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.
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Original Russian Text © O.V. Krestinina, Yu.L. Baburina, I.V. Odinokova, T.S. Azarashvili, V.S. Akatov, 2018, published in Neirokhimiya, 2018, Vol. 35, No. 1, pp. 35–41.
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Krestinina, O.V., Baburina, Y.L., Odinokova, I.V. et al. 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. Neurochem. J. 12, 33–40 (2018). https://doi.org/10.1134/S1819712418010051
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DOI: https://doi.org/10.1134/S1819712418010051