التفاصيل البيبلوغرافية
| العنوان: |
FLIM Imaging Reveals a Toxicogenic Interaction between Amyloid-β and Apolipoprotein-E. |
| المؤلفون: |
Dey, Arpan, Verma, Aditi, Bhaskar, Uchit, Sarkar, Bidyut, Kallianpur, Mamata, Vishvakarma, Vicky, Das, Anand Kant, Garai, Kanchan, Mukherjee, Odity, Ishii, Kunihiko, Tahara, Tahei, Maiti, Sudipta |
| المصدر: |
Indian Journal of Medical & Paediatric Oncology; 2024 Supplement 1, Vol. 45, pS1-S16, 16p |
| مصطلحات موضوعية: |
AMYLOID plaque, APOLIPOPROTEIN E4, OLIGOMERS, DRUG discovery |
| مستخلص: |
This article, titled "FLIM Imaging Reveals a Toxicogenic Interaction between Amyloid-β and Apolipoprotein-E," explores the role of apolipoprotein E (ApoE) in Alzheimer's disease (AD) pathology. The researchers used fluorescence lifetime imaging to study the interaction between reporter fluorescent Aβ oligomers and ApoE-containing cells. They discovered a new species of Aβ oligomer with a distinct lifetime, which varied across different cell types and correlated with ApoE concentrations. The researchers also found that these modified Aβ oligomers had an elevated affinity for lipid bilayers and exhibited conformational changes. The addition of an Aβ-ApoE interaction inhibitor reduced both the lifetime modification and oligomer toxicity, suggesting a direct role of ApoE-induced Aβ in AD. This study provides insights into the toxic transformation of intracellular Aβ oligomers induced by ApoE and may contribute to the development of novel AD drug discovery platforms. [Extracted from the article] |
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| قاعدة البيانات: |
Complementary Index |