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Related Concept Videos

Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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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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Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
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Sperm Structure and Semen Composition01:22

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During ejaculation, males release around 2-5 milliliters of semen, which is a complex mixture of mature sperm and various fluids produced by accessory glands. The mature sperm cells measure approximately 60 micrometers in length and consist of a head, neck, midpiece, and tail. The head is flattened and tapered, measuring about 4 to 5 micrometers in length. It contains a nucleus with condensed chromosomes and an acrosome, a cap-like structure filled with enzymes essential for penetrating the...
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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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Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
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Site-specific N-glycan changes during semen liquefaction.

Cheng Li1, Wei Dan1, Pengfei Li1

  • 1College of Life Sciences, Northwest University, Xi'an, Shaanxi Province, 710069, PR China.

Analytical Biochemistry
|September 11, 2023
PubMed
Summary

Semen liquefaction, crucial for fertilization, involves significant changes in glycosylation. This study identified 25 altered glycopeptides, with sialylated glycans playing a key role in the process.

Keywords:
GlycoproteomeLiquefactionMass spectrometryN-Glycan structuresSemen

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Area of Science:

  • Reproductive biology
  • Glycobiology
  • Proteomics

Background:

  • Normal semen liquefaction is essential for fertilization.
  • Glycosylation is implicated in fertilization, but its role in semen liquefaction is unknown.

Purpose of the Study:

  • To investigate changes in glycosylation during human semen liquefaction.
  • To identify specific glycoproteins and glycopeptides altered during this process.

Main Methods:

  • Glycoproteomic analysis of human semen at 0 min and 30 min liquefaction.
  • Utilized StrucGP software and Tandem Mass Tags (TMT) for quantification.

Main Results:

  • Identified 25 intact glycopeptides (IGPs) from 10 glycoproteins with significant changes.
  • 23 glycopeptides were up-regulated, and 2 were down-regulated.
  • Half of the up-regulated glycopeptides were modified with sialylated glycans.

Conclusions:

  • Glycosylation undergoes significant changes during semen liquefaction.
  • Sialylated glycans appear to play a critical role in semen liquefaction.
  • This study provides a valuable resource for understanding glycosylation's role in male fertility.