The complex relationship between soluble and insoluble tau in tauopathies revealed by efficient dephosphorylation and specific antibodies.

Abstract

Phosphorylated tau is deposited as insoluble inclusion bodies in the tauopathies. We have used a new efficient method to dephosphorylate tau extracted from control and tauopathy brain. In some tauopathies, including Alzheimer's disease and progressive supranuclear palsy, the pattern of insoluble tau isoforms reflected that of soluble tau. In contrast, in corticobasal degeneration, Pick's disease, and some forms of fronto-temporal dementia, specific tau isoforms were selectively sequestered into insoluble inclusion-forming tau. Therefore the overall expression of individual tau isoforms does not predict which tau isoforms are deposited in all tauopathies and different mechanisms must operate that result in the deposition of specific tau isoforms.

• Authors: D P Hanger, G M Gibb, R de Silva, A Boutajangout, J-P Brion, T Revesz, A J Lees, B H Anderton
• Journal: FEBS letters (FEBS Lett) Vol. 531 Issue 3 Pg. 538-42 (Nov 20 2002) ISSN: 0014-5793 [Print] England
• PMID: 12435607 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Protein Isoforms
• tau Proteins

Topics

• Amino Acid Sequence
• Blotting, Western
• Brain (metabolism)
• Brain Diseases (metabolism)
• Electrophoresis, Polyacrylamide Gel
• Humans
• Molecular Sequence Data
• Phosphorylation
• Protein Isoforms (metabolism)
• Solubility
• tau Proteins (metabolism)