Tau, a microtubule associated protein, has been implicated in the formation of neurofibrillary tangles, a hallmark of Alzheimer’s disease.1 Resulting from the hyperphosphorylation of tyrosine, serine and threonine residues, protein kinases play an intricate role in the pathway of NFT formation.2 While a number of serine/ threonine kinases such as Glycogen Synthase Kinase 3 beta, have been implicated in the hyperphosphorylation of tau, and it is now believed that tyrosine phosphorylation plays a role. It appears that the degree to which tau is phosphorylated, and region in which phosphorylation occurs play a critical role in aggregate formation. Here we present the use of Ferrocene bioconjugates to monitor tyrosine-mediated hyperphosphorylation and aggregation. Electrochemistry, electron microscopy, surface plasmon resonance, Time of Flight Secondary Ion Mass Spectrometry and X-Ray Photoelectron Spectroscopy were used to gain insight into the role of tyrosine phosphorylation on hyperphosphorylation.
Identifer | oai:union.ndltd.org:TORONTO/oai:tspace.library.utoronto.ca:1807/33503 |
Date | 26 November 2012 |
Creators | Rains, Meghan Krystyna |
Contributors | Kraatz, Heinz-Bernhard |
Source Sets | University of Toronto |
Language | en_ca |
Detected Language | English |
Type | Thesis |
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