Brain-derived neurotrophic factor exerts neuroprotective actions against amyloid β-induced apoptosis in neuroblastoma cells.
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. Aβ25-35was 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 Aβ25-35and 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.
Department of Neurosurgery, College of Medicine, Korea University, Seoul 136-701, Republic of Korea.
Jin Hee
JH
Kim
Akt; brain-derived neurotrophic factor; glycogen synthase kinase 3β; neuroblastoma cell; β-amyloid peptide