Alzheimer's disease:: just another tauopathy?

被引:4
|
作者
Buée, L [1 ]
Delacourte, A [1 ]
机构
[1] INSERM, U422, Inst Med Predict & Rech Therapeut, F-59045 Lille, France
来源
M S-MEDECINE SCIENCES | 2002年 / 18卷 / 6-7期
关键词
D O I
10.1051/medsci/20021867727
中图分类号
R-3 [医学研究方法]; R3 [基础医学];
学科分类号
1001 ;
摘要
Tau proteins belong to the family of microtubule-associated proteins. They are mainly expressed in neurons where they play an important role in the assembly of tubulin monomers into microtubules to constitute the neuronal microtubule network. Tau proteins ore translated from a single gene located on chromosome 17. Their expression is developmentally regulated by an alternative splicing mechanism and six different isoforms exist in the human adult brain. Tau proteins are the major constituents of fibrillar lesions described in Alzheimer's disease and numerous neurodegenerative disorders referred to as << tauopathies >>. Molecular analysis has revealed that an abnormal phosphorylation might be one of the important events in the process leading to their aggregation. Moreover, a specific set of pathological tau proteins exhibiting a typical biochemical pattern, and a different regional and laminar distribution could characterize each of these disorders. Finally, the recent discovery of tau gene mutations in frontotemporal dementia with parkinsonism linked to chromosome 17 has reinforced the direct role attributed to tau proteins in the pathogenesis of neurodegenerative disorders, and underlined the fact that distinct sets of tau isoforms expressed in different neuronal populations could lead to different pathologies. Based on these findings, new animal and cell models are developed and should allow for a better understanding of neurofibrillary degeneration.
引用
收藏
页码:727 / 736
页数:10
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