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Effect of phosphorylation on tau aggregation using model peptides and Circular Dichroism studies

  • Heather Palmer
  • Ajoy Basak
Part of the Advances in Experimental Medicine and Biology book series (volume 611)

Introduction

Human (h) tau is a microtubule (MT) associated protein that has been implicated in Alzheimer's Dementia (AD). AD leads to progressive and irreversible loss of brain activities such as memory, learning ability and cognitive functions. MTs help maintain cell shape, division, axonal transport, secretion and receptor activity. Tau through its binding with MT maintains those functions [1]. It includes 6 isoforms with 352 to 441 amino acids (aa) of which the 441aa form is the most abundant [2]. AD is characterized by the formation of (i) neurofibrillary tangles containing paired helical filaments (PHFs) composed of tau aggregates, and (ii) insoluble plaque containing aggregated amyloid beta (Aβ) peptide. Like Aβ, tau-aggregation has also become a major focus of AD research. Although the mechanism of tau aggregation is not well understood, it is linked to hyper and/or abnormal phosphorylation of Ser and/or Thr residues located at the N-terminal region. This aggregation possibly...

Keywords

Circular Dichroism Oligomeric Form Paired Helical Filament Circular Dichroism Study Aggregate Amyloid 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

References

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    Goedert, M, In Microtubules (Hyams & Lloyd, eds) 183–200, Wiley-Liss, NY, USA (1994).Google Scholar
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    Ko, L, et. al. Biochim. Biophys. Acta 1739, 125–139 (2005).Google Scholar
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    Yao, T.M. et. al. J. Biochem, 134, 91–99 (2003).CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, LLC 2009

Authors and Affiliations

  • Heather Palmer
    • 1
  • Ajoy Basak
    • 1
  1. 1.Hormones Growth and Development Program, Regional Protein Chemistry CenterOttawa Health Research InstituteOttawaCANADA

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