title: Protein O-GlcNAcylation in diabetes and diabetic complications.
abstract: The post-translational modification of serine and threonine residues of proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) is highly ubiquitous, dynamic and inducible. Protein O-GlcNAcylation serves as a key regulator of critical biological processes including transcription, translation, proteasomal degradation, signal transduction and apoptosis. Increased O-GlcNAcylation is directly linked to insulin resistance and to hyperglycemia-induced glucose toxicity, two hallmarks of diabetes and diabetic complications. In this review, we briefly summarize what is known about protein O-GlcNAcylation and nutrient metabolism, as well as discuss the commonly used tools to probe changes of O-GlcNAcylation in cultured cells and in animal models. We then focus on some key proteins modified by O-GlcNAc, which play crucial roles in the etiology and progression of diabetes and diabetic complications. Proteomic approaches are also highlighted to provide a system view of protein O-GlcNAcylation. Finally, we discuss how aberrant O-GlcNAcylation on certain proteins may be exploited to develop methods for the early diagnosis of pre-diabetes and/or diabetes.
authors.affiliation: Department of Biological Chemistry, The Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205-2185, USA.
authors.forename: Junfeng
authors.initials: J
authors.lastname: Ma
authors.forename: Gerald W
authors.initials: GW
authors.lastname: Hart
mesh_terms: D000107:Acetylation; D000117:Acetylglucosamine / Q000378:metabolism*; D003920:Diabetes Mellitus / Q000209:etiology / Q000378:metabolism*; D006801:Humans; D020543:Proteome / Q000378:metabolism
chemical_list: D020543:Proteome; D000117:Acetylglucosamine