IL-5 blocks apoptosis and tau hyperphosphorylation induced by Aβ25–35 peptide in PC12 cells

• Yuanyuan Zhou ^[1] ; Chaoyan Li ^[1] ; Deheng Li ^[1] ; Yaping Zheng ^[1] ; Jin Wang ^[1]
  1. [1] Luohe Medical College

     Luohe Medical College

     China

     
• Localización: Journal of physiology and biochemistry, ISSN-e 1877-8755, ISSN 1138-7548, Vol. 73, Nº. 2, 2017, págs. 259-266
• Idioma: inglés
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• Resumen

  • The primary features of Alzheimer’s disease (AD) are extracellular amyloid plaques consisting mainly of deposits of amyloid β (Aβ) peptides and intracellular neurofibrillary tangles (NFTs). Sets of evidence suggest that interleukin-5 (IL-5) is involved in the pathogenesis of AD. Herein, we investigated the protective role of IL-5 in PC12 cells, to provide new insights into understanding this disease. Western blot was employed to assess the protein levels of Bax and phospho-tau as well as phospho-JAK2; MTT assay was performed to decipher cell viability. Treatment of IL-5 decreased Aβ25–35-induced tau phosphorylation and apoptosis, effects blunted by JAK2 inhibition. IL-5 prevents Aβ25–35-evoked tau protein hyperphosphorylation and apoptosis through JAK2 signaling.