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	Formaldehyde at low concentration induces protein tau into globular amyloid-like aggregates in vitro and in vivo
	Nie, Chun Lai1; Wei, Yan1; Chen, Xinyong2; Liu, Yan Ying1; Dui, Wen1; Liu, Ying1; Davies, Martyn C.2; Tendler, Saul J. B.2; He, Rong Giao1
刊名	Plos one
	2007-07-18
卷号	2期号:7页码:13
ISSN号	1932-6203
DOI	10.1371/journal.pone.0000629
通讯作者	He, rong giao(herq@sun5.ibp.ac.cn)
英文摘要	Recent studies have shown that neurodegeneration is closely related to misfolding and aggregation of neuronal tau. our previous results show that neuronal tau aggregates in formaldehyde solution and that aggregated tau induces apoptosis of sh-sy5y and hippocampal cells. in the present study, based on atomic force microscopy (afm) observation, we have found that formaldehyde at low concentrations induces tau polymerization whilst acetaldehyde does not. neuronal tau misfolds and aggregates into globular-like polymers in 0.01-0.1% formaldehyde solutions. apart from globular-like aggregation, no fibril-like polymerization was observed when the protein was incubated with formaldehyde for 15 days. sds-page results also exhibit tau polymerizing in the presence of formaldehyde. under the same experimental conditions, polymerization of bovine serum albumin (bsa) or alpha-synuclein was not markedly detected. kinetic study shows that tau significantly misfolds and polymerizes in 60 minutes in 0.1% formaldehyde solution. however, presence of 10% methanol prevents protein tau from polymerization. this suggests that formaldehyde polymerization is involved in tau aggregation. such aggregation process is probably linked to the tau's special "worm-like'' structure, which leaves the epsilon-amino groups of lys and thiol groups of cys exposed to the exterior. such a structure can easily bond to formaldehyde molecules in vitro and in vivo. polymerizing of formaldehyde itself results in aggregation of protein tau. immunocytochemistry and thioflavin s staining of both endogenous and exogenous tau in the presence of formaldehyde at low concentrations in the cell culture have shown that formaldehyde can induce tau into amyloid-like aggregates in vivo during apoptosis. the significant protein tau aggregation induced by formaldehyde and the severe toxicity of the aggregated tau to neural cells may suggest that toxicity of methanol and formaldehyde ingestion is related to tau misfolding and aggregation.
WOS研究方向	Science & Technology - Other Topics
WOS类目	Multidisciplinary Sciences
语种	英语
出版者	PUBLIC LIBRARY SCIENCE
WOS记录号	WOS:000207452100018
内容类型	期刊论文
URI标识	http://www.corc.org.cn/handle/1471x/2380744
专题	中国科学院大学
通讯作者	He, Rong Giao
作者单位	1.Chinese Acad Sci, Inst Biophys, Grad Sch, State Key Lab Brain & Cognit Sci, Beijing 100080, Peoples R China 2.Univ Nottingham, Sch Pharm, Lab Biophys & Surface Anal, Nottingham NG7 2RD, England
推荐引用方式 GB/T 7714	Nie, Chun Lai,Wei, Yan,Chen, Xinyong,et al. Formaldehyde at low concentration induces protein tau into globular amyloid-like aggregates in vitro and in vivo[J]. Plos one,2007,2(7):13.
APA	Nie, Chun Lai.,Wei, Yan.,Chen, Xinyong.,Liu, Yan Ying.,Dui, Wen.,...&He, Rong Giao.(2007).Formaldehyde at low concentration induces protein tau into globular amyloid-like aggregates in vitro and in vivo.Plos one,2(7),13.
MLA	Nie, Chun Lai,et al."Formaldehyde at low concentration induces protein tau into globular amyloid-like aggregates in vitro and in vivo".Plos one 2.7(2007):13.

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