title: Multiple tissue-specific roles for the O-GlcNAc post-translational modification in the induction of and complications arising from type II diabetes.
abstract: In this minireview, we will highlight work in the last 30 years that has clearly demonstrated that the O-GlcNAc modification is nutrient-responsive and plays multiple roles in metabolic regulation of signaling and gene expression. Further, we will examine recent studies that have investigated the impact of O-GlcNAc in a variety of glucose- and insulin-responsive tissues and the roles attributed to O-GlcNAc in the induction of insulin resistance and glucose toxicity, the hallmarks of type II diabetes mellitus. We will also summarize potential causal roles for the O-GlcNAc modification in complications associated with diabetes.
authors.affiliation: From the Department of Biochemistry and Molecular Biology and Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia 30602-1516.
authors.forename: Krithika
authors.initials: K
authors.lastname: Vaidyanathan
authors.affiliation: From the Department of Biochemistry and Molecular Biology and Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia 30602-1516 lwells@ccrc.uga.edu.
authors.forename: Lance
authors.initials: L
authors.lastname: Wells
mesh_terms: D000117:Acetylglucosamine / Q000378:metabolism*; D000818:Animals; D003924:Diabetes Mellitus, Type 2 / Q000150:complications* / Q000378:metabolism* / Q000473:pathology; D006801:Humans; D007328:Insulin / Q000378:metabolism; D009928:Organ Specificity; D011499:Protein Processing, Post-Translational; D015398:Signal Transduction
chemical_list: D007328:Insulin; D000117:Acetylglucosamine
keywords: Diabetes; Hexosamine Biosynthetic Pathway; Insulin Resistance; O-GlcNAcylation; O-linked N-Acetylglucosamine (O-GlcNAc); OGA; OGT; Type 2 Diabetes