Scutellaria Barbata Flavonoids Regulate Protein Phosphorylation of Glycogen Synthase Kinase-3β and Tau in N2a Cells with Aβ25-35 -Induced Neurotoxicity Alzheimers
Journal Title: Online Journal of Complementary & Alternative Medicine (OJCAM) - Year 2018, Vol 1, Issue 1
Abstract
Alzheimer’s disease (AD) is a neurodegenerative disease caused by chronic or progressive structural damage of the brain. Neurofibrillary tangles (NFTs) induced by excessive phosphorylation of tau protein have toxity to neurons and to be one of the main pathogenesis of AD. Then, inhibiting the excessive phosphorylation of Tau protein is the key point to treat AD. While glycogen synthase kinase-3β (GSK-3β) plays an important role in causing abnormal hyperphosphorylation of AD-like Tau protein. It has been confirmed that GSK-3β can catalyze the hyperphosphorylation of Tau protein at several sites. Therefore, we research the regulatory effects of Scutellaria barbata flavonoids (SBF) on β-amyloid25-35 (Aβ25-35) induced Tau phosphorylation at Ser202, Ser199, Ser404, Ser214, Thr231 sites and regulatory mechanism by GSK-3β in mouse brain neuroblastoma cells(N2a). Our results showed that compared with control group, the protein expressive level of p-Tau (Ser202), p-Tau (Ser199), p-Tau (Ser404), p-Tau (Ser214) and p-GSK-3β (Tyr216) in model group were higher than those of control group (p< 0.05, p< 0.01). The expression of p-GSK-3β (Ser9) were markedly decreased (p< 0.01) and p-Tau (Thr231) has no obvious change (p>0.05) in model group, as compared with control group. Concerning to the inhibitor TWS119 group, p-Tau (Ser202), p-Tau (Ser199), p-Tau (Thr231) and p-GSK-3β (Ser9) protein expressive level increased (p< 0.01), p-Tau (Ser404), p-Tau (Ser214) protein expression decreased (p< 0.01) and p-GSK-3β (Tyr216) protein expressive level was not obviously, as compared with control group. Compared with model group, p-Tau (Ser202), p-Tau (Ser404), p-Tau (Ser214) and p-GSK-3β(Tyr216) protein expression level in Aβ25-35+TWS119 group significantly decreased (p< 0.01), p-Tau (Ser199), p-Tau (Thr231), p-GSK-3β(Ser9) A β25-35 + TWS119 set of protein expression levels or have no obvious change. Compared with Aβ25-35+ TWS119 group, each point of protein expression levels the SBF treatment group were decreased (p < 0.01 or p < 0.05), in addition to p-GSK-3β(Ser9) protein content increase. Our results indicate that SBF can inhibit the abnormal phosphorylation of Tau protein by regulating the activity of GSK-3β (Ser9) and decreasing the contents of Ser214 and Ser404 in Tau protein phosphorylation sites. Therefore, inhibiting the activity of GSK-3β may become one of the feasible and effective methods for the treatment of AD for achieving the goal of neuron protection.
Authors and Affiliations
Shang Yazhen
Keywords
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- EP ID EP620143
- DOI 10.33552/OJCAM.2018.01.000501
- Views 61
- Downloads 0
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