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	d-Ribosylated Tau forms globular aggregates with high cytotoxicity
	Chen, Lan1; Wei, Yan1,2; Wang, Xueqing1; He, Rongqiao1,3; R. Q. He
刊名	CELLULAR AND MOLECULAR LIFE SCIENCES
	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
内容类型	期刊论文
源URL	[http://ir.psych.ac.cn/handle/311026/5330]
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.

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