Altered glycosylation of acetylcholinesterase in APP (SW) Tg2576 transgenic mice occurs prior to amyloid plaque deposition

Previous studies have shown that a minor glycoform of acetylcholinesterase (AChE) is increased in Alzheimer's disease brain and cerebrospinal fluid. This glycoform can be distinguished from other AChE species by its lack of binding to concanavalin A (Con A). In this study, the temporal relation...

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Veröffentlicht in:	Journal of neurochemistry 2002-05, Vol.81 (3), p.441-448
Hauptverfasser:	Fodero, Lisa R., Sáez‐Valero, Javier, McLean, Catriona A., Martins, Ralph N., Beyreuther, Konrad, Masters, Colin L., Small, David H.
Format:	Artikel
Sprache:	eng
Schlagworte:	Acetylcholinesterase - chemistry Acetylcholinesterase - metabolism AChE Alzheimer Disease - metabolism Alzheimer Disease - pathology amyloid Animals Biological and medical sciences Brain - metabolism Brain - pathology Brain Chemistry Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases Disease Models, Animal Disease Progression Enzyme Activation Glial Fibrillary Acidic Protein - biosynthesis Glycosylation Immunohistochemistry Isoenzymes - chemistry Isoenzymes - metabolism Medical sciences Mice Mice, Transgenic Neurology Plaque, Amyloid - chemistry Plaque, Amyloid - metabolism Plaque, Amyloid - pathology Tg2576
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Zusammenfassung:	Previous studies have shown that a minor glycoform of acetylcholinesterase (AChE) is increased in Alzheimer's disease brain and cerebrospinal fluid. This glycoform can be distinguished from other AChE species by its lack of binding to concanavalin A (Con A). In this study, the temporal relationship between AChE glycosylation and Aβ deposition was examined in Tg2576 mice. There was a significant (p
ISSN:	0022-3042 1471-4159
DOI:	10.1046/j.1471-4159.2002.00902.x