O. G. Tatarnikova - Master's Student, Moscow State University n.a. M.V. Lomonosov; Engineer, ICB RAS (Pushchino, Moscow region). E-mail: olga.psn@mail.ru
A. N. Klenyaeva - Post-graduate Student, ICB RAS (Pushchino, Moscow region) E-mail: a-lina-a@yandex.ru
M. A. Orlov - Master's Student, Moscow State University n.a. M.V. Lomonosov. E-mail: fire-vortex@mail.ru
M. M. Panchenko - Post-graduate Student, ICB RAS (Pushchino, Moscow region). E-mail: mmpanchenko@gmail.com
A. I. Sergeev - Engineer, ICB RAS (Pushchino, Moscow region). E-mail: sergeev.bio@gmail.com
N. V. Bobkova - Ph.D. (Biol.), Head of Laboratory, ICB RAS (Pushchino, Moscow region). E-mail: nbobkova@mail.ru

Until recently beta-amyloid (Аβ) was assigned a central role in the pathogenesis of Alzheimer's disease (AD), and the Tau-protein was secondary. However, the number of tangles, composed of Tau-protein filaments, but not amyloid plaques, correlates with the loss of neurons and the degree of cognitive deficit in the case of AD [1]. The interest in the Tau protein grows not only because of failures in the development of therapeutic agents against AD which target was amyloid, but also because there are new data showing its role in the destabilization of neuronal transport system in AD [2], its localization in the cellular membrane, the possibility of its secretion outside of the cell, and finally the prion-like ability of tau protein toxic form to "infect" healthy cells and promoting the disease oligomeric forms of these proteins on neuronal survival [3]. Research of interaction of secreted oligomeric forms of these proteins effects and its influence on cell survivability is actual for now. Previously we developed in vitro cell model of process of formation of the fibrillar Tau-protein forms by line of cell 3T3-4R-Tay, constantly expressing human Tau-protein (4R-form), obtained on the basis of the parental line of NIH-3T3 cells, mice fibroblasts [4]. In experiment with co-cultivation 3T3-4R-Tau cells with newborn rats primary neuronal hippocampal cell cultures showed an increase increase in non-viable cells number of the hippocampus, that indicating to toxicity of Tau-protein. The preincubation of 3T3-4R-Tau cells with Аβ (1-42) increased their toxicity. This is indicated by the massive extinction of hippocampal cells. Thus, we have established toxic effect of βA mediated through protein Tau, which allows for new insights into the pathogenesis of AD. Developed cell system suitable for screening of pharmacological agents to prevent the formation of toxic forms of Tau-protein and Аβ, which is the most promising course for drug development treatment of AD. This work was supported by the Program for Basic Research of RAS, 2014.