What Is Protein Glycosylation (Protein Glycosylation Modification)
Protein glycosylation is a common form of post-translational modification in cells, wherein one or more sugar moieties are covalently attached to specific amino acid residues of a target protein. This process primarily takes place in the endoplasmic reticulum and Golgi apparatus. Glycosylation is generally categorized into two major types: N-glycosylation, in which glycans are linked to the amide group of asparagine residues, and O-glycosylation, where sugars are attached to the hydroxyl groups of serine or threonine residues. In addition, less common forms such as C-glycosylation and S-glycosylation also exist.
Protein glycosylation plays a critical role in preserving the structural integrity and functional properties of proteins. It influences protein stability, biological activity, solubility, as well as distribution and half-life in vivo. For instance, the glycosylation of antibodies within the immune system can modulate their antigen-binding specificity. Moreover, glycosylation is essential for intercellular communication and signal transduction; for example, the functionality of cell adhesion molecules often relies on their glycosylation state.
Aberrant glycosylation is implicated in the pathogenesis of numerous diseases. In cancer, alterations in glycosylation patterns may disrupt cell–cell and cell–matrix interactions, thereby facilitating tumor invasion and metastasis. In diabetes, dysregulated glycosylation can contribute to cellular dysfunction and subsequent tissue injury.
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