d-Ribosylated Tau forms globular aggregates with high cytotoxicity
文献类型：期刊论文
| 作者 | Chen, Lan1; Wei, Yan1,2; Wang, Xueqing1; He, Rongqiao1,3; R. Q. He |
| 刊名 | CELLULAR AND MOLECULAR LIFE SCIENCES
 |
| 出版日期 | 2009-08-01 |
| 卷号 | 66期号:15页码:2559-2571 |
| 关键词 | D-Ribose Tau protein Glycation Aggregation Cytotoxicity |
| ISSN号 | 1420-682X |
| 文献子类 | Article |
| 英文摘要 | Although the glycation of Tau that is involved in paired helical filament formation in Alzheimer's disease has been widely studied, little attention has been paid to the role of d-ribose in the glycation of Tau. Here, we show that Tau is rapidly glycated in the presence of d-ribose, resulting in oligomerization and polymerization. Glycated derivatives appeared after 24 h incubation. Western blotting indicated the formation of advanced glycation end-products (AGEs) during initial stages of glycation. Thioflavin T-positive (ThT-positive) aggregations that appeared from day 4 indicated the globular-like features. Atomic force microscopy revealed that the surface morphology of ribosylated Tau40 was globular-like. Kinetic studies suggested that d-ribosylated Tau is slowly oligomerized and rapidly polymerized with ThT-positive features. Moreover, d-ribosylated Tau aggregates were highly toxic to SHSY5Y cells and resulted in both apoptosis and necrosis. This work has demonstrated that d-ribose reacted with Tau protein rapidly, producing ThT-positive aggregations which had high cytotoxicity.; Although the glycation of Tau that is involved in paired helical filament formation in Alzheimer's disease has been widely studied, little attention has been paid to the role of d-ribose in the glycation of Tau. Here, we show that Tau is rapidly glycated in the presence of d-ribose, resulting in oligomerization and polymerization. Glycated derivatives appeared after 24 h incubation. Western blotting indicated the formation of advanced glycation end-products (AGEs) during initial stages of glycation. Thioflavin T-positive (ThT-positive) aggregations that appeared from day 4 indicated the globular-like features. Atomic force microscopy revealed that the surface morphology of ribosylated Tau40 was globular-like. Kinetic studies suggested that d-ribosylated Tau is slowly oligomerized and rapidly polymerized with ThT-positive features. Moreover, d-ribosylated Tau aggregates were highly toxic to SHSY5Y cells and resulted in both apoptosis and necrosis. This work has demonstrated that d-ribose reacted with Tau protein rapidly, producing ThT-positive aggregations which had high cytotoxicity. |
| 学科主题 | 生物学 |
| 语种 | 英语 |
| WOS记录号 | WOS:000268102000010 |
| 公开日期 | 2011-08-22 |
| 源URL | [http://ir.psych.ac.cn/handle/311026/5329]  |
| 专题 | 心理研究所_中国科学院心理研究所回溯数据库(1956-2010) |
| 通讯作者 | R. Q. He |
| 作者单位 | 1.Chinese Acad Sci, Inst Biophys, State Key Lab Brain & Cognit Sci, Beijing 100101, Peoples R China 2.Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China 3.Chinese Acad Sci, Inst Psychol, Key Lab Mental Hlth, Beijing 100101, Peoples R China |
| 推荐引用方式 GB/T 7714 | Chen, Lan,Wei, Yan,Wang, Xueqing,et al. d-Ribosylated Tau forms globular aggregates with high cytotoxicity[J]. CELLULAR AND MOLECULAR LIFE SCIENCES,2009,66(15):2559-2571. |
| APA | Chen, Lan,Wei, Yan,Wang, Xueqing,He, Rongqiao,&R. Q. He.(2009).d-Ribosylated Tau forms globular aggregates with high cytotoxicity.CELLULAR AND MOLECULAR LIFE SCIENCES,66(15),2559-2571. |
| MLA | Chen, Lan,et al."d-Ribosylated Tau forms globular aggregates with high cytotoxicity".CELLULAR AND MOLECULAR LIFE SCIENCES 66.15(2009):2559-2571. |
入库方式： OAI收割
来源：心理研究所
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