Phosphorylation of specific sets of tau isoforms reflects different neurofibrillary degeneration processes

FEBS Letters

Bussière, Thierry¹  Caillet-Boudin, Marie-Laure¹  Delacourte, André¹  Mailliot, Christel¹  Buée, Luc¹  Sergeant, Nicolas¹ 

[1] INSERM U422, Place de Verdun, F-59045 Lille Cedex, France

关键词: Alternative splicing;    Alzheimer's disease;    COS cell transfection;    Corticobasal degeneration;    Phosphorylation;    Pick's disease;    Progressive supranuclear palsy;    Tau protein;   

DOI  :  10.1016/S0014-5793(98)00910-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown