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Published on Web 12/09/2006 GlcNAcstatin: a Picomolar, Selective O-GlcNAcase Inhibitor That Modulates Intracellular O-GlcNAcylation Levels

By Helge C. Dorfmueller, Vladimir S. Borodkin, Marianne Schimpl, Sharon M. Shepherd, Natalia A. Shpiro and Daan M. F. Van Aalten

Abstract

Many proteins in the eukaryotic cell are modified by O-linked N-acetylglucosamine (O-GlcNAc) on serines and threonines. 1 O-GlcNAcylation has been shown to be important for regulation of the cell cycle, DNA transcription and translation, insulin sensitivity, and protein degradation. 2,3 Misregulation of O-GlcNAcylation is associated with diabetes and Alzheimer’s disease. 2,4,5 Two enzymes are involved in the dynamic cycling of this posttranslational modification, the O-GlcNAc transferase (OGT, classified as CAZY6 family GT41) and O-GlcNAcase (OGA, GH84). PUGNAc (O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate), a nanomolar inhibitor of OGA, has been extensively used to induce and study the effects of raised O-GlcNAc levels in the cell. 7,8 However, PUGNAc is also a potent inhibitor of the human lysosomal hexosaminidases HexA and HexB, inactivation of which has been associated with the Tay-Sachs an

Year: 2006
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