Publication
Title
Epitope mapping of monoclonal antibodies to the paired helical filaments of Alzheimer's disease : identification of phosphorylation sites in tau-protein
Author
Abstract
Tau is a neuronal phosphoprotein the expression of which is developmentally regulated. A single tau isoform is expressed in fetal human brain but six isoforms are expressed in adult human brain, with the fetal isoform corresponding to the shortest adult isoform. Phosphorylation is also developmentally regulated, as fetal tau is phosphorylated at more sites than adult tau. In Alzheimer's disease, the six adult tau isoforms become hyperphosphorylated and form the paired helical filament (PHF), the major fibrous component of the neurofibrillary lesions. One way to identify phosphorylated sites in tau is to use antibodies that recognize phosphorylated residues within a specific amino acid sequence. We here characterize the two novel phosphorylation-dependent anti-tau antibodies AT270 and AT180 and identify their epitopes as containing phosphorylated Thr-181 and Thr-231 respectively. With these antibodies we show that these two threonine residues are partially phosphorylated in fetal and adult tau and almost fully phosphorylated in PHF tau. This result contrasts with previous studies of Ser-202 and Ser-396 which are partially phosphorylated in fetal tan, unphosphorylated in adult tau but almost fully phosphorylated in PHF tau.
Language
English
Source (journal)
The biochemical journal. - London, 1984, currens
Publication
London : 1994
ISSN
0264-6021 [print]
1470-8728 [online]
Volume/pages
301:Part 3(1994), p. 871-877
ISI
A1994PB31100033
Full text (Publishers DOI)
Full text (publishers version - intranet only)
UAntwerpen
Faculty/Department
Research group
Publication type
Subject
Affiliation
Publications with a UAntwerp address
External links
Web of Science
Record
Identification
Creation 19.07.2012
Last edited 10.04.2017
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