Neuroscience 2004 Abstract
| Presentation Number: | 787.13 |
|---|---|
| Abstract Title: | Tau phosphorylation and cleavage in non-AD tauopathies. |
| Authors: |
Guillozet-Bongaarts, A. L.*1
; Cahill, M. E.1
; Lapin, B. R.1
; Clark, F. A.1
; Berry, R. W.1
; Binder, L. I.1
1Dept Cell & Mol Biol, Northwestern Univ, Chicago, IL |
| Primary Theme and Topics |
Neurological and Psychiatric Conditions - Neurodegenerative Disorders -- Alzheimer's Disease: Tau |
| Secondary Theme and Topics | Neurological and Psychiatric Conditions<br />- Neurodegenerative Disorders<br />-- Other |
| Session: |
787. Tau and Tau Kinases: Human Studies and Animal Models Poster |
| Presentation Time: | Tuesday, October 26, 2004 1:00 PM-2:00 PM |
| Location: | San Diego Convention Center - Hall A-H, Board # SS25 |
| Keywords: | ALZHEIMER, DEMENTIA, CASPASE-3, CORTEX |
In Alzheimer’s disease (AD), tau is aberrantly processed, forming insoluble aggregates that are deposited in the form of neurofibrillary tangles. Phosphorylation at multiple sites, cleavage of the tau protein, and altered conformational states have been cited as possible avenues to tangle formation. Specifically, we have shown that cleavage at Asp421 by caspase enhances polymerization and is associated with increased apoptosis in neuronal cultures. In aging and AD, cleaved tau is evident in NFT, dystrophic neurites and neuropil threads. In vivo, tau appears to be phosphorylated at Ser422 prior to its cleavage; in vitro, this phosphorylation can slow caspase cleavage and inhibit polymerization of tau. In this study, we use immunohistochemistry to examine the presence of phospho-Ser422 and the Asp421 cleavage epitope in non-AD tauopathies including Pick's disease (PiD), corticobasal degeneration (CBD), and progressive supranuclear palsy (PSP). We show that Asp421-cleaved tau, which is prevalent in AD, is also present in Pick bodies, but fails to appear in either glial or neuronal pathologies associated with both CBD and PSP. Conversely, extensive phosphorylation at Ser422 was evident in all tauopathies examined, decorating both glial and neuronal lesions, and was colocalized with additional markers of early tau changes. Our results suggest that the formation of tau filaments in PiD, CBD and PSP follows a molecular course that is initially consistent with AD, but deviates later in filament evolution.
Supported by AG20506 and AG09466
Sample Citation:
[Authors]. [Abstract Title]. Program No. XXX.XX. 2004 Neuroscience Meeting Planner. San Diego, CA: Society for Neuroscience, 2004. Online.
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