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Related Concept Videos

Proteoglycans01:05

Proteoglycans

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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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Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
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Protein Glycosylation01:25

Protein Glycosylation

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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.
Glycosylation occurs in...
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Mucosal Barrier of the Stomach01:25

Mucosal Barrier of the Stomach

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The gastric glands contain parietal cells that secrete hydrochloric acid (HCl) for digestion. The cells secrete HCl because it is highly corrosive and essential for breaking down food. To achieve this, they secrete hydrogen and chloride ions into the lumen of the gastric glands, which combine to form HCl.
Within parietal cells, carbonic acid is first formed through the reaction of water and carbon dioxide. The dissociation of carbonic acid releases bicarbonate and hydrogen ions. The bicarbonate...
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Pathophysiology of Peptic Ulcer Disease: Mucosal Defense Factors01:24

Pathophysiology of Peptic Ulcer Disease: Mucosal Defense Factors

1.1K
Peptic ulcer disease, commonly called PUD, represents a multifaceted condition characterized by disruptions in the lining of the gastrointestinal (GI)  tract. Central to the protection of the gastrointestinal lining is the mucosal-bicarbonate barrier. This physiological defense mechanism is a formidable shield against the corrosive effects of gastric acid and pepsin secretion in the stomach. Its role is pivotal in maintaining the structural integrity of the stomach's inner lining.
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Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

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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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Related Experiment Video

Updated: Jan 10, 2026

Profiling of Permethylated Mucin O-glycans Using Matrix-assisted Laser Desorption/Ionization Time-of-flight Mass Spectrometry
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Profiling of Permethylated Mucin O-glycans Using Matrix-assisted Laser Desorption/Ionization Time-of-flight Mass Spectrometry

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Intestinal Mucin Glycosylation: Structural Regulation, Homeostasis Maintenance and Disease Association.

Yunye Li1, Jia Pan1, Huimin Liu1

  • 1Department of Physiology, School of Medicine, Shandong University of Traditional Chinese Medicine, No. 4655, Daxue Road, Changqing District, Jinan 250355, China.

Biomolecules
|November 27, 2025
PubMed
Summary

Mucin glycosylation is vital for intestinal barrier integrity and gut health. Altered glycosylation compromises the barrier, leading to inflammation, dysbiosis, and diseases like colitis and colorectal cancer.

Keywords:
gut microbiotainflammatory bowel disease (IBD)intestinal barrierintestinal homeostasismucin glycosylation

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Area of Science:

  • Gastroenterology
  • Immunology
  • Microbiology

Background:

  • The intestinal barrier protects against pathogens and maintains homeostasis.
  • Mucins and their glycosylation are key structural components of this barrier.
  • Disrupted barrier function is linked to intestinal inflammation and diseases.

Purpose of the Study:

  • To review classifications and structures of intestinal mucin glycosylation.
  • To elucidate the role of mucin glycosylation in barrier function and disease.
  • To highlight implications for diagnosis and therapy of intestinal diseases.

Main Methods:

  • Literature review of mucin glycosylation in intestinal health and disease.
  • Analysis of structural features and functional roles of mucin glycans.
  • Exploration of pathological alterations and therapeutic strategies.

Main Results:

  • Mucin glycans are critical for mucus barrier integrity, immune modulation, and microbiota shaping.
  • Proper glycosylation maintains barrier function and a balanced gut ecosystem.
  • Disrupted glycosylation compromises barrier function, promotes dysbiosis, and contributes to colitis and colorectal cancer.

Conclusions:

  • Mucin glycosylation is crucial for preserving intestinal barrier integrity.
  • Alterations in mucin glycosylation are implicated in various intestinal disorders.
  • Understanding mucin glycosylation offers potential for precision diagnosis and targeted therapies.