Premium
Phosphorylation of specific sets of tau isoforms reflects different neurofibrillary degeneration processes
Author(s) -
Mailliot Christel,
Sergeant Nicolas,
Bussière Thierry,
Caillet-Boudin Marie-Laure,
Delacourte André,
Buée Luc
Publication year - 1998
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(98)00910-7
Subject(s) - progressive supranuclear palsy , corticobasal degeneration , gene isoform , exon , tau protein , tauopathy , phosphorylation , alzheimer's disease , biology , neurodegeneration , neuroscience , microbiology and biotechnology , pathology , biochemistry , disease , genetics , medicine , gene , atrophy
Tau proteins are the basic components of filaments that accumulate within neurons during neurofibrillary degeneration, a degenerating process with disease‐specific phenotypes. This specificity is likely to be sustained by both phosphorylation state and isoform content of tau aggregates that form neuronal inclusions. In the present study, characterization of tau isoforms involved in neurofibrillary degeneration in Alzheimer's disease, Pick's disease, corticobasal degeneration and progressive supra‐nuclear palsy was performed. Both analyses by immunoblotting using specific tau antibodies and cell transfection by tau isoform cDNAs allowed us to demonstrate the aggregation of (1) the six hyperphosphorylated tau isoforms in Alzheimer's disease, (2) tau isoforms without exon 10‐encoding sequence in Pick's disease and (3) hyperphosphorylated exon 10‐tau isoforms in corticobasal degeneration and progressive supranuclear palsy. Thus, neurofibrillary degeneration phenotypes are likely to be related to the phosphorylation of different combinations of tau isoforms (with and/or without exon 10‐encoding sequence) in subpopulations of neurons.