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The complex relationship between soluble and insoluble tau in tauopathies revealed by efficient dephosphorylation and specific antibodies
Author(s) -
Hanger D.P,
Gibb G.M,
de Silva R,
Boutajangout A,
Brion J.-P,
Revesz T,
Lees A.J,
Anderton B.H
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03611-6
Subject(s) - tauopathy , progressive supranuclear palsy , corticobasal degeneration , gene isoform , tau protein , dephosphorylation , tau pathology , chemistry , inclusion bodies , biochemistry , neuroscience , phosphorylation , microbiology and biotechnology , alzheimer's disease , biology , disease , neurodegeneration , medicine , phosphatase , escherichia coli , gene
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.