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Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
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Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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Deciphering Protein O-GalNAcylation: Method Development and Disease Implication.

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Mucin-type O-glycosylation, especially truncated O-glycosylation (Tn antigen), is vital for mucosal barriers but its dysregulation is linked to diseases. New analytical methods are emerging to study this challenging glycan.

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Area of Science:

  • Biochemistry
  • Glycobiology
  • Immunology

Background:

  • Mucin-type O-glycosylation is a crucial post-translational modification on cell surface proteins, essential for biological functions and immune responses.
  • Highly O-glycosylated mucins form the mucosal barrier, protecting against pathogens. Dysregulation impairs this defense.
  • Truncated O-glycosylation (Tn antigen/O-GalNAcylation) is upregulated in diseases like cancer and autoimmune disorders.

Purpose of the Study:

  • To summarize recent advances in analytical methods for O-GalNAcylation enrichment and identification.
  • To highlight the biological role of the Tn antigen in various diseases.
  • To discuss the clinical implications of identifying aberrant O-GalNAcylation.

Main Methods:

  • Review of recent literature on analytical methods for O-GalNAcylation.
  • Analysis of the biological roles and disease associations of Tn antigen.
  • Discussion of clinical implications.

Main Results:

  • O-glycosylation, particularly Tn antigen, plays significant roles in health and disease.
  • Challenges exist in the reliable enrichment and identification of O-GalNAcylation compared to N-glycosylation.
  • Advances in analytical methods are improving the study of O-GalNAcylation.

Conclusions:

  • Understanding O-GalNAcylation is critical for deciphering its role in physiopathology and developing therapies.
  • Improved analytical techniques are needed for robust O-GalNAcylation characterization.
  • Aberrant O-GalNAcylation has significant clinical implications across various diseases.