Journal of Glycomics & Lipidomics
Open Access

Role of Carbohydrates Glycosylation Modification in Health and Disease

Sarah Jacob^{* *}Correspondence: Sarah Jacob, Department of Food Science, University of Nebraska, Lincoln, Nebraska, USA, Email:

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Description

Glycoxylation, also known as oxidative glycosylation, is a posttranslational modification of proteins where a carbohydrate molecule is covalently attached to a protein amino acid residue in the presence of an oxidizing agent. This modification has been observed in various organisms, including mammals, plants, and fungi, and has been implicated in a variety of biological processes such as cell signaling, immune response, and protein folding. The process of glycoxylation involves the oxidation of a protein amino acid residue, typically a lysine or arginine, to form an aldehyde or ketone group. This reactive group then reacts with a nearby carbohydrate molecule, forming a covalent linkage known as a glycosylamine. The resulting glycosylated protein, or glycoprotein, contains a carbohydrate moiety that can affect the protein's function, stability, and localization.

The entire collection of glycoconjugates, which are made up of glycans carbohydrate chains that are covalently attached to lipid or protein molecules is referred to as the glycome. Glycan sequences, connections between them, and length of glycoconjugates can all vary due to the glycosylation process those results in their formation. Glycoconjugate synthesis is a dynamic process that is influenced not only by the cell types involved but also by cellular signals and the local milieu of enzymes, sugar precursors, and organelle structures.

One of the well-examined examples of glycoxylation is the formation of Advanced Glycation End Products (AGEs), which are a class of proteins modified by non-enzymatic glycation and oxidation reactions. AGEs are formed when reducing sugars such as glucose or fructose react with proteins in a process known as the Maillard reaction. This reaction leads to the formation of a Schiff base intermediate, which undergoes a series of rearrangements and oxidations to form AGEs such as Carboxymethyllysine (CML) and pentosidine. AGEs are implicated in various pathologies, including diabetes, atherosclerosis, and neurodegenerative diseases. They can contribute to tissue damage by cross-linking proteins, altering their structure and function, and promoting inflammation and oxidative stress. Glycoxylation, as a process that generates AGEs, can therefore have significant biological and clinical implications.

Glycoxylation has also been implicated in other biological processes. For example, the glycoxylation of the complement component C3 has been shown to modulate its interaction with complement receptor 1, affecting its ability to activate the complement system. Glycoxylation of the extracellular matrix protein fibronectin has been shown to affect its binding to integrin receptors and modulate cell adhesion and migration. In addition to its biological roles, glycoxylation has also been understood for its potential applications in biotechnology and medicine. For example, glycoxylation can be used to modify the properties of therapeutic proteins, such as antibodies and enzymes, by improving their stability, half-life, and immunogenicity. Glycoxylation can also be used to generate glycan-conjugate vaccines, where a protein antigen is linked to a carbohydrate moiety to enhance its immunogenicity.

Conclusion

Glycoxylation is a post-translational modification of proteins that involves the covalent attachment of a carbohydrate moiety in the presence of an oxidizing agent. This modification has been implicated in various biological processes and has significant clinical and biotechnological implications. Further evaluation into glycoxylation and its role in health and disease may lead to the development of novel therapeutic strategies and biomarkers. In infectious diseases, glycosylation plays a crucial role. Glycans, the structures of pathogens, carbohydrates, are involved in numerous important interactions with hosts. Pathogen adhesion, recognition, invasion, and immune evasion can all be mediated by glycan interactions.