Analysis of β-Amyloid Peptide -Binding Proteins in Microglial Cell

S. Ito, N. Nishio, K. Isobe
{"title":"Analysis of β-Amyloid Peptide -Binding Proteins in Microglial Cell","authors":"S. Ito, N. Nishio, K. Isobe","doi":"10.2174/1874827901205010001","DOIUrl":null,"url":null,"abstract":"Alzheimer's disease is the most common form of dementia in the elderly. Although � -amyloid peptide (A� ) has been considered major cause of Alzheimer pathology, molecular and cellular mechanisms of the disease development of Alzheimer have not been clarified yet. Presently Ahas been considered to induce neural cell death by direct penetration of aggregated form or indirect cell death by inflammatory responses induced by A� -activated microglia. In order to understand Ainduced microglial activation, we searched the proteins which bind to Ain activated microglial cell line. We stimulated Ra2 microglial cell line with A� . Activated Ra2 cells were immunoprecipitated with anti- Aand run the gel. Membrane was silver stained and bands were cut and digested with enzyme. They were analyzed by LC/MS/MS. We found that several proteins including myosin 9 and actin bound to A� . By the addition of A� , actin binding was enhanced and other proteins including IQGAP1, Plectin strongly bound to A� . These results indicate that Abinds to the proteins belonging to cellular cytoskeletal system.","PeriodicalId":89035,"journal":{"name":"The open geriatric medicine journal","volume":"50 1","pages":"1-6"},"PeriodicalIF":0.0000,"publicationDate":"2012-01-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"The open geriatric medicine journal","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.2174/1874827901205010001","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0

Abstract

Alzheimer's disease is the most common form of dementia in the elderly. Although � -amyloid peptide (A� ) has been considered major cause of Alzheimer pathology, molecular and cellular mechanisms of the disease development of Alzheimer have not been clarified yet. Presently Ahas been considered to induce neural cell death by direct penetration of aggregated form or indirect cell death by inflammatory responses induced by A� -activated microglia. In order to understand Ainduced microglial activation, we searched the proteins which bind to Ain activated microglial cell line. We stimulated Ra2 microglial cell line with A� . Activated Ra2 cells were immunoprecipitated with anti- Aand run the gel. Membrane was silver stained and bands were cut and digested with enzyme. They were analyzed by LC/MS/MS. We found that several proteins including myosin 9 and actin bound to A� . By the addition of A� , actin binding was enhanced and other proteins including IQGAP1, Plectin strongly bound to A� . These results indicate that Abinds to the proteins belonging to cellular cytoskeletal system.
小胶质细胞β-淀粉样肽结合蛋白的分析
阿尔茨海默病是老年人中最常见的痴呆症。虽然-淀粉样肽(A)被认为是阿尔茨海默病的主要病因,但阿尔茨海默病发生的分子和细胞机制尚不清楚。目前,人们认为A通过直接渗透聚集体形式诱导神经细胞死亡,或通过A激活的小胶质细胞诱导炎症反应间接诱导细胞死亡。为了了解诱导的小胶质细胞激活,我们寻找了与Ain激活的小胶质细胞系结合的蛋白。我们用A α刺激Ra2小胶质细胞系。活化的Ra2细胞用抗a免疫沉淀,并运行凝胶。膜染银,切条带,酶解。采用LC/MS/MS分析。我们发现包括肌凝蛋白9和肌动蛋白在内的几种蛋白与A结合。通过A α的加入,增强了肌动蛋白的结合,其他蛋白包括IQGAP1、Plectin与A α强结合。这些结果表明,它与属于细胞骨架系统的蛋白质结合。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信