ArticleJournal of neural transmission (Vienna, Austria : 1996)2006
Activation of glycogen synthase kinase-3 induces Alzheimer-like tau hyperphosphorylation in rat hippocampus slices in culture.
Article in Journal of neural transmission (Vienna, Austria : 1996), 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 69 citations in OpenAlex.
- Advances in Alzheimer's disease: mechanistic insights and therapeutic targets.Science China. Life sciences · 2026Review
- Differential impact of eicosapentaenoic acid and docosahexaenoic acid in an animal model of Alzheimer's disease.Journal of lipid research · 2024Article
- A Combination of Heavy Metals and Intracellular Pathway Modulators Induces Alzheimer Disease-like Pathologies in Organotypic Brain Slices.Biomolecules · 2024Article
- Pathologically phosphorylated tau at S396/404 (PHF-1) is accumulated inside of hippocampal synaptic mitochondria of aged Wild-type mice.Scientific reports · 2021Article
- Targeting Inflammation, PHA-767491 Shows a Broad Spectrum in Protein Aggregation Diseases.Journal of molecular neuroscience : MN · 2020Article
- Extracellular Vesicles Isolated from Familial Alzheimer's Disease Neuronal Cultures Induce Aberrant Tau Phosphorylation in the Wild-Type Mouse Brain.Journal of Alzheimer's disease : JAD · 2019Article
- The Akt pathway in oncology therapy and beyond (Review).International journal of oncology · 2018Review
- Cornel Iridoid Glycoside Inhibits Tau Hyperphosphorylation via Regulating Cross-Talk Between GSK-3β and PP2A Signaling.Frontiers in pharmacology · 2018Article
- Differential Hyperphosphorylation of Tau-S199, -T231 and -S396 in Organotypic Brain Slices of Alzheimer Mice. A Model to Study Early Tau Hyperphosphorylation Using Okadaic Acid.Frontiers in aging neuroscience · 2018Article
- Erythrocytes as Potential Link between Diabetes and Alzheimer's Disease.Frontiers in aging neuroscience · 2017Review
- The Potential of Indole/Indolylquinoline Compounds in Tau Misfolding Reduction by Enhancement of HSPB1.CNS neuroscience & therapeutics · 2017Article
- Treadmill exercise decreases incidence of Alzheimer's disease by suppressing glycogen synthase kinase-3β expression in streptozotocin-induced diabetic rats.Journal of exercise rehabilitation · 2015Article
- Link between type 2 diabetes and Alzheimer's disease: from epidemiology to mechanism and treatment.Clinical interventions in aging · 2015Review
- Xanthoceraside attenuates tau hyperphosphorylation and cognitive deficits in intracerebroventricular-streptozotocin injected rats.Psychopharmacology · 2014Article
- Article
- NMDA receptor subunit composition determines beta-amyloid-induced neurodegeneration and synaptic loss.Cell death & disease · 2013Article
- Insulin: an emerging treatment for Alzheimer's disease dementia?Current neurology and neuroscience reports · 2012Review
- Synergistic influence of phosphorylation and metal ions on tau oligomer formation and coaggregation with α-synuclein at the single molecule level.Molecular neurodegeneration · 2012Article
- Lysophosphatidic acid induces neurite retraction in differentiated neuroblastoma cells via GSK-3β activation.Molecules and cells · 2011Article
- The marine natural-derived inhibitors of glycogen synthase kinase-3beta phenylmethylene hydantoins: In vitro and in vivo activities and pharmacophore modeling.Bioorganic & medicinal chemistry · 2009Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Formation of neurofibrillary tangle from hyperphosphorylated tau is one of the hallmark lesions seen in Alzheimer's disease (AD) brain, and neuronal deregulation of glycogen synthase kinase-3 (GSK-3) activity plays key role in tau hyperphosphorylation. In the present study, the role of GSK-3 on tau phosphorylation in hippocampus slice culture was examined by incubating the slice with wortmannin (WT), an inhibitor of phosphatidylinositol 3-kinase (PI3K) and GF-109203X (GFX), an inhibitor of protein kinase C (PKC). It was found that treatment of the slices with GFX or WT separately induced tau hyperphosphorylation both at Ser396/Ser404 (PHF-1) and Ser199/Ser202 (Tau-1) sites. The phosphorylation rate of tau at PHF-1 and Tau-1 epitopes was further increased when GFX and WT were used in combination, and at this condition, AD-like tau accumulation was observed. GSK-3 activity was significantly increased with a concurrently decreased level of inactivated form of GSK-3. Lithium chloride (LiCl), a GSK-3 inhibitor, prevented tau from WT- and GFX-induced hyperphosphorylation. It suggests that GSK-3 is regulated through PI3K and PKC pathway, and activation of GSK-3 not only induces hyperphosphorylation of tau but also leads to accumulation of tau in cultured rat brain slice.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.