کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2048047 1074056 2013 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Partitioning and confinement of GM1 ganglioside induced by amyloid aggregates
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
Partitioning and confinement of GM1 ganglioside induced by amyloid aggregates
چکیده انگلیسی


• Co-localization of GM1 with Aβ1–42 and amylin aggregates supported by in situ PLA.
• Tracking of single GM1 reveals interaction with Aβ oligomers and amylin aggregates.
• Amyloid aggregates interact generically with GM1 and decrease its mobility.

Growing evidence shows that GM1 ganglioside is involved in amyloid deposition and toxicity. By means of real-time single particle tracking, we show that amyloid oligomers and aggregates formed by Aβ1–42 and amylin, two peptides associated, respectively, with the development of Alzheimer’s disease and type II diabetes, interact with GM1 and decrease dramatically its lateral diffusion on the plasma membrane of living neuroblastoma cells. The confinement of GM1, a constituent of membrane rafts involved in neuroprotection, at the level of both types of amyloid aggregates can interfere with cell signaling pathways and contribute to the loss of neuroprotection.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 587, Issue 9, 2 May 2013, Pages 1385–1391
نویسندگان
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