Target intelligence / Profile preview

Gastrointestinal epithelial surface glycans (GI glycans)

Target
GI glycans
Molecular classification
Carbohydrate, Glycoprotein, Glycolipid, Other
01

Overview

Gastrointestinal epithelial surface glycans are complex carbohydrate structures, including O-glycans and N-glycans, that are covalently attached to proteins and lipids on the apical surface of the intestinal epithelium (Essentials of Glycobiology, 2022). They form the structural backbone of the glycocalyx and the overlying mucus layer, acting as a primary defense mechanism and a mediator of host-microbe interactions (Nature Reviews Microbiology, 2020). These glycans serve as attachment sites for commensal microbiota, helping to maintain gut homeostasis, but are also exploited by pathogens like Helicobacter pylori and Rotavirus for colonization and entry (Cell Host & Microbe, 2018). In diseases such as ulcerative colitis and Crohn's disease, there is a documented shift in glycosylation patterns, often characterized by reduced complexity and increased expression of truncated glycans, which compromises the mucosal barrier (Gastroenterology, 2019). Therapeutic strategies targeting these glycans include the use of glycomimetics to competitively inhibit pathogen binding and the development of lectin-based delivery systems for site-specific drug release (Journal of Controlled Release, 2021). Furthermore, specific glycan epitopes like Sialyl-Lewis X serve as important biomarkers for inflammatory processes and neoplastic transformation in the gut (Clinical Cancer Research, 2020).

Other names
Gut glycocalyxMucosal glycansIntestinal surface carbohydratesEnterocyte surface glycansMucin-associated glycansGastrointestinal glycocalyx
02

Mechanism of action

Competitive inhibition of pathogen binding to epithelial receptors, enhancement of the protective mucosal barrier, and modulation of host-microbiota interactions through glycan-mimicry or binding.

03

Biological functions

Cell-cell recognitionMucosal barrier protectionPathogen adhesionMicrobiota modulationImmune responseSignal transduction
04

Disease associations

InfectionInflammationCancerInflammatory bowel diseaseGastritisColorectal cancer
05

Safety considerations

Disruption of commensal microbiotaOff-target binding to non-gastrointestinal tissuesPotential immunogenicity of synthetic glycomimeticsAlteration of nutrient absorptionSystemic toxicity if glycan-binding agents are absorbed
06

Interacting drugs

Sucralfate

5 more in the full profile.

07

Biomarkers

CA19-9 (Sialyl-Lewis A)Sialyl-Lewis XCarcinoembryonic antigen (CEA)MUC1 expression levelsTn antigen

Beyond the preview

Go deeper on Gastrointestinal epithelial surface glycans (GI glycans).

Explore the evidence, development activity, and competitive landscape with Gosset’s full data platform.

Drug pipeline

Full profile access

Explore the programs pursuing this target and their development progress.

  • Drug candidates
  • Developers
  • Development stage

Clinical trials

Full profile access

Follow the clinical studies evaluating therapies directed at this target.

  • Trial design
  • Status
  • Readouts

Competitive landscape

Full profile access

Compare approaches across drug candidates, modalities, and indications.

  • Programs
  • Modalities
  • Indications

Literature & evidence

Full profile access

Investigate the research and source evidence behind target biology and development.

  • Publications
  • Sources
  • Analysis

Patents

Full profile access

Explore patent activity around therapies and technologies addressing this target.

  • Patents
  • Assignees
  • Technologies

Research & analysis

Full profile access

Connect target biology, drug development, and emerging evidence in your research.

  • Biology
  • Development news
  • Analysis

Bring the full picture into focus.

See how Gosset can support your research on Gastrointestinal epithelial surface glycans (GI glycans).

Explore the full profile

Gosset Free

Get started with Gosset.

Enter your work email and we’ll be in touch with next steps.

Work email preferred.

Book a call