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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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The mammalian target of rapamycin or mTOR protein was discovered in 1994 due to its direct interaction with rapamycin. The protein gets its name from a yeast homolog called TOR. The mTOR protein complex in mammalian cells plays a major role in balancing anabolic processes such as the synthesis of proteins, lipids, and nucleotides and catabolic processes, such as autophagy in response to environmental cues, such as availability of nutrients and growth factors.
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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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Tumor progression is a phenomenon where the pre-formed tumor acquires successive mutations to become clinically more aggressive and malignant. In the 1950s, Foulds first described the stepwise progression of cancer cells through successive stages.
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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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Related Experiment Video

Updated: Jan 16, 2026

Glycan Node Analysis: A Bottom-up Approach to Glycomics
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IgG galactosylation changes in cancer.

Yumeng Liu1, Xiequn Xu1, Zejian Zhang2

  • 1Department of General Surgery, Peking Union Medical College Hospital, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, 100730, People's Republic of China.

Carbohydrate Research
|September 30, 2025
PubMed
Summary

Changes in IgG galactosylation, a key glycan structure, show promise for early cancer detection. Monitoring these alterations in blood may improve cancer diagnosis, staging, and prognosis, aiding timely treatment.

Keywords:
CancerCancer biomarkersGalactosylationIgGN-Glycosylation

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Area of Science:

  • Biochemistry
  • Oncology
  • Glycobiology

Background:

  • Cancer incidence and mortality are rising globally, necessitating improved diagnostic tools.
  • Glycosylation, particularly galactose structures on IgG, is implicated in cancer progression.
  • The role of IgG galactosylation in clinical cancer detection remains debated.

Purpose of the Study:

  • To review current evidence on alterations in serum and plasma IgG galactosylation in cancer patients.
  • To discuss potential mechanisms behind these glycosylation changes.
  • To highlight the future utility of IgG galactosylation in cancer detection, diagnosis, and prognosis.

Main Methods:

  • Literature review of studies examining IgG galactosylation in cancer.
  • Analysis of evidence linking IgG galactosylation patterns to cancer occurrence and progression.
  • Synthesis of findings regarding diagnostic and prognostic potential.

Main Results:

  • Increased agalactosylated IgG is frequently associated with cancer development and advancement.
  • Serum and plasma IgG galactosylation patterns are altered in cancer patients.
  • IgG galactosylation shows potential for distinguishing benign from malignant tumors and cancer staging.

Conclusions:

  • IgG galactosylation alterations are a promising biomarker for cancer detection and diagnosis.
  • This glycan marker could complement existing cancer markers for more precise patient management.
  • Monitoring IgG galactosylation may enhance timely cancer diagnosis, staging, and treatment monitoring.