Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Protein Glycosylation01:25

Protein Glycosylation

9.9K
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...
9.9K
Glycocalyx and its Functions01:14

Glycocalyx and its Functions

9.2K
The glycocalyx is a carbohydrate-rich, fuzzy-appearing layer on the outer surface of the cell membrane. It is highly hydrophilic, because of this it attracts large amounts of water to the cell's surface. This aids the cell's interaction with the watery environment and also helps it to obtain substances dissolved in the water. It is also important for cell identification, self/non-self determination, and embryonic development and is used in cell-to-cell attachments to form tissues.
9.2K
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

3.7K
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...
3.7K
Proteoglycans01:05

Proteoglycans

4.9K
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,...
4.9K
Matrix Proteoglycans and Glycoproteins01:21

Matrix Proteoglycans and Glycoproteins

5.3K
Proteoglycans are extensively glycosylated proteins, commonly found in the extracellular matrix, interwoven with collagen fibers. Hyaline cartilage, the most common type of cartilage in the body, consists of short and dispersed collagen fibers associated with large amounts of proteoglycans. These proteoglycans have long negative charges that attract cations, which in turn attract water molecules. This influx of ions and water molecules swells up the proteoglycan like a water-soaked gel that can...
5.3K
Selectins01:25

Selectins

4.4K
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,...
4.4K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Unraveling the GM<sub>1</sub> Specificity of Galectin‑1 Binding to Lipid Membranes.

ACS bio & med chem Au·2025
Same author

Cysteine Oxidation in Human Galectin-1 Occurs Sequentially via a Folded Intermediate to a Fully Oxidized Unfolded Form.

International journal of molecular sciences·2024
Same author

Altering the Modular Architecture of Galectins Affects its Binding with Synthetic α-Dystroglycan O-Mannosylated Core M1 Glycoconjugates In situ.

Chembiochem : a European journal of chemical biology·2023
Same author

Targeting osteoarthritis-associated galectins and an induced effector class by a ditopic bifunctional reagent: Impact of its glycan part on binding measured in the tissue context.

Bioorganic & medicinal chemistry·2022
Same author

Exploring the In situ pairing of human galectins toward synthetic O-mannosylated core M1 glycopeptides of α-dystroglycan.

Scientific reports·2022
Same author

Structure of Galectin-3 bound to a model membrane containing ganglioside GM1.

Biophysical journal·2022

Related Experiment Video

Updated: Feb 19, 2026

Author Spotlight: Advancing Protein Glycosylation Research Using a Fully Automated System
05:19

Author Spotlight: Advancing Protein Glycosylation Research Using a Fully Automated System

Published on: June 28, 2024

1.4K

Glycans: bioactive signals decoded by lectins.

Hans-Joachim Gabius1

  • 1Department of Veterinary Sciences, Faculty of Veterinary Medicine, Ludwig-Maximilians-University Munich, Munich, Germany. gabius@tiph.vetmed.uni-muenchen.de

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

Oligosaccharides, or glycans, are powerful biological signals due to their complex structures and ability to form specific interactions. Understanding glycan-lectin binding is key for medical applications and disease biomarker development.

More Related Videos

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
11:21

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions

Published on: January 20, 2022

4.1K
Glycan Node Analysis: A Bottom-up Approach to Glycomics
11:36

Glycan Node Analysis: A Bottom-up Approach to Glycomics

Published on: May 22, 2016

11.2K

Related Experiment Videos

Last Updated: Feb 19, 2026

Author Spotlight: Advancing Protein Glycosylation Research Using a Fully Automated System
05:19

Author Spotlight: Advancing Protein Glycosylation Research Using a Fully Automated System

Published on: June 28, 2024

1.4K
Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
11:21

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions

Published on: January 20, 2022

4.1K
Glycan Node Analysis: A Bottom-up Approach to Glycomics
11:36

Glycan Node Analysis: A Bottom-up Approach to Glycomics

Published on: May 22, 2016

11.2K

Area of Science:

  • Carbohydrate Chemistry
  • Biochemistry
  • Molecular Biology

Background:

  • Cellular glycoconjugates utilize glycans for biochemical signaling.
  • Oligosaccharides possess exceptional coding capacity due to structural factors like linkage variability, branching, and conformation.
  • Protein folds have evolved to recognize specific glycans, leveraging hydrogen bonds and C-H/pi-interactions.

Purpose of the Study:

  • To explore the coding potential of oligosaccharides in biological signaling.
  • To elucidate the structural and thermodynamic factors governing glycan-lectin interactions.
  • To demonstrate the physiological and medical relevance of glycan-lectin orchestration in disease models.

Main Methods:

  • Analysis of glycan structural features contributing to coding capacity (linkage, anomer, ring size, branching).
  • Investigation of intermolecular recognition mechanisms, including hydrogen bonds and C-H/pi-interactions.
  • Thermodynamic analysis of glycan-protein binding, considering glycan conformation and presentation (e.g., multivalency).

Main Results:

  • Four key structural factors enhance the coding capacity of oligosaccharides.
  • Specific protein folds have evolved for selective glycan recognition.
  • Glycan conformation and presentation regulate lectin binding avidity.
  • Distinct glycan determinants serve as biomarkers, with co-regulation of lectins impacting cellular functions like growth.

Conclusions:

  • Orchestration of glycan and lectin expression is a significant mechanism for exploiting oligosaccharide coding potential.
  • This glycan-lectin interplay has broad physiological and medical relevance, particularly in disease contexts.
  • The study highlights the potential of targeting glycan-lectin interactions for therapeutic and diagnostic purposes.