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O-GlcNAc Modification: Friend or Foe in Diabetic Cardiovascular Disease
Udayakumar Karunakaran1, Nam Ho Jeoung
1Department of Medical Sciences, Kyungpook National University School of Medicine, Daegu, Korea.
Abstract:
O-Linked β-N-acetyl glucosaminylation (O-GlcNAcylation) is a dynamic post-translational modification that occurs on serine and threonine residues of cytosolic and nuclear proteins in all cell types, including those involved in the cardiovascular system. O-GlcNAcylation is thought to act in a manner analogous to protein phosphorylation. O-GlcNAcylation rapidly cycles on/off proteins in a time scale similar to that for phosphorylation/dephosphorylation of proteins. Several studies indicate that O-GlcNAc might induce nuclear localization of some transcription factors and may affect their DNA binding activities. However, at the cellular level, it has been shown that O-GlcNAc levels increase in response to stress and augmentation of this response suppresses cell survival. Increased levels of O-GlcNAc have been implicated as a pathogenic contributor to glucose toxicity and insulin resistance, which are major hallmarks of type 2 diabetes and diabetes-related cardiovascular complications. Thus, O-GlcNAc and its metabolic functions are not yet well-understood; focusing on the role of O-GlcNAc in the cardiovascular system is a viable target for biomedical investigation. In this review, we summarize our current understanding of the role of O-GlcNAc on the regulation of cell function and survival in the cardiovascular system.
Insights
O-Linked β-N-acetyl glucosaminylation (O-GlcNAcylation) is a dynamic protein modification impacting cardiovascular cells. Understanding its role in cell survival and disease is crucial for biomedical research.
Area of Science:
- Biochemistry
- Molecular Biology
- Cardiovascular Biology
Background:
- O-Linked β-N-acetyl glucosaminylation (O-GlcNAcylation) is a dynamic post-translational modification occurring on serine/threonine residues in cytosolic and nuclear proteins.
- This modification cycles rapidly, similar to protein phosphorylation, and influences transcription factor activity and localization.
- Elevated O-GlcNAcylation is linked to cellular stress, reduced cell survival, glucose toxicity, and insulin resistance, particularly in diabetes-related cardiovascular complications.
Purpose of the Study:
- To review the current understanding of O-GlcNAcylation's role in cardiovascular cell function and survival.
- To highlight O-GlcNAcylation as a significant target for biomedical investigation within the cardiovascular system.
Main Methods:
- Literature review summarizing existing research on O-GlcNAcylation in the cardiovascular system.
- Analysis of studies investigating the impact of O-GlcNAcylation on cellular processes and disease states.
Main Results:
- O-GlcNAcylation influences cell function and survival in cardiovascular tissues.
- Increased O-GlcNAcylation is associated with detrimental effects, including impaired cell survival and contribution to diabetic cardiovascular complications.
Conclusions:
- O-GlcNAcylation plays a critical role in regulating cardiovascular cell function and survival.
- Further research into O-GlcNAcylation's metabolic functions is warranted for understanding and treating cardiovascular diseases.
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