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阿尔茨海默病β-淀粉样蛋白的分泌动力学不同于分泌型β-淀粉样前体蛋白。

Secretion kinetics of Alzheimer's amyloid beta-protein differs from secreted beta-amyloid precursor protein.

作者信息

Araki W, Kunishita T, Takahashi K, Ikeda S, Tabira T

机构信息

Division of Demyelinating Disease and Aging, National Institute of Neuroscience, NCNP, Tokyo, Japan.

出版信息

Biochem Biophys Res Commun. 1995 Sep 14;214(2):490-5. doi: 10.1006/bbrc.1995.2313.

Abstract

Amyloid beta-protein (A beta) and secreted beta-amyloid precursor protein (sAPP), derived from beta-amyloid precursor protein (APP), are normally released by cultured mammalian cells. We investigated by pulse-chase analysis the secretion kinetics of these two APP derivatives using mouse cholinergic SN49 cell lines stably transfected with mouse APP695 cDNA. After both A beta and sAPP peaked at about the second hour, sAPP decreased with a half-life of approximately 5 hours, but A beta remained almost unchanged for at least 14 hours. These results indicate that A beta is more stable than sAPP in the SN49 conditioned medium.

摘要

源自β-淀粉样前体蛋白(APP)的β-淀粉样蛋白(Aβ)和分泌型β-淀粉样前体蛋白(sAPP)通常由培养的哺乳动物细胞释放。我们使用稳定转染了小鼠APP695 cDNA的小鼠胆碱能SN49细胞系,通过脉冲追踪分析研究了这两种APP衍生物的分泌动力学。在Aβ和sAPP均在大约第二小时达到峰值后,sAPP以约5小时的半衰期下降,但Aβ至少14小时几乎保持不变。这些结果表明,在SN49条件培养基中,Aβ比sAPP更稳定。

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