Affiliations: [a] Alzheimer's and Parkinson's Disease Laboratory, Brain and Mind Research Institute, University of Sydney, Camperdown, NSW, Australia | [b] Max-Planck Research Unit for Enzymology of Protein Folding, Halle (Saale), Germany
Correspondence:
[*]
Corresponding author: Dr. J. Götz, Alzheimer's and Parkinson's Disease Laboratory, Brain and Mind Research Institute, University of Sydney, 100, Mallett St., Camperdown, NSW 2050, Australia. Tel.: +61 2 935 10789; Fax.: +61 2 935 10731; E-mail: j.goetz@med.usyd.edu.au.
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.
