Abstract
Alzheimer’s disease (AD) brains demonstrate decreased levels of brain-derived neurotrophic factor (BDNF) and increased levels of β-amyloid peptide (Aβ), which is neurotoxic. The present study assessed the impact of BDNF on the toxic effects of Aβ25–35-induced apoptosis and the effects on BDNF-mediated signaling using the MTT assay, western blotting and reverse transcription quantitative polymerase chain reaction. Aβ25–35 was found to induce an apoptosis, dose-dependent effect on SH-SY5Y neuroblastoma cells, which peaked at a concentration of 20 μM after 24 h. A combination of Aβ25–35 and BDNF treatment increased the levels of Akt and decreased the level of glycogen synthase kinase-3β (GSK3β) in SH-SY5Y neuroblastoma cells. These findings indicated that BDNF administration exerted a neuroprotective effect against the toxicity of the Aβ25–35-induced apoptosis in these cells, which was accompanied by phosphoinositide 3-kinase/Akt activation and GSK3β phosphorylation. The mechanisms and signaling pathways underlying neuronal degeneration induced by the Aβ peptide remain to be further elucidated.
Highlights
Alzheimer's disease (AD) is a neurodegenerative disorder of the human brain and is associated with loss of memory and cognitive abilities [1]
In AD brains, there is an abundance of two abnormal structures: Senile plaques composed of β‐amyloid peptide (Aβ), that are deposited outside neuronal bodies, and neurofibrillary tangles, which are aggregates of hyperphosphorylated tau proteins that bind to microtubules within the neurons [3]
Human SH‐SY5Y neuroblastoma cells were maintained in Dulbecco's modified Eagles's medium (DMEM) and F‐12 (Gibco‐BRL, Gaithersburg, MD, USA) supplemented with 10% fetal bovine serum (FBS; HyClone, Logan, UT, USA) in a humidified atmosphere of 5% CO2 and 95% air at 37 ̊C
Summary
Alzheimer's disease (AD) is a neurodegenerative disorder of the human brain and is associated with loss of memory and cognitive abilities [1]. AD is characterized by amyloid plaques, neurofibrillary tangles and neuronal loss [2]. In AD brains, there is an abundance of two abnormal structures: Senile plaques composed of β‐amyloid peptide (Aβ), that are deposited outside neuronal bodies, and neurofibrillary tangles, which are aggregates of hyperphosphorylated tau proteins that bind to microtubules within the neurons [3]. Synaptic dysfunction in AD may be caused by accumulation of aggregated amyloid peptides [3]. Aβ peptides induce cell death, decrease survival rate, and increase inflammation, oxidative stress and neurotoxicity in in vitro models used to study AD [5,6]
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