REVIEW: Beta-Amyloid and Tau-Protein: Structure, Interaction, and Prion-Like Properties

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O. G. Tatarnikova^1,2*, M. A. Orlov¹, and N. V. Bobkova^1*

¹Institute of Cell Biophysics, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia; E-mail: nbobkova@mail.ru

²Pushchino State Natural Research Institute, 142290 Pushchino, Moscow Region, Russia; E-mail: olga.psn@mail.ru

^* To whom correspondence should be addressed.

Received October 10, 2015

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During the last twenty years, molecular genetic investigations of Alzheimer’s disease (AD) have significantly broadened our knowledge of basic mechanisms of this disorder. However, still no unambiguous concept on the molecular bases of AD pathogenesis has been elaborated, which significantly impedes the development of AD therapy. In this review, we analyze issues concerning processes of generation of two proteins (β-amyloid peptide and Tau-protein) in the cell, which are believed to play the key role in AD genesis. Until recently, these agents were considered independently of each other, but in light of the latest studies, it becomes clear that it is necessary to study their interaction and combined effects. Studies of mechanisms of toxic action of these endogenous compounds, beginning from their interaction with known receptors of main neurotransmitters to specific peculiarities of functioning of signal intracellular pathways upon development of this pathology, open the way to development of new pharmaceutical substances directed concurrently on key mechanisms of interaction of toxic proteins inside the cell and on the pathways of their propagation in the extracellular space.

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KEY WORDS: Alzheimer’s disease, β-amyloid, Tau-protein, APP, presenilins, prion-like mechanism of AD

DOI: 10.1134/S000629791513012X

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