Related Experiment Video
Updated: Aug 28, 2025
11:21
Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
Published on: January 20, 2022
3.5K
Galectokines: The Promiscuous Relationship between Galectins and Cytokines
Lucía Sanjurjo1, Esmee C Broekhuizen2, Rory R Koenen3
1Health Research Institute of Santiago de Compostela (IDIS), Center for Research in Molecular Medicine and Chronic Diseases (CiMUS), Barcelona Ave., 15782 Santiago de Compostela, Spain.
Biomolecules
|September 23, 2022
Summary
Galectins (glycan-binding proteins) form novel complexes with cytokines, termed galectokines. These galectokines introduce new mechanisms for regulating immune homeostasis and the immune microenvironment.
Area of Science:
- Immunology
- Molecular Biology
- Glycobiology
Background:
- Galectins are glycan-binding proteins crucial for immune microenvironment regulation.
- Galectins influence immune cell activity and survival.
- Emerging evidence shows galectins interact with cytokines, modulating immune responses.
Purpose of the Study:
- To summarize current knowledge on galectokine formation and function.
- To explore mechanisms by which galectokines shape the immune microenvironment.
- To identify future research directions for galectokines in immunomodulation.
Main Methods:
- Review of existing literature on galectin-cytokine interactions.
- Analysis of proposed mechanisms for galectokine-mediated immune regulation.
- Discussion of current challenges and future research avenues.
Main Results:
- Galectins bind cytokines to form galectokine heterodimers.
- Galectokines represent a new layer of immune homeostasis regulation.
- These interactions offer novel pathways for shaping the immune microenvironment.
Conclusions:
- Galectokines are significant players in immunomodulation.
- Understanding galectokine function is key to advancing immune regulation research.
- Further investigation is needed to fully elucidate the role of galectokines.
Related Concept Videos
01:20The JAK-STAT Signaling Pathway
9.2K
Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as SH2...
9.2K
01:21Matrix Proteoglycans and Glycoproteins
4.0K
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...
4.0K
01:15Receptor Downregulation in MVBs
2.1K
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...
The EGFR can initiate signaling pathways that lead to cell proliferation, migration, and differentiation. Overexpression of EGFR stimulates cells to proliferate. Excessive EGFR...
2.1K
01:05Proteoglycans
4.0K
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,...
4.0K
01:25Selectins
3.4K
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,...
3.4K
01:31Immunoglobulin-like Cell Adhesion Molecules
3.4K
Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
3.4K