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Vol 50(2016) N 6 p. 930-932; DOI 10.1134/S0026893316060236  M.M. Yurinskaya1,2, V.A. Mit'kevich1, M.B. Evgen'ev1,2, A.A. Makarov1, M.G. Vinokurov2* Heat-shock protein HSP70 reduces the secretion of TNFα by neuroblastoma cells and human monocytes induced with beta-amyloid peptides 1Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, 119991 Russia2Institute of Cell Biophysics, Russian Academy of Sciences, Pushchino, Moscow Region, 142290 Russia *m_vinokurov@mail.ru Received - 2016-03-30; Accepted - 2016-04-29 The progress of neurodegeneration in Alzheimer's disease is closely associated with inflammatory processes in the brain tissues induced by beta-amyloid peptides (Aβ). In this paper, we showed that Aβ(1-42) and isoAβ(1-42) in human neuroblastoma cells SK-N-SH and promonocyte THP-1 activated the production of tumor necrosis factor (TNFα). Notably, isoAβ(1-42) had the strongest effect on the increase in the level of TNFα. The addition of recombinant heat-shock protein HSP70 reduces TNFα production induced by Aβ, which leads to a decrease in neuronal cell damage at the organism level. HSP70, β-amyloid peptide, Аβ(1-42), TNFα, neuroblastoma cells SK-N-SH, promonocyte cells THP-1 |
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