Abstract
Glycation and glycosylation are non-enzymatic and enzymatic reactions, respectively, of glucose, glucose metabolites, and other reducing sugars with different substrates, such as proteins, lipids, and nucleic acids. Increased availability of glucose is a recognized risk factor for the onset and progression of diabetes-mellitus-associated disorders, among which cardiovascular diseases have a great impact on patient mortality. Both advanced glycation end products, the result of non-enzymatic glycation of substrates, and O-linked-N-Acetylglucosaminylation, a glycosylation reaction that is controlled by O-N-AcetylGlucosamine (GlcNAc) transferase (OGT) and O-GlcNAcase (OGA), have been shown to play a role in cardiovascular remodeling. In this review, we aim (1) to summarize the most recent data regarding the role of glycation and O-linked-N-Acetylglucosaminylation as glucose-related pathogenetic factors and disease markers in cardiovascular remodeling, and (2) to discuss potential common mechanisms linking these pathways to the dysregulation and/or loss of function of different biomolecules involved in this field.
Highlights
advanced glycation end products (AGE) synthesis is mainly due to hyperglycemia, such as in diabetes mellitus (DM), and O-linked glycosylation, a type of glycosylation, as pathogenetic factors and disease their production is accelerated in any pathological condition characterized by increased markers in cardiovascular remodeling associated with metabolic disorders, and to discuss oxidative stress and inflammation, such as obesity, metabolic syndrome, as well as in many potential common mechanisms linking these pathways to dysregulation and/or loss of cardiovascular disorders, such as myocardial infarction and ischemia/reperfusion injury function of different biomolecules involved in this field
Unlike phosphorylation, which is regulated by multiple kinases and phosphatases, just two specific enzymes tightly control O-GlcNAcylation: O-glycosylation reaction that is controlled by O-N-AcetylGlucosamine (GlcNAc) transferase (OGT), which catalyzes the addition of GlcNAc to the hydroxyl group of serine or threonine residues, and O-GlcNAcase (OGA), which removes GlcNAc from proteins [119]
Glycation and O-GlcNAcylation are two glucose-related pathways that can affect the function of different substrates and activate responses leading to the onset and progression of many diseases associated with altered glucose metabolism, such as cardiovascular remodeling
Summary
Publisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations. Its main role is to confer defined properties to living cells and it is a normal part of protein biosynthesis [4] These types of protein modifications, namely glycation and glycosylation, seem to have little in common, both have been shown to promote the onset and progression of cardiovascular remodeling associated with metabolic disorders. AGE synthesis is mainly due to hyperglycemia, such as in diabetes mellitus (DM), and O-linked glycosylation, a type of glycosylation, as pathogenetic factors and disease their production is accelerated in any pathological condition characterized by increased markers in cardiovascular remodeling associated with metabolic disorders, and to discuss oxidative stress and inflammation, such as obesity, metabolic syndrome, as well as in many potential common mechanisms linking these pathways to dysregulation and/or loss of cardiovascular disorders, such as myocardial infarction and ischemia/reperfusion injury function of different biomolecules involved in this field. High levels of reactive oxygen species (ROS) and inflammatory mediators can promote
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