[Abstract Title]. - Society for Neuroscience

SY5Y and SH-SY5Y/pEGFP-LC3 cells. On the other hand, nicotine, the α7nAChR agonist,
enhanced the autophagic process and inhibited cell death following Aβ25-35 application. Nicotine
but not α-BTX increased primary hippocampal neuronal survival following Aβ treatment.
Confocal double-staining image shows that nicotine treatment enhanced the co-localization of
α7nAChR with autophagosome. These results suggest that α7nAChR may act as a carrier
binding with eAβ and internalized into cytoplasm and further detoxify Aβ-induced neurotoxicity
via autophagic degradation pathway. Taken together, these results suggest that autophagy
process plays a neuroprotective role against Aβ-induced neurotoxicity. Defect in autophagic
regulation or Aβ-α7nAChR transport system will impair the clearance of Aβ and enhance
neuronal death.
Disclosures: S. Hung, None; W. Huang, None; H. Liou, None; W. Fu, None.
Poster
244. Abeta Toxicity I
Time: Sunday, November 16, 2008, 1:00 pm - 5:00 pm
Program#/Poster#: 244.6/L11
Topic: C.01.c. Abeta toxicity
Support: Brain Korea 21
National Core Research Center
Title: Inhibition of soluble amyloid precursor protein alpha by amyloid beta in SH-SY5Y cells
Authors: M.-H. CHAE 1 , J.-Y. OH 1 , *H.-J. KIM 2 ;
1 Div. of Life & Pharmaceu. Sci., 2 Coll Pharmacy, Divi Life, Ewha Womans Univ., Seoul,
Republic of Korea
Abstract: Beta amlyoid peptide (βA4) is hypothesized to be toxic in Alzheimer's disease (AD)
by forming its soluble oligomeric and protofibrillar assemblies, however, the role of Aβoligomers
or mature Aβ-fibrils remains controversial and the underlying mechanisms of toxicity
and the neuronal cellular signaling cascades activated by βA4 are not fully understood. Cleavage
of amyloid precursor protin (APP) by α-secretase within the βA4 sequence results in the
secretion of a soluble N-terminal APP fragment (sAPPα). We have studied the mechanisms of
muscarinic recptor-mediated increase in sAPPα in human neuroblastoma (SH-SY5Y) cells. In
the present study, effects of Aβ-oligomers and Aβ-fibrils on both basal and muscarinic receptormediated
were investigated in SH-SY5Y cells. The cell viability and the level of phospho-AKT
were not changed by treatment of aggregated βA4 prepared with different incubation conditions.