Inhibition of glycogen synthase kinase-3β by Angelica sinensis extract decreases β-amyloid-induced neurotoxicity and tau phosphorylation in cultured cortical neurons

2010 ◽  
Vol 89 (3) ◽  
pp. 437-447 ◽  
Author(s):  
Zhaoxu Zhang ◽  
Ruiping Zhao ◽  
Jiping Qi ◽  
Shirong Wen ◽  
Ying Tang ◽  
...  
Keyword(s):  
Cortical Neurons ◽  
Glycogen Synthase ◽  
Tau Phosphorylation ◽  
Glycogen Synthase Kinase ◽  
Angelica Sinensis ◽  
Glycogen Synthase Kinase 3Β ◽  
Cultured Cortical Neurons ◽  
Β Amyloid

Tau phosphorylation in transgenic mice expressing glycogen synthase kinase-3β transgenes

Neuroreport ◽  
1997 ◽  
Vol 8 (15) ◽  
pp. 3251-3255 ◽  
Author(s):  
Janet Brownlees ◽  
Nicholas G. Irving ◽  
Jean-Pierre Brion ◽  
Barry J. M. Gibb ◽  
Uta Wagner ◽  
...  
Keyword(s):  
Transgenic Mice ◽  
Glycogen Synthase ◽  
Tau Phosphorylation ◽  
Glycogen Synthase Kinase ◽  
Glycogen Synthase Kinase 3Β

scholarly journals Tau phosphorylation by glycogen synthase kinase 3β modulates enzyme acetylcholinesterase expression

2020 ◽  
Author(s):  
María‐Ángeles Cortés‐Gómez ◽  
Esther Llorens‐Álvarez ◽  
Jordi Alom ◽  
Teodoro del Ser ◽  
Jesús Avila ◽  
...  
Keyword(s):  
Glycogen Synthase ◽  
Tau Phosphorylation ◽  
Glycogen Synthase Kinase ◽  
Glycogen Synthase Kinase 3Β

Glycogen synthase kinase-3β-mediated tau phosphorylation in cultured cell lines

Neuroreport ◽  
2003 ◽  
Vol 14 (2) ◽  
pp. 257-260 ◽  
Author(s):  
Chris Wing-Cheung Lee ◽  
Kwok-Fai Lau ◽  
Christopher C. J. Miller ◽  
Pang-Chui Shaw
Keyword(s):  
Cell Lines ◽  
Glycogen Synthase ◽  
Tau Phosphorylation ◽  
Glycogen Synthase Kinase ◽  
Glycogen Synthase Kinase 3Β ◽  
Cultured Cell

scholarly journals Leptin inhibits glycogen synthase kinase-3β to prevent tau phosphorylation in neuronal cells

2009 ◽  
Vol 455 (3) ◽  
pp. 191-194 ◽  
Author(s):  
Steven J. Greco ◽  
Sraboni Sarkar ◽  
Gemma Casadesus ◽  
Xiongwei Zhu ◽  
Mark A. Smith ◽  
...  
Keyword(s):  
Glycogen Synthase ◽  
Neuronal Cells ◽  
Tau Phosphorylation ◽  
Glycogen Synthase Kinase ◽  
Glycogen Synthase Kinase 3Β

Apolipoprotein E and Reelin ligands modulate tau phosphorylation through an Apolipoprotein E receptor/disabled‐1/glycogen synthase kinase‐3β cascade

2002 ◽  
Vol 17 (2) ◽  
pp. 295-297 ◽  
Author(s):  
Nobutaka Ohkubo ◽  
Young‐Don Lee ◽  
Atsuyuki Morishima ◽  
Toshio Terashima ◽  
Satoshi Kikkawa ◽  
...  
Keyword(s):  
Apolipoprotein E ◽  
Glycogen Synthase ◽  
Tau Phosphorylation ◽  
Glycogen Synthase Kinase ◽  
Glycogen Synthase Kinase 3Β

scholarly journals ERK1/2 Antagonizes Glycogen Synthase Kinase-3β-induced Apoptosis in Cortical Neurons

2002 ◽  
Vol 277 (51) ◽  
pp. 49577-49584 ◽  
Author(s):  
Michal Hetman ◽  
Shih-Ling Hsuan ◽  
Agata Habas ◽  
Matthew J. Higgins ◽  
Zhengui Xia
Keyword(s):  
Cortical Neuron ◽  
Cortical Neurons ◽  
Glycogen Synthase ◽  
Glycogen Synthase Kinase ◽  
Glycogen Synthase Kinase 3Β ◽  
Phosphatidylinositol 3 Kinase ◽  
Pi3k Activation ◽  
Induced Apoptosis ◽  
Neuron Apoptosis ◽  
Constitutively Active

Inhibition of glycogen synthase kinase-3β (GSK3β) is one of the mechanisms by which phosphatidylinositol 3-kinase (PI3K) activation protects neurons from apoptosis. Here, we report that inhibition of ERK1/2 increased the basal activity of GSK3β in cortical neurons and that both ERK1/2 and PI3K were required for brain-derived neurotrophic factor (BDNF) suppression of GSK3β activity. Moreover, cortical neuron apoptosis induced by expression of recombinant GSK3β was inhibited by coexpression of constitutively active MKK1 or PI3K. Activation of both endogenous ERK1/2 and PI3K signaling pathways was required for BDNF to block apoptosis induced by expression of recombinant GSK3β. Furthermore, cortical neuron apoptosis induced by LY294002-mediated activation of endogenous GSK3β was blocked by expression of constitutively active MKK1 or by BDNF via stimulation of the endogenous ERK1/2 pathway. Although both PI3K and ERK1/2 inhibited GSK3β activity, neither had an effect on GSK3β phosphorylation at Tyr-216. Interestingly, PI3K (but not ERK1/2) induced the inhibitory phosphorylation of GSK3β at Ser-9. Significantly, coexpression of constitutively active MKK1 (but not PI3K) still suppressed neuronal apoptosis induced by expression of the GSK3β(S9A) mutant. These data suggest that activation of the ERK1/2 signaling pathway protects neurons from GSK3β-induced apoptosis and that inhibition of GSK3β may be a common target by which ERK1/2 and PI3K protect neurons from apoptosis. Furthermore, ERK1/2 inhibits GSK3β activity via a novel mechanism that is independent of Ser-9 phosphorylation and likely does not involve Tyr-216 phosphorylation.

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