NDLI: Î³-Secretase associated with lipid rafts: multiple interactive pathways in the stepwise processing of ß-carboxyl-terminal fragment.

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Î³-Secretase associated with lipid rafts: multiple interactive pathways in the stepwise processing of ß-carboxyl-terminal fragment.

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Î³-Secretase associated with lipid rafts: multiple interactive pathways in the stepwise processing of ß-carboxyl-terminal fragment.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Ihara, Yasuo Wada-kakuda, Satoko Fujiwara, Hitomi Morishima-kawashima, Maho Takami, Mako Funamoto, Satoru Okochi, Masayasu Matsumura, Nobutaka Tagami, Shinji
Description	Author Affiliation: Matsumura N ( From the Department of Molecular Neuropathology, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812.)
Abstract	Î³-Secretase generates amyloid ß-protein (Aß), a pathogenic molecule in Alzheimer disease, through the intramembrane cleavage of the ß-carboxyl-terminal fragment (ßCTF) of ß-amyloid precursor protein. We previously showed the framework of the Î³-secretase cleavage, i.e. the stepwise successive processing of ßCTF at every three (or four) amino acids. However, the membrane integrity of Î³-secretase was not taken into consideration because of the use of the 3-[(3-cholamidopropyl)dimethylammonio]-2-hydroxy-1-propanesulfonic acid-solubilized reconstituted Î³-secretase system. Here, we sought to address how the membrane-integrated Î³-secretase cleaves ßCTF by using Î³-secretase associated with lipid rafts. Quantitative analyses using liquid chromatography-tandem mass spectrometry of the ßCTF transmembrane domain-derived peptides released along with Aß generation revealed that the raft-associated Î³-secretase cleaves ßCTF in a stepwise sequential manner, but novel penta- and hexapeptides as well as tri- and tetrapeptides are released. The cropping of these peptides links the two major tripeptide-cleaving pathways generating Aß40 and Aß42 at several points, implying that there are multiple interactive pathways for the stepwise cleavages of ßCTF. It should be noted that Aß38 and Aß43 are generated through three routes, and Î³-secretase modulator 1 enhances all the three routes generating Aß38, which results in decreases in Aß42 and Aß43 and an increase in Aß38. These observations indicate that multiple interactive pathways for stepwise successive processing by Î³-secretase define the species and quantity of Aß produced.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	8
Volume Number	289
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2014-02-21
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Amyloid Precursor Protein Secretases Metabolism Amyloid Beta-Peptides Membrane Microdomains Protein Processing, Post-Translational Signal Transduction Chemistry Animals Brain CHO Cells Cricetinae Cricetulus Models, Biological Oligopeptides Rats, Wistar Time Factors Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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