Abstract
O-GlcNAcylation is a ubiquitous and reversible post-translational protein modification that has recently gained renewed interest due to the rapid development of analytical tools and new molecules designed to specifically increase the level of protein O-GlcNAcylation. The level of O-GlcNAc modification appears to have either deleterious or beneficial effects, depending on the context (exposure time, pathophysiological context). While high O-GlcNAcylation levels are mostly reported in chronic diseases, the increase in O-GlcNAc level in acute stresses such as during ischemia reperfusion or hemorrhagic shock is reported to be beneficial in vitro, ex vivo, or in vivo. In this context, an increase in O-GlcNAc levels could be a potential new cardioprotective therapy, but the ambivalent effects of protein O-GlcNAcylation augmentation remains as a key problem to be solved prior to their transfer to the clinic. The emergence of new analytical tools has opened new avenues to decipher the mechanisms underlying the beneficial effects associated with an O-GlcNAc level increase. A better understanding of the exact roles of O-GlcNAc on protein function, targeting or stability will help to develop more targeted approaches. The aim of this review is to discuss the mechanisms and potential beneficial impact of O-GlcNAc modulation, and its potential as a new clinical target in cardiology.
Highlights
Definition, Pathway, and RegulationThe O-N-acetyl glucosaminylation, commonly known as O-GlcNAcylation, is a reversible posttranslational modification (PTM) that involves the addition of the monosaccharide β-D-Nacetylglucosamine to serine and threonine residues of proteins
The first enzyme, glutamine fructose-6P amidotransferase (GFAT) uses glutamine and 2 to 5% of glycolytic fructose-6-P to perform the first step of the HBP
Glutamine supplementation is recommended for parenteral or enteral supplementation in neonatal, pediatric and adult intensive care units and seems to be safe [26, 27]
Summary
The O-N-acetyl glucosaminylation, commonly known as O-GlcNAcylation, is a reversible posttranslational modification (PTM) that involves the addition of the monosaccharide β-D-Nacetylglucosamine to serine and threonine residues of proteins. It was first described by Torres and Hart on the internal surface of plasma membranes of lymphocytes [1]. Little attention was paid to this minor sugar moiety, probably because the tools available to study this PTM were limited Detecting it is difficult as it cannot be studied with classic techniques such as electrophoresis or high pressure liquid chromatography (HPLC) as the Cardiac Improvements Through Protein O-GlcNAcylation
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