Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
6022829 | Neurobiology of Disease | 2011 | 10 Pages |
Abstract
âºNaïve primary microglia internalized oligomeric amyloid-β peptide (oAβ) in a time- and dose-dependent manner. âºKnockdown of scavenger receptor type-A, but not CD36 by small interfering RNAs (siRNAs) attenuated oAβ internalization by primary microglia. âºLysosomal cysteine protease including cathepsin B, but neither serine nor aspartate proteases, degraded internalized oAβ by primary microglia. âºEpoxomicin, a specific proteasome inhibitor, failed to prevent oAβ degradation in microglia. âºNeprilysin, matrix metalloproteinases, and insulin degrading enzyme were not involved in oAβ degradation in microglia.
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Authors
Cheng-Ning Yang, Young-Ji Shiao, Feng-Shiun Shie, Bo-Shen Guo, Pei-Hao Chen, Chi-Yuan Cho, Yi-Jen Chen, Fong-Lee Huang, Huey-Jen Tsay,