著者

Naoki KANEKO Rie YAMAMOTO Taka-Aki SATO Koichi TANAKA

出版者

日本学士院

雑誌

Proceedings of the Japan Academy, Series B (ISSN:03862208)

巻号頁・発行日

vol.90, no.3, pp.104-117, 2014-03-11 (Released:2014-03-11)

参考文献数

41

被引用文献数

10 51 1

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Proteolytic processing of the amyloid precursor protein (APP) by β-secretase and γ-secretase leads to the generation and deposition of amyloid β (Aβ) in Alzheimer’s disease (AD). N-terminally or C-terminally truncated Aβ variants have been found in human cerebrospinal fluid and cultured cell media using immunoprecipitation and mass spectrometry. Unfortunately, the profile of plasma Aβ variants has not been revealed due to the difficulty of isolating Aβ from plasma. We present here for the first time studies of Aβ and related peptides in human plasma. Twenty-two Aβ-related peptides including novel peptides truncated before the β-secretase site were detected in human plasma and 20 of the peptides were identified by tandem mass spectrometry. Using an internal standard, we developed a quantitative assay for the Aβ-related peptides and demonstrated plasma dilution linearity and the precision required for their quantitation. The present method should enhance the understanding of APP processing and clearance in AD progression.