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Related Concept Videos

Selectins01:25

Selectins

Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain, which...
Role of Ephrin-Eph Signalling in Intestinal Stem Cell Renewal01:22

Role of Ephrin-Eph Signalling in Intestinal Stem Cell Renewal

Erythropoietin-producing hepatocellular carcinoma receptor (Eph) and its ligand, Eph receptor-interacting protein (Ephrin) were first discovered in the human carcinoma cell line, hence the name. Ephrin-Eph interaction guides cells to reach their appropriate location in adult tissues. They also play an essential role in the immune system by helping in immune cell migration, adhesion, and activation. Based on their structure and function, Eph is divided into two classes — EphA and EphB.
Adherens Junctions01:24

Adherens Junctions

Strong contact points between adjacent cells anchor them to each other, forming tissues. Such anchoring junctions are of two types –  adherens junctions and desmosomes. Adherens junctions are abundant in tissues such as  epithelium and endothelium, forming a continuous zone of adhesion called the adhesion belt. In other tissues, such as  heart muscle, they appear as clusters, linking the cells to produce coordinated heart muscle contraction.
Adherens Junctions are Dynamic
The endothelial cells...
Tight Junctions01:29

Tight Junctions

Tight junctions are molecular seals between cells that prevent the leaking of fluids, ions, and other small solutes across cavities and compartments in multicellular organisms. They are mainly composed of claudin and occludin transmembrane proteins, and other proteins such as tricellulin and JAM (junctional adhesion molecule). All these proteins are 4-pass transmembrane proteins, except JAM, which is a single-pass transmembrane protein belonging to the immunoglobulin superfamily. The...
Renewal of Intestinal Stem Cells01:23

Renewal of Intestinal Stem Cells

The intestinal epithelial lining rapidly renews every 4 to 5 days. The renewal is facilitated by intestinal stem cells (ISCs) located at the base of the crypt– a gland located at the bottom of each villus. ISCs divide asymmetrically to form new stem cells and progenitor daughter cells. The daughter cells are called transit-amplifying (TA) cells which move upwards along the crypt and either differentiate into absorptive cells– the enterocytes or secretory cells– including the goblet,...
Anchoring Junctions01:03

Anchoring Junctions

Anchoring junctions are multiprotein complexes that help cells connect to other cells and the extracellular matrix. Anchoring junctions are present on the lateral and basal surfaces of cells, providing strong and flexible connections. Focal adhesions are often formed due to cell interactions with the ECM substrata, which initiate signal transduction via kinase cascades and other mechanisms. Together, they provide stability and tissue integrity. There are three types of anchoring junctions:...

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Related Experiment Video

Updated: Jun 27, 2026

Human Colonoid Monolayers to Study Interactions Between Pathogens, Commensals, and Host Intestinal Epithelium
07:20

Human Colonoid Monolayers to Study Interactions Between Pathogens, Commensals, and Host Intestinal Epithelium

Published on: April 9, 2019

Lectin-epithelial interactions in the human colon.

Jonathan M Rhodes1, Barry J Campbell, Lu-Gang Yu

  • 1School of Clinical Sciences, University of Liverpool, Duncan Building, Liverpool, UK. rhodesjm@liverpool.ac.uk

Biochemical Society Transactions
|November 22, 2008
PubMed
Summary
This summary is machine-generated.

Glycosylation changes in the colon, including reduced O-glycans and increased sialyl-Tn and Thomsen-Friedenreich (TF) antigens, are linked to inflammatory bowel disease and colon cancer. These alterations affect epithelial cell interactions with lectins, potentially driving cancer metastasis.

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Studying the Epithelial Effects of Intestinal Inflammation In Vitro on Established Murine Colonoids
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Studying the Epithelial Effects of Intestinal Inflammation In Vitro on Established Murine Colonoids

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Human Colonoid Monolayers to Study Interactions Between Pathogens, Commensals, and Host Intestinal Epithelium
07:20

Human Colonoid Monolayers to Study Interactions Between Pathogens, Commensals, and Host Intestinal Epithelium

Published on: April 9, 2019

Studying the Epithelial Effects of Intestinal Inflammation In Vitro on Established Murine Colonoids
06:31

Studying the Epithelial Effects of Intestinal Inflammation In Vitro on Established Murine Colonoids

Published on: June 2, 2023

Area of Science:

  • Glycobiology
  • Oncology
  • Gastroenterology

Background:

  • Altered glycosylation patterns, including reduced O-glycan length, sulfation, and increased sialylation, are observed in colonic epithelium during inflammation (ulcerative colitis, Crohn's disease) and neoplastic conditions (colon cancer, adenomatous polyps).
  • These changes involve the aberrant expression of oncofetal carbohydrate antigens like sialyl-Tn and the Thomsen-Friedenreich (TF) antigen.

Purpose of the Study:

  • To investigate the functional consequences of altered colonic epithelial glycosylation, particularly the role of TF antigen expression.
  • To explore the interactions between modified epithelial glycoproteins and various lectins (dietary, microbial, human) and their impact on epithelial cell behavior.
  • To elucidate the mechanism by which TF antigen expression on cancer cells, via galectin-3 binding, promotes metastasis.

Main Methods:

  • Analysis of glycosylation changes in colonic epithelium in inflammatory and cancerous conditions.
  • Characterization of interactions between epithelial cells and different TF-binding lectins.
  • Investigation of galectin-3 binding to TF antigen on MUC1 in cancer cells and its effect on cell adhesion and metastasis.

Main Results:

  • Diverse effects of TF-binding lectins on epithelial cells, with some interactions (e.g., peanut lectin) potentially being biologically significant.
  • Increased TF expression on cancer cells facilitates binding to galectin-3, leading to MUC1 clustering and exposure of adhesion molecules.
  • This interaction promotes endothelial adhesion, a key mechanism in cancer metastasis, highlighting galectin-3 and TF as therapeutic targets.

Conclusions:

  • Glycosylation changes in epithelial diseases create specific binding sites for lectins, influencing cellular interactions and disease progression.
  • The interaction between cancer cell TF antigen and galectin-3 represents a significant pathway in metastasis and a potential therapeutic target.
  • Advanced tools enable detailed characterization of these glycosylation changes and lectin interactions, promising future research in epithelial diseases.