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Review
. 2017 Apr 15;45(2):545-553.
doi: 10.1042/BST20160164.

O-GlcNAcylation and cardiovascular disease

JaLessa N Wright  1 , Helen E Collins  1 , Adam R Wende  1 , John C Chatham  2
Affiliations
Review

O-GlcNAcylation and cardiovascular disease

JaLessa N Wright et al. Biochem Soc Trans. .

Abstract

The post-translational modification of serine and threonine residues of proteins found in numerous subcellular locations by O-linked N-acetylglucosamine (O-GlcNAc) is emerging as a key mediator of many cardiovascular pathophysiological processes. Early studies implicated increased protein O-GlcNAcylation as contributing to the cardiovascular complications associated with diabetes, whereas subsequent studies demonstrated that acute increases in O-GlcNAc levels were protective against ischemia/reperfusion injury. There is now a growing understanding that O-GlcNAc modification of proteins influences numerous cellular functions, including transcription, protein turnover, calcium handling, and bioenergetics. As a result, a more nuanced view of the role of protein O-GlcNAcylation in the cardiovascular system is emerging along with the recognition that it is required for normal cellular function and homeostasis. Consequently, the impact of changes in O-GlcNAc cycling due to stress or disease on the heart is complex and highly dependent on the specific context of these events. The goal of this review is to provide an overview of some of the more recent advances in our understanding of the role O-GlcNAcylation plays in mediating cardiovascular function and disease.

Keywords: O-GlcNAc; cardiac hypertrophy; cardiovascular physiology; diabetes; ischemia; myocardium.

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Conflict of interest statement

Competing Interests

The authors declare that there are no competing interests associated with this manuscript.

Figures

Figure 1
Figure 1. O-GlcNAcylation in Cardiovascular Function and Disease
Cellular signaling includes the protein post-translational modification (PTM) and regulation of proteins by O-linkage of N-acetylglucosamine (O-GlcNAc). Within the cardiovascular system this PTM confers both protection against ischemic injury and contributes to stem cell growth while in excess O-GlcNAc contributes to pathologic hypertrophy, contractile dysfunction, and decreased mitochondrial capacity. These changes occur throughout the cell in the nucleus to regulate gene expression, to mitochondria to decrease oxidative phosphorylation, within other membrane proteins to disrupt autophagy, and on contractile and Ca2+ handling proteins. Please see text for additional details. OGT, O-GlcNAc transferase; OXPHOS, oxidative phosphorylation; TF, transcription factor. This figure was produced using free images modified from Servier Medical Art (www.servier.com).
See this image and copyright information in PMC

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