Generation and characterization of a rabbit monoclonal antibody site-specific for tau O-GlcNAcylated at serine 400

被引：27

作者：

Cameron, Andrew ^{[1
]}

Giacomozzi, Brandy ^{[1
]}

Joyce, John ^{[1
]}

Gray, Audrey ^{[1
]}

Graham, Danielle ^{[1
]}

Ousson, Solenne ^{[2
]}

Neny, Maud ^{[2
]}

Beher, Dirk ^{[2
]}

Carlson, George ^{[3
]}

O'Moore, Jill ^{[3
]}

Shearman, Mark ^{[1
]}

Hering, Heike ^{[1
]}

机构：

[1] EMD Serono Res & Dev Inst, Billerica, MA 01821 USA

[2] Asceneuron SA, Lausanne, Switzerland

[3] McLaughlin Res Inst, Great Falls, MT 59405 USA

来源：

FEBS LETTERS | 2013年 / 587卷 / 22期

关键词：

O-GlcNAc; Tau; Site-specific; Monoclonal antibody; OGA; N-ACETYLGLUCOSAMINE; CROSS-TALK; PHOSPHORYLATION; GLYCOSYLATION; DYNAMICS; ROLES;

D O I：

10.1016/j.febslet.2013.09.042

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Aggregation of tau into paired helical filaments is a pathological process leading to neurotoxicity in Alzheimer's disease and other tauopathies. Tau is posttranslationally modified by O-linked N-acetylglucosamine (O-GlcNAc), and increasing tau O-GlcNAcylation may protect against its aggregation. Research tools to study the relationship between tau aggregation and tau O-GlcNAcylation have not been widely available. Here we describe the generation of a rabbit monoclonal antibody specific for tau O-GlcNAcylated at Ser400 (O-tau(S400)). We show the utility of this antibody for in vitro and in vivo experiments to investigate the function of O-GlcNAc modifications of tau at Ser400. (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

引用

页码：3722 / 3728

页数：7

共 20 条

[1] Chemical approaches to study O-GlcNAcylation [J].