Macromolecular crowding converts the human recombinant prpc to the soluble neurotoxic beta-oligomers
文献类型：期刊论文
| 作者 | Huang, Liqin2; Jin, Rui1; Li, Jiarui2; Luo, Kan2; Huang, Tao2; Wu, Di2; Wang, Wenxi2; Chen, Rui2; Xiao, Gengfu1,2 |
| 刊名 | Faseb journal
 |
| 出版日期 | 2010-09-01 |
| 卷号 | 24期号:9页码:3536-3543 |
| 关键词 | Prion protein Thermodynamic stability Neurotoxicity Crowded environment Oligomerization |
| ISSN号 | 0892-6638 |
| DOI | 10.1096/fj.09-150987 |
| 通讯作者 | Xiao, gengfu(xiaogf@wh.iov.cn) |
| 英文摘要 | Prion diseases are fatal neurodegenerative disorders and are linked with the conversion of the cellular isoform of the prion protein (prpc) into the abnormal beta-sheet-rich isoform. it is widely accepted that the soluble oligomers of beta-prp are neurotoxic and that they are more pathologically significant. to unravel the molecular mechanism under the conversion process, it is critical to identify the factors that can promote the conversion from prpc to the beta-oligomers. by recording circular dichroism spectra and performing a size-exclusion hplc assay, we found that the conformation of the recombinant human prion protein (rprp(c)) was converted from an alpha-helical conformation into beta-sheet oligomers under a macromolecular crowding condition. the soluble beta-oligomers of rprp were resistant to proteinase k digestion and could bind to the dyes thioflavin t and 8-anilino-1-naphthalene sulfonate. furthermore, by the 3-(4, 5-dimethylthiazol-2-yl)-5-(3-carboxymethoxyphenyl)-2-(4-sulfophenyl)-2h-tetrazolium assay, we showed that the soluble beta-oligomers were neurotoxic. these results suggest that macromolecular crowding, which has not been considered before, is a key intracellular factor in the formation of soluble neurotoxic beta-oligomers in prion diseases.-huang, l., jin, r., li, j., luo, k., huang, t., wu, d., wang, w., chen, r., xiao, g. macromolecular crowding converts the human recombinant prpc to the soluble neurotoxic beta-oligomers. faseb j. 24, 3536-3543 (2010). www.fasebj.org |
| WOS关键词 | SCRAPIE PRION PROTEINS ; INSERTION MUTATIONS ; FIBRIL FORMATION ; ALPHA-SYNUCLEIN ; CONFORMATION ; AGGREGATION ; PATHWAY ; FIBRILLIZATION ; TRANSITION ; STABILITY |
| WOS研究方向 | Biochemistry & Molecular Biology ; Life Sciences & Biomedicine - Other Topics ; Cell Biology |
| WOS类目 | Biochemistry & Molecular Biology ; Biology ; Cell Biology |
| 语种 | 英语 |
| WOS记录号 | WOS:000281446400040 |
| 出版者 | FEDERATION AMER SOC EXP BIOL |
| URI标识 | http://www.irgrid.ac.cn/handle/1471x/2375705 |
| 专题 | 武汉病毒研究所 |
| 通讯作者 | Xiao, Gengfu |
| 作者单位 | 1.Wuhan Univ, Chinese Acad Sci, State Key Lab Virol, Wuhan Inst Virol, Wuhan 430071, Hubei, Peoples R China 2.Wuhan Univ, State Key Lab Virol, Coll Life Sci, Wuhan 430071, Hubei, Peoples R China |
| 推荐引用方式 GB/T 7714 | Huang, Liqin,Jin, Rui,Li, Jiarui,et al. Macromolecular crowding converts the human recombinant prpc to the soluble neurotoxic beta-oligomers[J]. Faseb journal,2010,24(9):3536-3543. |
| APA | Huang, Liqin.,Jin, Rui.,Li, Jiarui.,Luo, Kan.,Huang, Tao.,...&Xiao, Gengfu.(2010).Macromolecular crowding converts the human recombinant prpc to the soluble neurotoxic beta-oligomers.Faseb journal,24(9),3536-3543. |
| MLA | Huang, Liqin,et al."Macromolecular crowding converts the human recombinant prpc to the soluble neurotoxic beta-oligomers".Faseb journal 24.9(2010):3536-3543. |
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来源：武汉病毒研究所
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