Role of glycosyltransferases in carcinogenesis; growth factor signaling and EMT/MET programs

Motoko Takahashi1, Yoshihiro Hasegawa2, Kento Maeda3

  • 1Department of Biochemistry, Sapporo Medical University School of Medicine, South-1 West-17, Chuo-ku, Hokkaido, 060-8556, Japan. takam@sapmed.ac.jp.

Glycoconjugate Journal
|January 28, 2022
PubMed

Insights

Glycosylation of cell surface receptors regulates signaling pathways. This review explores how N-glycan modification by glycosyltransferases impacts cell signaling, differentiation, and cancer progression.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Cell surface receptor glycosylation is crucial for signal transduction.
  • Glycosylation affects receptor trafficking, ligand binding, dimerization, phosphorylation, and endocytosis.

Purpose of the Study:

  • To review the role of glycosyltransferases in N-glycan modification.
  • To discuss the impact of N-glycan branching and elongation on cell surface receptor signaling.
  • To examine the involvement of these enzymes in epithelial-mesenchymal transition (EMT) and mesenchymal-epithelial transition (MET) programs, cancer development, and therapy resistance.

Main Methods:

  • Literature review focusing on glycosyltransferases and N-glycan modification.
  • Analysis of signaling pathways regulated by glycosylation.
  • Discussion of the role of glycosylation in cancer biology and therapeutic resistance.

Main Results:

  • N-glycan modifications by glycosyltransferases significantly influence cell surface receptor signaling.
  • Aberrant glycosylation patterns are linked to altered EMT/MET programs.
  • Glycosyltransferases play a role in cancer progression and the development of therapy resistance.

Conclusions:

  • Glycosyltransferases are key regulators of cell signaling through N-glycan modification.
  • Understanding these roles is critical for insights into differentiation, cancer development, and treatment strategies.

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