Glycosylation is a global target for androgen control in prostate cancer cells

Jennifer Munkley1

  • 1Institute of Genetic MedicineNewcastle University, Newcastle-upon-Tyne, UK jennifer.munkley@ncl.ac.uk.

Endocrine-Related Cancer
|February 5, 2017
PubMed

Insights

Androgen receptor (AR) controls key glycosylation enzymes in prostate cancer, altering cancer-associated glycans. These changes impact cancer hallmarks, offering potential biomarkers and therapeutic targets for improved patient outcomes.

Area of Science:

  • Oncology
  • Glycobiology
  • Molecular Biology

Background:

  • Glycan composition changes are hallmarks of cancer, influencing critical biological processes.
  • Prostate cancer exhibits altered glycosylation patterns, presenting opportunities for targeted therapies.

Purpose of the Study:

  • To investigate the role of androgen receptor (AR) in regulating glycosylation in prostate cancer.
  • To identify specific glycosylation enzymes and their associated glycans implicated in prostate cancer progression.

Main Methods:

  • Analysis of glycosylation enzyme expression in prostate cancer tissue.
  • Identification of AR-controlled glycosylation pathways and associated glycans.

Main Results:

  • Eight specific glycosylation enzymes (GALNT7, ST6GalNAc1, GCNT1, UAP1, PGM3, CSGALNACT1, ST6Gal1, EDEM3) are upregulated and AR-controlled in prostate cancer.
  • These enzymes are linked to the synthesis of cancer-associated glycans like sialyl-Tn (sTn), sialyl LewisX (SLeX), O-GlcNAc, and chondroitin sulfate.
  • Androgen-mediated glycosylation alterations potentially modify cell adhesion, migration, immune surveillance, and metabolism in prostate cancer.

Conclusions:

  • Androgen control of glycosylation represents a significant mechanism in prostate cancer.
  • Targeting these AR-regulated glycosylation pathways may offer novel therapeutic strategies and biomarkers for prostate cancer risk stratification and treatment.

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