N-linked glycosylation supports cross-talk between receptor tyrosine kinases and androgen receptor

Harri M Itkonen1, Ian G Mills

  • 1Prostate Cancer Research Group, Centre for Molecular Medicine Norway, Nordic European Molecular Biology Laboratory (EMBL) Partnership, University of Oslo and Oslo University Hospital, Oslo, Norway.

Plos One
|June 1, 2013
PubMed

Insights

Prostate cancer cells show higher hexosamine biosynthesis pathway (HBP) activity. Inhibiting N-linked glycosylation disrupts androgen receptor (AR) signaling and IGF-1R activation, offering potential therapeutic strategies for prostate cancer.

Area of Science:

  • Molecular Oncology
  • Cancer Cell Biology
  • Biochemistry

Background:

  • Androgen receptor (AR) signaling drives prostate cancer, a leading cause of cancer death in men.
  • Androgen treatment influences oncogenes, including receptor tyrosine kinases (RTKs).
  • The hexosamine biosynthesis pathway (HBP) produces hexosamines crucial for protein glycosylation.

Purpose of the Study:

  • To investigate the role of the hexosamine biosynthesis pathway (HBP) in AR-positive prostate cancer.
  • To determine the impact of glycosylation inhibition on AR signaling and RTK activity.
  • To elucidate the relationship between androgen stimulation, N-linked glycosylation, and IGF-1R activation.

Main Methods:

  • Comparison of HBP enzyme levels in AR-positive versus AR-negative prostate cancer cell lines.
  • Inhibition of O-linked and N-linked glycosylation using ST045849 and tunicamycin, respectively.
  • Analysis of AR target gene expression (KLK3, CaMKK2), RTK phosphorylation status via antibody arrays, IGF-1R glycosylation and processing via lectin enrichment and immunoprecipitation, and receptor localization via confocal imaging.

Main Results:

  • AR-positive prostate cancer cells exhibit 50% higher HBP enzyme levels.
  • Inhibition of glycosylation decreased cell viability and androgen-induced AR target gene expression.
  • Androgen stimulation increased IGF-1R activity tenfold, accompanied by increased N-linked glycosylation and enhanced plasma-membrane localization; tunicamycin blocked these effects and caused pro-receptor accumulation.

Conclusions:

  • N-linked glycosylation of IGF-1R is essential for its full activation by androgen.
  • Disrupting IGF-1R glycosylation can interrupt the AR-IGF-1R feedback loop in prostate cancer cells.
  • Targeting protein glycosylation represents a potential therapeutic strategy for prostate cancer, though clinical application requires further research.

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