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Cloning and purifying of Soluble amyloid precursor protein and its modulating MAPK signal pathway
CHEN Keping 1,DOU Fei 2 * #
1.Medical School Southeast University
2.College of life science, Beijing Normal University
*Correspondence author
#Submitted by
Subject:
Funding: Specialized Research Fund for the Doctoral Program of Higher Education（No.No.20090003110015)NSF）
Opened online: 9 January 2013
Accepted by: none
Citation: CHEN Keping,DOU Fei.Cloning and purifying of Soluble amyloid precursor protein and its modulating MAPK signal pathway[OL]. [ 9 January 2013] http://en.paper.edu.cn/en_releasepaper/content/4509550
 
 
It is well known that the proteolytic processing of the amyloid precursor protein (APP) release β-amyloid (Aβ), which plays a central role in the pathogenesis of Alzheimer's disease (AD). Understanding APP processing is important for reducing Aβ levels in AD therapeutic strategy. Soluble amyloid precursor protein (sAPPa) is a proteolyte of APP cleavage by α-secretase. The significance of the cleavage and the physiological functions of sAPPα are poorly understood. In this study, we constructed the stable cell lines expressing sAPPα fusion protein and purified with tandem affinity purification (TAP) technology. We also found sAPPα could modulate the MAPK signal pathway involving in NCAM-induced neurite outgrowth, likes the full length APP.
Keywords:cell biology; secreted APP; tandem affinity purification; MAPK
 
 
 

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