Effect of truncated-ApoE4 overexpression on tau phosphorylation in cultured N2a cells
| Autor: | Juan Chen, Youmei Feng, Jie Zhou |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
Recombinant Fusion Proteins
Apolipoprotein E4 Blotting Western Green Fluorescent Proteins Biomedical Engineering tau Proteins Transfection Biochemistry Biomaterials Glycogen Synthase Kinase 3 Neuroblastoma GSK-3 Cell Line Tumor mental disorders Genetics Animals Phosphorylation Glycogen synthase Sequence Deletion Earth-Surface Processes biology Molecular biology In vitro Blot Cell culture Lipofectamine biology.protein lipids (amino acids peptides and proteins) human activities |
| Zdroj: | Journal of Huazhong University of Science and Technology [Medical Sciences]. 26:272-274 |
| ISSN: | 1993-1352 1672-0733 |
| DOI: | 10.1007/bf02829548 |
| Popis: | The carboxyl-terminal amino acids 272-299-truncated apoE4 (delta272-299) is the main fragments of apoE4 hydrolysate in neurons. The effects of truncated-ApoE4 (delta272-299) overexpression on tau phosphorylation in cultured N2a cells were investigated. The truncated-apoE4 (delta272-299) cDNA was subcloned into pEGFP-c3 to form recombinant pEGFP-T-apoE4. pEGFP-c3, pEGFP-T-apoE4 and pEGFP-apoE4 were transfected into N2a cells respectively by lipofectamine 2000 method. After 24--48 h, tau phosphorylation was detected by Western blot assay and glycogen synthase kinase-3 (GSK-3) activity by using GSK-3 activity assay. The results showed that the overexpression of both full length-apoE4 and truncated apoE4 fragments in N2a cells induced a dramatic increase in phosphorylation of tau at Ser202 sites and the activation of GSK-3 as compared with untransfected cells, most significantly in the cells transfected with pEGFP-T-apoE4 (P0.05). It was concluded that in vitro overexpression of truncated-ApoE4 (delta272-299) can result in tau hyperphosphorylation in N2a cells by activating GSK-3, suggesting truncated-ApoE4 (delta272-299) might contribute the pathogenesis of Alzheimer disease. |
| Databáze: | OpenAIRE |
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