Phosphorylation and cleavage of tau in non-AD tauopathies

Angela L. Guillozet-Bongaarts*, Kelly E. Glajch, Emilie G. Libson, Michael E. Cahill, Eileen Bigio, Robert W. Berry, Lester I. Binder

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

49 Scopus citations

Abstract

The tau protein, well known as the primary component of neurofibrillary tangles, also comprises the Pick bodies found in Pick's disease (PiD) and the glial lesions associated with progressive supranuclear palsy (PSP) and cortico-basal ganglionic degeneration (CBD). Many of the tau alterations that are characteristic of Alzheimer's disease have also been identified in PSP and CBD. In this report, we examine three non-AD tauopathies (PSP, CBD, and PiD) for the presence of two specific tau alterations, phosphorylation at Ser422 and truncation at Asp421. We find that truncation at Asp421 is an alteration that is unique to neuronal lesions, occurring in Pick bodies as well as in neurofibrillary tangles, but not in lesions associated with glia. Conversely, phosphorylation at Ser422 is not only present in all these lesions, but identifies additional glial and neuronal pathology in disease-susceptible cortical regions. These results suggest that the molecular alterations of tau that occur during the initial process of tangle formation in AD are similar in non-AD tauopathies, but the middle and later changes are not common to all diseases.

Original languageEnglish (US)
Pages (from-to)513-520
Number of pages8
JournalActa Neuropathologica
Volume113
Issue number5
DOIs
StatePublished - May 1 2007

Keywords

  • Astrocytes
  • Caspase
  • Cortico-basal ganglionic degeneration
  • Pick's disease
  • Progressive supranuclear palsy

ASJC Scopus subject areas

  • Pathology and Forensic Medicine
  • Clinical Neurology
  • Cellular and Molecular Neuroscience

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