Related Experiment Video

Updated: Oct 9, 2025

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

3.6K

Chemokines modulate glycan binding and the immunoregulatory activity of galectins

Lucía Sanjurjo1, Iris A Schulkens1, Pauline Touarin2

  • 1Amsterdam UMC location VUmc, Department of Medical Oncology, Cancer Center Amsterdam, Amsterdam, The Netherlands.

Communications Biology
|December 21, 2021
PubMed

Insights

Chemokines, such as CXCL4, can modulate the immune functions of galectins by altering their glycan-binding properties. This interaction specifically impacts T cell apoptosis, revealing a novel immunomodulatory pathway.

Area of Science:

  • Immunology
  • Molecular Biology
  • Biochemistry

Background:

  • Galectins are key regulators of immune responses through glycan binding.
  • Cytokines and chemokines are known to be modulated by galectins.
  • The precise mechanisms of galectin-chemokine interactions in immunity require further elucidation.

Purpose of the Study:

  • To investigate the inverse mechanism where chemokines control galectin immunomodulatory functions.
  • To identify specific galectin-chemokine binding pairs and their functional consequences.
  • To elucidate how chemokine binding affects galectin glycan-binding activity and specificity.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy to analyze protein-protein interactions.
  • Assessment of galectin glycan-binding affinity and specificity.
  • Functional assays measuring T cell apoptosis induced by galectin-chemokine complexes.

Main Results:

  • Specific galectin-chemokine binding pairs were identified, including galectin-1/CXCL4 and galectin-9/CCL5.
  • CXCL4 binding induced structural changes in galectin-1's carbohydrate-binding site, altering its glycan-binding properties.
  • Galectin-1/CXCL4 enhanced apoptosis in CD8+ T cells, while galectin-9/CCL5 reduced apoptosis in CD4+ T cells.

Conclusions:

  • Chemokines can directly control the immunomodulatory functions of galectins through specific binding.
  • Galectin-chemokine interactions represent a novel mechanism for regulating immune cell responses, particularly T cell apoptosis.
  • These findings offer new insights into the complex interplay between galectins and chemokines in immune regulation.

More Related Videos

Author Spotlight: Dendritic Cells Maturation Using Sialidases-Based Enzymatic Treatment of the Cell Surface13:36

Author Spotlight: Dendritic Cells Maturation Using Sialidases-Based Enzymatic Treatment of the Cell Surface

Published on: October 20, 2023

3.7K
Glycan Node Analysis: A Bottom-up Approach to Glycomics11:36

Glycan Node Analysis: A Bottom-up Approach to Glycomics

Published on: May 22, 2016

10.7K

Related Concept Videos

Proteoglycans01:05

Proteoglycans

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,...
4.1K
Glycocalyx and its Functions01:14

Glycocalyx and its Functions

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.
6.4K
Protein Glycosylation01:25

Protein Glycosylation

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...
7.6K
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,...
3.5K
Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR...
2.2K
GPCRs Regulate Adenylyl Cylase Activity01:09

GPCRs Regulate Adenylyl Cylase Activity

Some GPCRs transmit signals through adenylyl cyclase (AC), a transmembrane enzyme. AC helps synthesize second messenger cyclic adenosine monophosphate (cAMP). AC catalyzes cyclization reaction and converts ATP to cAMP by releasing a pyrophosphate. The pyrophosphate is further hydrolyzed to phosphate by the enzyme pyrophosphatase, which drives cAMP synthesis to completion. However, cAMP is rapidly degraded to 5′ AMP by the enzymes phosphodiesterase (PDE), preventing overstimulation of...
6.1K