Interaction of Myelin Basic Protein and 2′,3′-Cyclic Nucleotide Phosphodiesterase with Mitochondria

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Yu. L. Baburina^*, A. E. Gordeeva, D. A. Moshkov^#, O. V. Krestinina, A. A. Azarashvili, I. V. Odinokova, and T. S. Azarashvili^*

Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia; fax: (4967) 330-553; E-mail: azartam@yandex.ru; byul@rambler.ru

^* To whom correspondence should be addressed.

^# Deceased.

Received December 11, 2013; Revision received February 24, 2014

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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 nonsynaptic 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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KEY WORDS: mitochondria, myelin, permeability transition pore, myelin basic protein, CNPase

DOI: 10.1134/S0006297914060091

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