Abstract：
:Alzheimer's disease (AD) is pathologically characterized by presence of senile plaques in the hippocampus, which are composed mainly of extracellular deposition of a polypeptide known as the beta amyloid, the Aβ. It has been demonstrated on numerous occasions that it was the deposition and aggregation of this Aβ peptide that cause neuronal dysfunction and even finally, the dementia. Lowering the deposition of Aβ or decreasing its neurotoxicity has long been one of the purposes of AD therapy. In previous study, we reported that protein kinase C (PKC) activator TPPB could regulate APP processing by increasing α-secretase activity. In this study we further investigated the potential neuroprotective effect of TPPB against Aβ(25-35)-induced neurotoxicity in PC12 cells. The results indicated that TPPB at concentration of 1 μM could antagonize Aβ(25-35) induced cell damage as evidenced by MTT assays, LDH release and by morphological changes. Furthermore, the neuroprotection in cell viability can be blocked by inhibitors of PKC, Akt and MAPK. The experiment also indicated that TPPB could increase the phosphorylation of Akt, PKC, MARCKS and MAPK, which were inhibited by Aβ(25-35) treatment. Finally, TPPB inhibited the activation of caspase-3 induced by Aβ(25-35). Taken together, the experiment here implies that TPPB has a role against Aβ(25-35)-induced neurotoxicity in PC12 cells and may suggest its therapeutic potential in AD.
journal_name
Neurochem Resjournal_title
Neurochemical researchauthors
Yang HQ,Li X,Yang WM,Feng SM,Ma JJdoi
10.1007/s11064-012-0846-6subject
Has Abstractpub_date
2012-10-01 00:00:00pages
2213-21issue
10eissn
0364-3190issn
1573-6903journal_volume
37pub_type
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