MONOCLONAL-ANTIBODY AT8 RECOGNIZES TAU-PROTEIN PHOSPHORYLATED AT BOTH SERINE-202 AND THREONINE-205

被引：521

作者：

GOEDERT, M ^{[1
]}

JAKES, R ^{[1
]}

VANMECHELEN, E ^{[1
]}

机构：

[1] INNOGENET,B-9052 GHENT,BELGIUM

来源：

NEUROSCIENCE LETTERS | 1995年 / 189卷 / 03期

关键词：

TAU PROTEIN; PHOSPHORYLATION; ALZHEIMERS DISEASE;

D O I：

10.1016/0304-3940(95)11484-E

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

Hyperphosphorylated microtubule-associated protein tau is the major component of the paired helical filament of Alzheimer's disease, Phosphorylation-dependent anti-tau antibodies are being used to identify specific amino acids that are phosphorylated in tau from normal brain and Alzheimer's disease brain. As such, monoclonal antibody AT8 is widely used. By a combination of site-directed mutagenesis of recombinant tan and in vitro phosphorylation, we show that AT8 requires tau protein to be phosphorylated at both serine 202 and threonine 205 (using the numbering of the longest human brain tan isoform).

引用

页码：167 / 170

页数：4

共 24 条

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