Is tau aggregation toxic or protective

a sensible question in the absence of sensitive methods?

Jürgen Götz*, Lars M. Ittner, Marcus Fändrich, Nicole Schonrock

*Corresponding author for this work

Research output: Contribution to journalReview article

28 Citations (Scopus)

Abstract

In Alzheimer's disease brain, the microtubule-associated protein tau detaches from the microtubules, pathologically interacts with cellular proteins, and eventually forms insoluble aggregates that also bind and trap a myriad of proteins. As these proteins are depleted from the cellular pool, they are unavailable for physiological functions. Thus elevated tau levels are pathogenic, even in the absence of tau aggregation. Whereas it is reasonable to assume that tau aggregation is toxic during late stages of disease, the question arises whether early in disease it may be protective. This question can be addressed in tau transgenic animal models in which tau aggregation has been correlated with behavioral impairment. We discuss ways of how tau aggregation is monitored in these mice and what the detection limits are of these methods. We conclude that new tools are needed to measure the different stages of tau aggregation.

Original languageEnglish
Pages (from-to)423-429
Number of pages7
JournalJournal of Alzheimer's Disease
Volume14
Issue number4
DOIs
Publication statusPublished - 1 Jan 2008
Externally publishedYes

Keywords

  • Axonal transport
  • Fibril
  • Immuno-precipitation
  • Mass spectrometry
  • Oligomer
  • Phosphorylation
  • Thioflavin
  • Transgenic
  • β-sheet structure

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