Differential effects of apolipoprotein E isoforms on phosphorylation at specific sites on tau by glycogen synthase kinase-3 beta identified by nano-electrospray mass spectrometry

G M Gibb, J Pearce, J C Betts, S Lovestone, M M Hoffmann, W Maerz, W P Blackstock, B H Anderton

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    23 Citations (Scopus)

    Abstract

    Previously published data have shown an allele-specific variation in the in vitro binding of apolipoprotein E (apoE) to tau, which prompted the hypothesis that apoE binding may protect tau from phosphorylation, apoE3 being more efficient than apoE4, We have, therefore, investigated the effects of apoE on tau phosphorylation in vitro by the proline-directed kinase, glycogen synthase kinase (GSK)-3 beta The phosphopeptide maps of tau alone, of tau with apoE3 and of tau with apoE4 were very similar. When apoE2 was present a further four spots were evident. Additionally, of the 15 peptides phosphorylated in the presence or absence of apoE, subtle differences, some isoform-specific, in the relative amounts of phosphorylation were observed. (C) 2000 Federation of European Biochemical Societies, Published by Elsevier Science B.V. All rights reserved.
    Original languageEnglish
    Pages (from-to)99 - 103
    Number of pages5
    JournalFEBS Letters
    Volume485
    Issue number2-3
    DOIs
    Publication statusPublished - 24 Nov 2000

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