کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10770612 | 1050834 | 2005 | 5 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
GM1 ganglioside-mediated accumulation of amyloid β-protein on cell membranes
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
The conversion of soluble, nontoxic amyloid β-protein (Aβ) to aggregated, toxic Aβ is the key step in the development of Alzheimer's disease. Liposomal studies proposed that Aβ specifically recognizes a cholesterol-dependent cluster of monosialoganglioside GM1 and a conformationally altered form of Aβ promotes the aggregation of the protein. In this study, the accumulation of Aβ on living cells was investigated for the first time. The interaction of fluorescein-labeled Aβ (FL-Aβ) with rat pheochromocytoma PC12 cells was visualized using confocal laser microscopy. FL-Aβ was found to colocalize with GM1-rich domains on cell membranes and to accumulate in a concentration- and time-dependent manner, leading to cytotoxicity. Cholesterol depletion significantly reduced Aβ accumulation. These observations corroborate the GM1-mediated Aβ accumulation model.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 328, Issue 4, 25 March 2005, Pages 1019-1023
Journal: Biochemical and Biophysical Research Communications - Volume 328, Issue 4, 25 March 2005, Pages 1019-1023
نویسندگان
Masaki Wakabayashi, Takuma Okada, Yasunori Kozutsumi, Katsumi Matsuzaki,