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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,...
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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.
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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,...
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In multicellular organisms, many molecules transmit signals between cells to pass information. These signals vary in complexity and include small peptides, nucleotides, steroids, fatty acid derivatives, and dissolved gases such as nitric oxide. Some signaling molecules diffuse through the plasma membrane to act locally between neighboring cells or travel long distances. Others remain attached to the cell surface, transmitting information to other cells only when they make contact. In some...
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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.
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Ganglioside Extraction, Purification and Profiling
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Gangliosides as Siglec ligands.

Ronald L Schnaar1

  • 1Department of Pharmacology and Molecular Sciences, Department of Neuroscience, Johns Hopkins University School of Medicine, 725 N Wolfe St, Baltimore, MD, 21205, USA. schnaar@jhu.edu.

Glycoconjugate Journal
|January 26, 2023
PubMed
Summary
This summary is machine-generated.

Sialic acid-binding immunoglobulin-like lectins (Siglecs) interact with gangliosides, influencing biological responses in the nervous and immune systems. These interactions are crucial for cell communication and immune regulation.

Keywords:
CD33MacrophagesMyelin-associated glycoproteinNatural killer cellsSialic acidSialoadhesin

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Area of Science:

  • Immunology
  • Neuroscience
  • Glycobiology

Background:

  • Sialoglycans bind to endogenous lectins, triggering biological responses.
  • The Siglec family comprises 15 human sialic acid-binding lectins, primarily on immune cells.
  • Gangliosides and sialoglycoproteins act as Siglec ligands, initiating signaling pathways.

Purpose of the Study:

  • To explore the diverse roles of Siglec-ganglioside interactions in biological systems.
  • To highlight the significance of these interactions in both the nervous and immune systems.
  • To elucidate the functional implications of Siglec-mediated signaling.

Main Methods:

  • Literature review of Siglec-ganglioside interactions.
  • Analysis of Siglec expression patterns and ligand specificities.
  • Examination of biological outcomes associated with these binding events.

Main Results:

  • Siglec-4 mediates axon-myelin stability via ganglioside binding (GD1a, GT1b).
  • Siglec-7 inhibits immune signaling through GD3 and GD2 binding, impacting cancer immune evasion.
  • Siglec-1 interacts with tumor and viral gangliosides, influencing antigen presentation and viral spread.

Conclusions:

  • Gangliosides are functional Siglec ligands with cell-specific distributions and varied roles.
  • Siglec-ganglioside interactions are critical for nervous system development and immune function.
  • Further research is needed to fully establish the biological significance of all Siglec-ganglioside interactions.