Aberrant Glycosylation in Cancer: A Novel Molecular Mechanism Controlling Metastasis

Ana Magalhães1, Henrique O Duarte2, Celso A Reis3

  • 1Institute for Research and Innovation in Health (i3S), University of Porto, 4200-135 Porto, Portugal; Institute of Molecular Pathology and Immunology of the University of Porto (IPATIMUP), 4200-135 Porto, Portugal.

Cancer Cell
|June 14, 2017
PubMed

Insights

Altered glycosylation is key in cancer. Researchers found the enzyme FUT8 drives melanoma metastasis, suggesting core fucosylation as a new therapeutic target for cancer treatment.

Area of Science:

  • Biochemistry
  • Oncology
  • Molecular Biology

Background:

  • Glycosylation is a crucial post-translational modification involved in various cellular processes.
  • Aberrant glycosylation patterns are hallmarks of cancer, influencing tumor progression and metastasis.

Purpose of the Study:

  • To investigate the role of specific glycosyltransferases in melanoma metastasis.
  • To identify novel therapeutic targets for preventing and treating metastatic melanoma.

Main Methods:

  • Utilized genetic and pharmacological approaches to modulate FUT8 activity in melanoma models.
  • Analyzed changes in cell surface glycosylation and metastatic potential.

Main Results:

  • Identified the glycosyltransferase FUT8 as a key mediator of melanoma cell invasion and metastasis.
  • Demonstrated that FUT8-dependent core fucosylation promotes tumor spread.

Conclusions:

  • FUT8-mediated core fucosylation is a critical driver of melanoma metastasis.
  • Targeting FUT8 or core fucosylation pathways presents a promising therapeutic strategy for metastatic melanoma.

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