Publication in refereed journal
香港中文大学研究人员 ( 现职)
| 吴浩强教授 (病理解剖及细胞学系) |
| 包立怡教授 (药剂学院) |
全文
| 数位物件识别号 (DOI) http://dx.doi.org/10.1016/j.mcn.2009.01.006 |
引用次数
Web of Sciencehttp://aims.cuhk.edu.hk/converis/portal/Publication/23WOS source URL
Scopushttp://aims.cuhk.edu.hk/converis/portal/Publication/28Scopus source URL
其它资讯
摘要The endoplasmic reticulum (ER) is a dynamic multifunction organelle that is responsible for Ca2+ homeostasis, protein folding, post-translational modification, protein degradation, and transportation of nascent proteins. Disruption of ER architecture might affect the normal physiology of the cell. In yeast, expansion of the ER is observed under unfolded protein response (UPR) and subsequently induces autophagy initiated from the ER. Here, we found that soluble low molecular weight of Aβ disrupted the anchoring between ER and microtubules (MT) and induced collapse of ER. In addition, it decreased the stability of MT. Subsequently, low molecular weight Aβ triggered autophagy and enhanced lysosomal degradation, as shown by electron microscopy and live-cell imaging. Dysfunction of ER can be further proved in postmortem AD brain and transgenic mice bearing APP Swedish mutation by immunohistochemical analysis of calreticulin. Treatment with Taxol, a MT-stabilizing agent, could partially inhibit collapse of the ER and induction of autophagy. The results show that Aβ-induced disruption of MT can affect the architecture of the ER. Collapse/aggregation of the ER may play an important role in Aβ peptide-triggered neurodegenerative processes. ? 2009 Elsevier Inc. All rights reserved.
着者Lai C.S.-W., Preisler J., Baum L., Lee D.H.-S., Ng H.-K., Hugon J., So K.-F., Chang R.C.-C.
期刊名称MOLECULAR AND CELLULAR NEUROSCIENCE
出版年份2009
月份5
日期1
卷号41
期次1
出版社Academic Press
出版地United States
页次32 - 43
国际标準期刊号1044-7431
电子国际标準期刊号1095-9327
语言英式英语
关键词Alzheimer's disease, Autophagy, Cytoskeleton, Endoplasmic reticulum, β-amyloid
