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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
2009-08-01
Source PublicationCELLULAR AND MOLECULAR LIFE SCIENCES
ISSN1420-682X
SubtypeArticle
Volume66Issue:15Pages:2559-2571
AbstractAlthough 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.
KeywordD-Ribose Tau protein Glycation Aggregation Cytotoxicity
Subject Area生物学
Indexed BySCI
Language英语
WOS IDWOS:000268102000010
Citation statistics
Cited Times:40[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.psych.ac.cn/handle/311026/5329
Collection中国科学院心理研究所回溯数据库(1956-2010)
Corresponding AuthorR. Q. He
Affiliation1.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
Recommended Citation
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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