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Related Concept Videos

Integrins01:10

Integrins

Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
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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,...
Selectins01:25

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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...
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
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Assembly of Signaling Complexes01:30

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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
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Related Experiment Video

Updated: May 26, 2026

Complementation of Splicing Activity by a Galectin-3 - U1 snRNP Complex on Beads
08:48

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Published on: December 9, 2020

Integrating structure and function of 'tandem-repeat' galectins.

Maria F Troncoso1, Maria T Elola, Diego O Croci

  • 1Institute of Biological Chemistry and Physicochemistry (UBA-CONICET), Department of Biological Chemistry, School of Pharmacy and Biochemistry, University of Buenos Aires, Buenos Aires, Argentina.

Frontiers in Bioscience (Scholar Edition)
|December 29, 2011
PubMed
Summary

Tandem-repeat galectins (GAL-4, -6, -8, -9, -12) are emerging as key players in inflammatory and neoplastic diseases. Their roles in conditions like inflammatory bowel disease, autoimmune disorders, and cancer progression are increasingly understood.

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Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures

Published on: June 26, 2020

Area of Science:

  • Biochemistry
  • Immunology
  • Molecular Biology

Background:

  • Galectins (GALs) are conserved lectins with carbohydrate recognition domains (CRDs).
  • While GAL-1 and GAL-3 functions are well-studied, 'tandem-repeat' galectins (GAL-4, -6, -8, -9, -12) roles are emerging.
  • These galectins possess two distinct CRDs linked by a peptide.

Purpose of the Study:

  • To review and synthesize current knowledge on 'tandem-repeat' galectins.
  • To explore their structures, ligands, and involvement in disease.
  • To highlight their potential in inflammatory and neoplastic diseases.

Main Methods:

  • Literature review and data integration.
  • Analysis of structural features and ligand interactions.
  • Correlation of galectin functions with disease pathologies.

Main Results:

  • GAL-4 is linked to inflammatory bowel diseases as a pro-inflammatory or pro-apoptotic factor.
  • GAL-8 influences autoimmune diseases (rheumatoid arthritis, lupus) and cancer progression.
  • GAL-9 regulates allergic inflammation, autoimmunity, and has prognostic value in tumors.
  • GAL-12 is crucial for adipocyte physiology.

Conclusions:

  • 'Tandem-repeat' galectins exhibit diverse roles in inflammation, autoimmunity, and cancer.
  • Further research is essential to fully elucidate their functions in health and disease.
  • These galectins represent potential therapeutic targets and biomarkers.