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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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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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The complement system is a group of approximately 20 plasma proteins that strengthen the body's defenses against infections through opsonization, inflammation, and cell lysis. Opsonization involves coating pathogens with complement proteins, making them more recognizable and facilitating phagocyte engulfment. Certain complement proteins induce inflammation that attracts immune cells to the site of infection. Cell lysis involves the destruction of pathogens through the formation of a...
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Related Experiment Video

Updated: Jul 12, 2025

Preparation of CD4+ T Cells for Analysis of GD3 and GD2 Ganglioside Membrane Expression by Microscopy
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The monosialoganglioside GM1a protects against complement attack.

Henri Wedekind1, Julia Beimdiek1, Charlotte Rossdam1

  • 1Institute of Clinical Biochemistry, Hannover Medical School, Hannover, Germany.

Cell Death Discovery
|October 25, 2023
PubMed
Summary
This summary is machine-generated.

Sialylation loss on cells triggers complement attack. Adding monosialoganglioside GM1a protects cells by enhancing complement factor H binding, offering a new therapeutic approach for complement-mediated diseases.

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Ganglioside Extraction, Purification and Profiling
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Area of Science:

  • Immunology
  • Glycobiology
  • Cell Biology

Background:

  • The complement system, crucial for innate immunity, requires strict host cell surface regulation to prevent self-damage.
  • Loss of cell surface sialylation in placental cells in mice caused maternal complement attack and pregnancy loss.
  • Trophoblast stem cells (TSCs) lacking sialylation exhibit complement sensitivity and cell death in vitro.

Purpose of the Study:

  • To investigate the role of sialylation in regulating complement activation.
  • To identify specific sialylated molecules involved in complement control.
  • To explore the therapeutic potential of exogenous sialylated molecules in preventing complement-mediated cell damage.

Main Methods:

  • Generation of sialylation-deficient trophoblast stem cells (TSCs).
  • Glycolipid analysis using multiplexed capillary gel electrophoresis coupled to laser-induced fluorescence detection (xCGE-LIF).
  • Assessment of complement sensitivity and cell death in vitro and in vivo models.

Main Results:

  • Monosialoganglioside GM1a was identified as a key regulator of complement on the cell surface.
  • Exogenously administered GM1a integrated into trophoblast membranes, increased complement factor H (FH) binding, and protected cells from complement attack.
  • GM1a treatment rescued human endothelial cells and erythrocytes from complement-mediated damage and reduced hemolysis in Paroxysmal nocturnal hemoglobinuria (PNH) erythrocytes.

Conclusions:

  • Cell surface sialylation, specifically via GM1a, is critical for regulating complement activation.
  • Exogenous administration of GM1a demonstrates significant complement regulatory potential.
  • Gangliosides represent a promising new class of sialoglycotherapeutics for targeted complement inhibition.