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Related Concept Videos

Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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

Matrix Proteoglycans and Glycoproteins

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...
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...
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

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...
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.
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Updated: Jun 11, 2026

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
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Published on: January 20, 2022

Galectins: a key intersection between glycobiology and immunology.

G A Rabinovich1, C M Riera, C A Landa

  • 1Departamento de Bioquímica Clínica, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Argentina. gabyrabi@onenet.com.ar

Brazilian Journal of Medical and Biological Research = Revista Brasileira De Pesquisas Medicas E Biologicas
|May 29, 1999
PubMed
Summary

Galectins are evolutionarily conserved proteins involved in cell adhesion, growth, and immunity. Understanding their roles in disease offers potential for novel therapeutic strategies targeting carbohydrate recognition.

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Area of Science:

  • Immunology
  • Glycobiology
  • Biomedical Research

Background:

  • Galectins are conserved animal lectins found across diverse species.
  • They possess conserved carbohydrate recognition domains specific for polylactosamine glycoconjugates.
  • Galectins play roles in cell adhesion, growth regulation, inflammation, immunomodulation, apoptosis, and metastasis.

Purpose of the Study:

  • To review recent advances in galectin research.
  • To highlight the significance of galectins in immunological processes.
  • To discuss the implications of galectins in biomedical research, disease diagnosis, and clinical intervention.

Main Methods:

  • Literature review of experimental data on galectin functions.
  • Analysis of galectin involvement in various biological processes.
  • Exploration of therapeutic strategies based on galectin-carbohydrate interactions.

Main Results:

  • Accumulated experimental data demonstrate galectin participation in key biological processes.
  • Galectins are significant in immunological processes, impacting disease mechanisms.
  • Galectin research provides insights for disease diagnosis and therapeutic interventions.

Conclusions:

  • Galectins are crucial in diverse biological functions, particularly immunity.
  • Targeting galectin-carbohydrate recognition offers potential for treating autoimmune disorders, inflammation, allergies, and cancer.
  • Further research into galectins can lead to novel therapeutic strategies and improved clinical outcomes.