Ellagic acid promotes Abeta42 fibrillization and inhibits Abeta42-induced neurotoxicity
| Autor: | Xi Zhang, Xiao-xia Sun, Shi-gao Yang, Min Zhao, Xue-ting Du, Rui-tian Liu, Gui-yuan Sun, Ying Feng |
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| Rok vydání: | 2009 |
| Předmět: |
Biophysics
Pharmacology Fibril Biochemistry Oligomer Protein Structure Secondary Cell Line chemistry.chemical_compound Western blot Ellagic Acid Alzheimer Disease mental disorders medicine Humans Molecular Biology Amyloid beta-Peptides medicine.diagnostic_test Neurotoxicity Cell Biology medicine.disease In vitro Peptide Fragments nervous system diseases chemistry Polyphenol Cell culture Ellagic acid |
| Zdroj: | Biochemical and biophysical research communications. 390(4) |
| ISSN: | 1090-2104 |
| Popis: | Smaller, soluble oligomers of beta-amyloid (Abeta) play a critical role in the pathogenesis of Alzheimer's disease (AD). Selective inhibition of Abeta oligomer formation provides an optimum target for AD therapy. Some polyphenols have potent anti-amyloidogenic activities and protect against Abeta neurotoxicity. Here, we tested the effects of ellagic acid (EA), a polyphenolic compound, on Abeta42 aggregation and neurotoxicity in vitro. EA promoted Abeta fibril formation and significant oligomer loss, contrary to previous results that polyphenols inhibited Abeta aggregation. The results of transmission electron microscopy (TEM) and Western blot displayed more fibrils in Abeta42 samples co-incubated with EA in earlier phases of aggregation. Consistent with the hypothesis that plaque formation may represent a protective mechanism in which the body sequesters toxic Abeta aggregates to render them harmless, our MTT results showed that EA could significantly reduce Abeta42-induced neurotoxicity toward SH-SY5Y cells. Taken together, our results suggest that EA, an active ingredient in many fruits and nuts, may have therapeutic potential in AD. |
| Databáze: | OpenAIRE |
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