doi: 10.1161/01.RES.0000103190.20260.37
© 2003 American Heart Association, Inc.
Reviews |
Proteomic Approaches to Analyze the Dynamic Relationships Between Nucleocytoplasmic Protein Glycosylation and Phosphorylation
From Johns Hopkins University School of Medicine, Department of Biological Chemistry, Baltimore, Md.
Correspondence to Gerald W. Hart, Department of Biological Chemistry, Johns Hopkins University School of Medicine, 725 N Wolfe St, Baltimore, MD. E-mail gwhart{at}jhmi.edu
Jennifer E. Van Eyk Guest Editor This Review is part of a thematic series on Proteomics, which includes the following articles:
Cardiovascular Proteomics: Evolution and Potential
Applied Proteomics: Mitochondrial Proteins and Effect on Function
Organelle Proteomics: Implications for Subcellular Fractionation in Proteomics
Identification of Novel Signaling Complexes by Functional Proteomics
Proteomic Approaches to Analyze the Dynamic Relationships Between Nucleocytoplasmic Protein Glycosylation and Phosphorylation
Proteomics in the Cardiomyopathies and Heart Failure: A Step Beyond Genomics
Glycosylation of Apolipoprotein E
O-linked ß-N-acetylglucosamine (O-GlcNAc) is both an abundant and dynamic posttranslational modification similar to phosphorylation that occurs on serine and threonine residues of cytosolic and nuclear proteins in all metazoans and cell types examined, including cardiovascular tissue. Since the discovery of O-GlcNAc more than 20 years ago, the elucidation of O-GlcNAc as a posttranslational modification has been slow, albeit similar to the rate of acceptance of phosphorylation, because of the lack of tools available for its study. Identifying O-GlcNAc posttranslational modifications on proteins is a major challenge to proteomics. The recent development of mild ß-elimination followed by Michael addition with dithiothreitol has significantly improved the site mapping of both O-GlcNAc and O-phosphate in functional proteomics. ß-Elimination followed by Michael addition with dithiothreitol facilitates the study of the labile O-GlcNAc modification in the etiology of disease states. We discuss how recent technological innovations will expand our present understanding of O-GlcNAc and what the implications are for diabetes and cardiovascular complications.
Key Words: O-linked ß-N-acetylglucosamine • proteomics • BEMAD • OGT • O-GlcNAcase
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