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Related Concept Videos

Protein Modifications in the RER01:26

Protein Modifications in the RER

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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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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.
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Mucosal Barrier of the Stomach01:25

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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.
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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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Functions of the Gut Microbiota01:18

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The gut microbiota includes trillions of microorganisms that colonize the human gastrointestinal tract, including bacteria, archaea, viruses, and fungi. This complex ecosystem plays a critical role in maintaining intestinal and systemic health. Most of these microbes inhabit the large intestine, establishing a relatively stable and diverse community that contributes to gut homeostasis through various metabolic, immunological, and protective mechanisms.Dominant bacterial phyla, such as...
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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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Updated: Mar 25, 2026

Three-dimensional Quantification of Intestinal Mucus Using Whole-mount Tissue Imaging
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Three-dimensional Quantification of Intestinal Mucus Using Whole-mount Tissue Imaging

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Ruminococcus gnavus E1 modulates mucin expression and intestinal glycosylation.

F Graziani1, A Pujol1, C Nicoletti1

  • 1iSm2 UMR 7313, CNRS, Centrale Marseille, Aix Marseille Université, Marseille, France.

Journal of Applied Microbiology
|February 13, 2016
PubMed
Summary
This summary is machine-generated.

Ruminococcus gnavus E1 enhances intestinal mucus production and glycosylation in goblet cells. This bacterium modifies the glycosylation pattern and MUC2 expression via a small, heat-stable peptide factor.

Keywords:
Ruminococcus gnavusglycosylationgoblet cellsgut microbiotahost-microbiota interactionsintestinal epithelial cells IECmucin

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Area of Science:

  • Microbiology
  • Gastroenterology
  • Immunology

Background:

  • Commensal bacteria and gut interactions are vital for intestinal homeostasis and health.
  • Ruminococcus gnavus is a significant Gram-positive anaerobic bacterium in the human gut microbiota.

Purpose of the Study:

  • To investigate the impact of Ruminococcus gnavus on intestinal mucus production and glycosylation patterns in goblet cells.

Main Methods:

  • Mono-association of mice with R. gnavus E1.
  • In vitro studies using human HT29-MTX cells.
  • Analysis of gene expression for mucin (MUC2) and glycosyltransferase enzymes.

Main Results:

  • R. gnavus E1 significantly increased the expression and glycosylation of intestinal glyco-conjugates in goblet cells.
  • This effect was observed in both mono-associated mice and HT29-MTX cells.
  • R. gnavus E1 induced mRNA levels for MUC2 and glycosyltransferase enzymes.

Conclusions:

  • R. gnavus E1 modulates the glycosylation profile of glyco-conjugates and mucus in goblet cells.
  • The bacterium utilizes a small, heat-stable peptide factor (<3 kDa) to alter glycosylation and MUC2 expression.