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Oligosaccharide Assembly01:24

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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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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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Related Experiment Video

Updated: Jul 12, 2025

Isolation of Human Endometrial Stromal Cells for In Vitro Decidualization
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Elevated high-mannose N-glycans hamper endometrial decidualization.

Siyi Chen1, Aihui Zhang1, Na Li1

  • 1Liaoning Provincial Core Lab of Glycobiology and Glycoengineering, College of Basic Medical Science, Department of Biochemistry and Molecular Biology, Dalian Medical University, Dalian 116044, China.

Iscience
|November 2, 2023
PubMed
Summary

Dysfunctional endometrial decidualization in miscarriage is linked to altered high-mannose glycans and decreased MAN1A1 enzyme levels. Increased lncNEAT1 further inhibits MAN1A1, impacting embryo implantation.

Keywords:
BiochemistryMolecular biologyPhysiology

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Area of Science:

  • Reproductive biology
  • Glycobiology
  • Molecular genetics

Background:

  • Decidualization is crucial for embryo implantation and pregnancy success.
  • Dysfunctional decidualization is linked to pregnancy failure.
  • Protein glycosylation, particularly high-mannose structures, plays a role in cellular function.

Purpose of the Study:

  • Investigate the role of high-mannose glycans and MAN1A1 in endometrial decidualization.
  • Explore the association between lncNEAT1, MAN1A1, and miscarriage.
  • Elucidate the molecular mechanism linking lncNEAT1 to impaired decidualization.

Main Methods:

  • Lectin microarray analysis of decidual tissues.
  • Quantification of MAN1A1 enzyme levels.
  • Screening and expression analysis of long non-coding RNAs (lncRNAs), specifically lncNEAT1.

Main Results:

  • Elevated high-mannose epitopes in decidual tissues of miscarriage patients.
  • Decreased levels of mannosyl-oligosaccharide α-1,2 mannosidase IA (MAN1A1) in miscarriage patients.
  • Increased lncNEAT1 expression in miscarriage patients, negatively correlating with MAN1A1.
  • lncNEAT1 inhibits MAN1A1 expression via the NPM1-SP1 complex, impairing decidualization.

Conclusions:

  • High-mannose glycan alterations and reduced MAN1A1 are associated with miscarriage.
  • lncNEAT1 exacerbates miscarriage by inhibiting MAN1A1 and hindering endometrial decidualization.
  • Findings provide new insights into glycan modifications in early pregnancy failure.