Phosphorylation of soluble tau differs in Pick's disease and Alzheimer's disease brains

Janet van Eersel, Mian Bi, Yazi D. Ke, John R. Hodges, John H. Xuereb, Gillian C. Gregory, Glenda M. Halliday, Jürgen Götz, Jillian J. Kril, Lars M. Ittner

Research output: Contribution to journalArticlepeer-review

31 Citations (Scopus)


Frontotemporal lobar degeneration (FTLD) is a common cause of presenile dementia characterised by behavioural and language disturbances. Pick's disease (PiD) is a subtype of FTLD, which presents with intraneuronal inclusions consisting of hyperphosphorylated tau protein aggregates. Although Alzheimer's disease (AD) is also characterised by tau lesions, these are both histologically and biochemically distinct from the tau aggregates found in PiD. What determines the distinct characteristics of these tau lesions is unknown. As phosphorylated, soluble tau has been suggested to be the precursor of tau aggregates, we compared both the level and phosphorylation profile of tau in tissue extracts of AD and PiD brains to determine whether the differences in the tau lesions are reflected by differences in soluble tau. Levels of soluble tau were decreased in AD but not PiD. In addition, soluble tau was phosphorylated to a greater extent in AD than in PiD and displayed a different phosphorylation profile in the two disorders. Consistently, tau kinases were activated to different degrees in AD compared with PiD. Such differences in solubility and phosphorylation may contribute, at least in part, to the formation of distinct tau deposits, but may also have implications for the clinical differences between AD and PiD.

Original languageEnglish
Pages (from-to)1243-1251
Number of pages9
JournalJournal of Neural Transmission
Issue number10
Publication statusPublished - 1 Oct 2009
Externally publishedYes


  • Alzheimer's disease
  • ERK
  • Frontotemporal lobar degeneration
  • Phosphorylation
  • Pick's disease
  • Tau


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