摘要
MTT法和荧光分光光度计检测发现β淀粉样蛋白膜内片段(intramembranous fragments of amyloid-β,IF-Aβ)可以抑制β淀粉样蛋白42(amyloid-β,Aβ42)对体外培养神经元的毒性.通过体外检测IF-Aβ对淀粉样前体蛋白(amyloid precursor protein,APP)表达的影响,探索IF-Aβ对Aβ42的神经毒性抑制机制.分别从mRNA水平和蛋白质水平用RT-PCR方法和Western-blot方法检测IF-Aβ对体外培养神经元APP表达的影响.发现IF-Aβ加入原代培养的神经元后,APP从mRNA水平和蛋白质水平均表达下降,说明IF-Aβ通过抑制APP的表达,减少了Aβ生成,达到神经保护的作用.
MTT assay and the calcium ion concentration in cell showed that intramembranous fragments of amyloidJ3(IF-A]3 were able to neutralize amyloid43 42(Aβ42)-neurotoxicity in cultured primary cortical neurons. To explore the inhibitory mechanism of Aβ42-neurotoxicity, the expression of amyloid precursor protein (APP) in vitro was determined when IF-Aβand IF-Aβplus Aβ42 were administered into cultured primcorti- cal neurons. APP mRNA and protein were decreased after IF-Aβ into primary cultured neurons by RT-PCR and Western-blot. These results suggested that IF-Aβ appear to protect neurons from Alzheimer's disease (AD) by inhibitting the expression of APP
出处
《生命科学研究》
CAS
CSCD
北大核心
2013年第3期200-204,215,共6页
Life Science Research
基金
2010年河南省重点科技攻关项目(102102310327)
关键词
阿尔茨海默病
β淀粉样蛋白膜内片段
淀粉样前体蛋白
表达
Alzheimer's disease
intramembranous fragments of amyloid-β
amyloid precursor protein
expression