NDLI: The role of Î³-secretase activating protein (GSAP) and imatinib in the regulation of Î³-secretase activity and amyloid-ß generation.

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The role of Î³-secretase activating protein (GSAP) and imatinib in the regulation of Î³-secretase activity and amyloid-ß generation.

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The role of Î³-secretase activating protein (GSAP) and imatinib in the regulation of Î³-secretase activity and amyloid-ß generation.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Fabrègue, Julien Anderes, Laurence Beher, Dirk Ousson, Solenne Eligert, Valérie Berger, Sébastien Dimitrov, Mitko Hussain, Ishrut Borlat, Frédéric Fraering, Patrick C. Alattia, Jean-rené
Description	Author Affiliation: Hussain I ( Department of Therapeutic Area Neurodegenerative Diseases, Merck Serono S.A., Chemin des Mines 9, 1202 Geneva, Switzerland. ishruthssn@gmail.com)
Abstract	Î³-Secretase is a large enzyme complex comprising presenilin, nicastrin, presenilin enhancer 2, and anterior pharynx-defective 1 that mediates the intramembrane proteolysis of a large number of proteins including amyloid precursor protein and Notch. Recently, a novel Î³-secretase activating protein (GSAP) was identified that interacts with Î³-secretase and the C-terminal fragment of amyloid precursor protein to selectively increase amyloid-ß production. In this study we have further characterized the role of endogenous and exogenous GSAP in the regulation of Î³-secretase activity and amyloid-ß production in vitro. Knockdown of GSAP expression in N2a cells decreased amyloid-ß levels. In contrast, overexpression of GSAP in HEK cells expressing amyloid precursor protein or in N2a cells had no overt effect on amyloid-ß generation. Likewise, purified recombinant GSAP had no effect on amyloid-ß generation in two distinct in vitro Î³-secretase assays. In subsequent cellular studies with imatinib, a kinase inhibitor that reportedly prevents the interaction of GSAP with the C-terminal fragment of amyloid precursor protein, a concentration-dependent decrease in amyloid-ß levels was observed. However, no interaction between GSAP and the C-terminal fragment of amyloid precursor protein was evident in co-immunoprecipitation studies. In addition, subchronic administration of imatinib to rats had no effect on brain amyloid-ß levels. In summary, these findings suggest the roles of GSAP and imatinib in the regulation of Î³-secretase activity and amyloid-ß generation are uncertain.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	4
Volume Number	288
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2013-01-25
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Amyloid Precursor Protein Secretases Metabolism Amyloid Beta-Peptides Gene Expression Regulation Piperazines Pharmacology Proteins Chemistry Pyrimidines Alzheimer Disease Drug Therapy Animals Benzamides Brain Cell Line, Tumor Imatinib Mesylate Mice Protein Binding Protein Kinase Inhibitors RNA, Small Interfering Rats, Sprague-Dawley Recombinant Proteins 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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