The novel amyloid-beta peptide aptamer inhibitsintracellular amyloid-beta peptide toxicity
Amyloid β peptide binding alcohol dehydrogenase (ABAD) decoy peptide (DP) can competitively antagonize binding of amyloid β peptide to ABAD and inhibit the cytotoxic effects of amyloid β peptide. Based on peptide aptamers, the present study inserted ABAD-DP into the disulfide bond of human thioredox...
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Veröffentlicht in: | 中国神经再生研究:英文版 2013, Vol.8 (1), p.39-48 |
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creator | Xu Wang Yi Yang Mingyue Jia Chi Ma Mingyu Wang Lihe Che YuYang Jiang Wu |
description | Amyloid β peptide binding alcohol dehydrogenase (ABAD) decoy peptide (DP) can competitively antagonize binding of amyloid β peptide to ABAD and inhibit the cytotoxic effects of amyloid β peptide. Based on peptide aptamers, the present study inserted ABAD-DP into the disulfide bond of human thioredoxin (TRX) using molecular cloning technique to construct a fusion gene that can express the TRX1-ABAD-DP-TRX2 aptamer. Moreover, adeno-associated virus was used to allow its stable expression. Immunofluorescent staining revealed the co-expression of the transduced fusion gene TRX1-ABAD-DP-TRX2 and amyloid β peptide in NIH-3T3 cells, indicating that the TRXl-ABAD-DP-TRX2 aptamer can bind amyloid β peptide within cells. In addition, cell morphology and MTT results suggested that TRX1-ABAD-DP-TRX2 attenuated amyloid β peptide-induced SH-SY5Y cell injury and improved cell viability. These findings confirmed the possibility of constructing TRX-based peptide aptamer using ABAD-DP. Moreover, TRXl-ABAD-DP-TRX2 inhibited the cytotoxic effect of amyloid β peptide. |
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Based on peptide aptamers, the present study inserted ABAD-DP into the disulfide bond of human thioredoxin (TRX) using molecular cloning technique to construct a fusion gene that can express the TRX1-ABAD-DP-TRX2 aptamer. Moreover, adeno-associated virus was used to allow its stable expression. Immunofluorescent staining revealed the co-expression of the transduced fusion gene TRX1-ABAD-DP-TRX2 and amyloid β peptide in NIH-3T3 cells, indicating that the TRXl-ABAD-DP-TRX2 aptamer can bind amyloid β peptide within cells. In addition, cell morphology and MTT results suggested that TRX1-ABAD-DP-TRX2 attenuated amyloid β peptide-induced SH-SY5Y cell injury and improved cell viability. These findings confirmed the possibility of constructing TRX-based peptide aptamer using ABAD-DP. Moreover, TRXl-ABAD-DP-TRX2 inhibited the cytotoxic effect of amyloid β peptide.</description><identifier>ISSN: 1673-5374</identifier><language>eng</language><subject>SH-SY5Y ; 人硫氧还蛋白 ; 免疫荧光染色 ; 拮抗肽 ; 淀粉样蛋白 ; 细胞毒性 ; 融合基因 ; 适体</subject><ispartof>中国神经再生研究:英文版, 2013, Vol.8 (1), p.39-48</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://image.cqvip.com/vip1000/qk/88507X/88507X.jpg</thumbnail><link.rule.ids>314,780,784,4024</link.rule.ids></links><search><creatorcontrib>Xu Wang Yi Yang Mingyue Jia Chi Ma Mingyu Wang Lihe Che YuYang Jiang Wu</creatorcontrib><title>The novel amyloid-beta peptide aptamer inhibitsintracellular amyloid-beta peptide toxicity</title><title>中国神经再生研究:英文版</title><addtitle>Neural Regeneration Research</addtitle><description>Amyloid β peptide binding alcohol dehydrogenase (ABAD) decoy peptide (DP) can competitively antagonize binding of amyloid β peptide to ABAD and inhibit the cytotoxic effects of amyloid β peptide. Based on peptide aptamers, the present study inserted ABAD-DP into the disulfide bond of human thioredoxin (TRX) using molecular cloning technique to construct a fusion gene that can express the TRX1-ABAD-DP-TRX2 aptamer. Moreover, adeno-associated virus was used to allow its stable expression. Immunofluorescent staining revealed the co-expression of the transduced fusion gene TRX1-ABAD-DP-TRX2 and amyloid β peptide in NIH-3T3 cells, indicating that the TRXl-ABAD-DP-TRX2 aptamer can bind amyloid β peptide within cells. In addition, cell morphology and MTT results suggested that TRX1-ABAD-DP-TRX2 attenuated amyloid β peptide-induced SH-SY5Y cell injury and improved cell viability. These findings confirmed the possibility of constructing TRX-based peptide aptamer using ABAD-DP. Moreover, TRXl-ABAD-DP-TRX2 inhibited the cytotoxic effect of amyloid β peptide.</description><subject>SH-SY5Y</subject><subject>人硫氧还蛋白</subject><subject>免疫荧光染色</subject><subject>拮抗肽</subject><subject>淀粉样蛋白</subject><subject>细胞毒性</subject><subject>融合基因</subject><subject>适体</subject><issn>1673-5374</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><recordid>eNqNyzkOwjAQQFEXIBGWO5gDREpwNmoE4gBUNNEkGZJBjm3sAZHb01BSUP3m_ZmI0qJUca7KbCGWIdyTJK_2OxWJ62VAaewLtYRx0pa6uEEG6dAxdSjBMYzoJZmBGuJAhj20qPVTg_-9sH1TSzytxfwGOuDm25XYno6XwzluB2v6B5m-dp5G8FOdZUWZFkml_jEfQ01COg</recordid><startdate>2013</startdate><enddate>2013</enddate><creator>Xu Wang Yi Yang Mingyue Jia Chi Ma Mingyu Wang Lihe Che YuYang Jiang Wu</creator><scope>2RA</scope><scope>92L</scope><scope>CQIGP</scope><scope>W91</scope><scope>~WA</scope></search><sort><creationdate>2013</creationdate><title>The novel amyloid-beta peptide aptamer inhibitsintracellular amyloid-beta peptide toxicity</title><author>Xu Wang Yi Yang Mingyue Jia Chi Ma Mingyu Wang Lihe Che YuYang Jiang Wu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-chongqing_primary_446716083</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>SH-SY5Y</topic><topic>人硫氧还蛋白</topic><topic>免疫荧光染色</topic><topic>拮抗肽</topic><topic>淀粉样蛋白</topic><topic>细胞毒性</topic><topic>融合基因</topic><topic>适体</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Xu Wang Yi Yang Mingyue Jia Chi Ma Mingyu Wang Lihe Che YuYang Jiang Wu</creatorcontrib><collection>中文科技期刊数据库</collection><collection>中文科技期刊数据库-CALIS站点</collection><collection>中文科技期刊数据库-7.0平台</collection><collection>中文科技期刊数据库-医药卫生</collection><collection>中文科技期刊数据库- 镜像站点</collection><jtitle>中国神经再生研究:英文版</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Xu Wang Yi Yang Mingyue Jia Chi Ma Mingyu Wang Lihe Che YuYang Jiang Wu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The novel amyloid-beta peptide aptamer inhibitsintracellular amyloid-beta peptide toxicity</atitle><jtitle>中国神经再生研究:英文版</jtitle><addtitle>Neural Regeneration Research</addtitle><date>2013</date><risdate>2013</risdate><volume>8</volume><issue>1</issue><spage>39</spage><epage>48</epage><pages>39-48</pages><issn>1673-5374</issn><abstract>Amyloid β peptide binding alcohol dehydrogenase (ABAD) decoy peptide (DP) can competitively antagonize binding of amyloid β peptide to ABAD and inhibit the cytotoxic effects of amyloid β peptide. Based on peptide aptamers, the present study inserted ABAD-DP into the disulfide bond of human thioredoxin (TRX) using molecular cloning technique to construct a fusion gene that can express the TRX1-ABAD-DP-TRX2 aptamer. Moreover, adeno-associated virus was used to allow its stable expression. Immunofluorescent staining revealed the co-expression of the transduced fusion gene TRX1-ABAD-DP-TRX2 and amyloid β peptide in NIH-3T3 cells, indicating that the TRXl-ABAD-DP-TRX2 aptamer can bind amyloid β peptide within cells. In addition, cell morphology and MTT results suggested that TRX1-ABAD-DP-TRX2 attenuated amyloid β peptide-induced SH-SY5Y cell injury and improved cell viability. These findings confirmed the possibility of constructing TRX-based peptide aptamer using ABAD-DP. Moreover, TRXl-ABAD-DP-TRX2 inhibited the cytotoxic effect of amyloid β peptide.</abstract></addata></record> |
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subjects | SH-SY5Y 人硫氧还蛋白 免疫荧光染色 拮抗肽 淀粉样蛋白 细胞毒性 融合基因 适体 |
title | The novel amyloid-beta peptide aptamer inhibitsintracellular amyloid-beta peptide toxicity |
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