Domain a' of protein disulfide isomerase plays key role in inhibiting alpha-synuclein fibril formation | |
Cheng, Han1,2; Wang, Lei1; Wang, Chih-chen1 | |
刊名 | Cell stress & chaperones |
2010-07-01 | |
卷号 | 15期号:4页码:415-421 |
关键词 | Protein disulfide isomerase Alpha-synuclein Fibril Isothermal titration calorimetry |
ISSN号 | 1355-8145 |
DOI | 10.1007/s12192-009-0157-2 |
通讯作者 | Wang, chih-chen(chihwang@sun5.ibp.ac.cn) |
英文摘要 | Alpha-synuclein (alpha syn) is the main component of lewy bodies formed in midbrain dopaminergic neurons which is a pathological characteristic of parkinson's disease. it has been recently showed to induce endoplasmic reticulum (er) stress and impair er functions. however, the mechanism of how er responds to alpha syn toxicity is poorly understood. in the present study, we found that protein disulfide isomerase (pdi), a stress protein abundant in er, effectively inhibits alpha syn fibril formation in vitro. in pdi molecule with a structure of abb'xa'c, domain a' was found to be essential and sufficient for pdi to inhibit alpha syn fibril formation. pdi was further found to be more avid for binding with intermediate species formed during alpha syn fibril formation, and the binding was more intensive in the later lag phase. our results provide new insight into the role of pdi in protecting er from the deleterious effects of misfolded protein accumulation in many neurodegenerative diseases. |
WOS关键词 | ENDOPLASMIC-RETICULUM STRESS ; PARKINSONS-DISEASE ; MOLECULAR CHAPERONES ; BINDING SITE ; IN-VITRO ; MUTATION ; FAMILY ; GENE ; IDENTIFICATION ; PATHOGENESIS |
WOS研究方向 | Cell Biology |
WOS类目 | Cell Biology |
语种 | 英语 |
出版者 | SPRINGER |
WOS记录号 | WOS:000278681300008 |
内容类型 | 期刊论文 |
URI标识 | http://www.corc.org.cn/handle/1471x/2413055 |
专题 | 中国科学院大学 |
通讯作者 | Wang, Chih-chen |
作者单位 | 1.Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China 2.Chinese Acad Sci, Grad Sch, Beijing 100049, Peoples R China |
推荐引用方式 GB/T 7714 | Cheng, Han,Wang, Lei,Wang, Chih-chen. Domain a' of protein disulfide isomerase plays key role in inhibiting alpha-synuclein fibril formation[J]. Cell stress & chaperones,2010,15(4):415-421. |
APA | Cheng, Han,Wang, Lei,&Wang, Chih-chen.(2010).Domain a' of protein disulfide isomerase plays key role in inhibiting alpha-synuclein fibril formation.Cell stress & chaperones,15(4),415-421. |
MLA | Cheng, Han,et al."Domain a' of protein disulfide isomerase plays key role in inhibiting alpha-synuclein fibril formation".Cell stress & chaperones 15.4(2010):415-421. |
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