A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2008-06-29

AUTHORS

Scott A Yuzwa, Matthew S Macauley, Julia E Heinonen, Xiaoyang Shan, Rebecca J Dennis, Yuan He, Garrett E Whitworth, Keith A Stubbs, Ernest J McEachern, Gideon J Davies, David J Vocadlo

ABSTRACT

Pathological hyperphosphorylation of the microtubule-associated protein tau is characteristic of Alzheimer's disease (AD) and the associated tauopathies. The reciprocal relationship between phosphorylation and O-GlcNAc modification of tau and reductions in O-GlcNAc levels on tau in AD brain offers motivation for the generation of potent and selective inhibitors that can effectively enhance O-GlcNAc in vertebrate brain. We describe the rational design and synthesis of such an inhibitor (thiamet-G, K(i) = 21 nM; 1) of human O-GlcNAcase. Thiamet-G decreased phosphorylation of tau in PC-12 cells at pathologically relevant sites including Thr231 and Ser396. Thiamet-G also efficiently reduced phosphorylation of tau at Thr231, Ser396 and Ser422 in both rat cortex and hippocampus, which reveals the rapid and dynamic relationship between O-GlcNAc and phosphorylation of tau in vivo. We anticipate that thiamet-G will find wide use in probing the functional role of O-GlcNAc in vertebrate brain, and it may also offer a route to blocking pathological hyperphosphorylation of tau in AD. More... »

PAGES

483-490

References to SciGraph publications

Journal

TITLE

Nature Chemical Biology

ISSUE

8

VOLUME

4

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nchembio.96

DOI

http://dx.doi.org/10.1038/nchembio.96

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1050435297

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/18587388


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