stricker, R., and Reiser, G. (2011) Am. J. Physiol. Cell Physiol., 300, 707–720.
Kim, T., and Pfeiffer, S. E. (1999) J. Neurocytol., 28, 281–293.
Lee, J., O’Neill, R. C., Park, M. W., Gravel, M., and Braun, P. E. (2006) Mol. Cell Neurosci., 31, 446–462.
Sprinkle, T. J. (1989) Crit. Rev. Neurobiol., 4, 235–301.
Agrawal, H. C., Sprinkle, T. J., and Agrawal, D. (1990) Biochem. Biophys. Res. Commun., 170, 817–823.
Gravel, M., DeAngelis, D., and Braun, P. E. (1994) J. Neurosci. Res., 38, 243–247.
Gravel, M., Robert, F., Kottis, V., Gallouzi, I. E., Pelletier, J., and Braun, P. E. (2009) J. Neurosci. Res., 87, 1069–1079.
Panfoli, I., Ravera, S., Bruschi, M., Candiano, G., and Morelli, A. (2011) Expert. Rev. Proteom., 8, 231–239.
Morelli, A., Ravera, S., and Panfoli, I. (2011) Cell Biochem. Biophys., 61, 179–187.
Ravera, S., Panfoli, I., Calzia, D., Aluigi, M. G., Bianchini, P., Diaspro, A., Mancardi, G., and Morelli, A. (2009) J. Biochem. Cell Biol., 41, 1581–1591.
Harris, J. J., and Attwell, D. (2013) J. Cereb. Blood Flow Metab., 33, 33–36.
Karthigasan, J., and Kirschner, D. A. (1988) J. Neurochem., 51, 228–236.
Rand, R. P., Fuller, N. L., and Lis, L. J. (1979) Nature, 279, 258–260.
Zambonin, J. L., Zhao, C., Ohno, N., Campbell, G. R., Engeham, S., Ziabreva, I., Schwarz, N., Lee, S. E., Frischer, J. M., Turnbull, D. M., Trapp, B. D., Lassmann, H., Franklin, R. J., and Mahad, D. J. (2011) Brain, 134, 1901–1913.
Beest, M., and Hoekstra, D. (1993) Eur. J. Biochem., 211, 689–696.
Smith, G. S., Seymour, L. V., Boggs, J. M., and Harauz, G. (2012) Biochem. Biophys. Res. Commun., 422, 670–675.
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Original Russian Text © Yu. L. Baburina, A. E. Gordeeva, D. A. Moshkov, O. V. Krestinina, A. A. Azarashvili, I. V. Odinokova, T. S. Azarashvili, 2014, published in Biokhimiya, 2014, Vol. 79, No. 6, pp. 705–717.
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Baburina, Y.L., Gordeeva, A.E., Moshkov, D.A. et al. Interaction of myelin basic protein and 2′,3′-cyclic nucleotide phosphodiesterase with mitochondria. Biochemistry Moscow 79, 555–565 (2014). https://doi.org/10.1134/S0006297914060091
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DOI: https://doi.org/10.1134/S0006297914060091