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Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay
Published on: December 19, 2018
N-linked glycosylation supports cross-talk between receptor tyrosine kinases and androgen receptor
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.
Abstract:
Prostate cancer is the second most common cause of cancer-associated deaths in men and signalling via a transcription factor called androgen receptor (AR) is an important driver of the disease. Androgen treatment is known to affect the expression and activity of other oncogenes including receptor tyrosine kinases (RTKs). In this study we report that AR-positive prostate cancer cell-lines express 50% higher levels of enzymes in the hexosamine biosynthesis pathway (HBP) than AR-negative prostate cell-lines. HBP produces hexosamines that are used by endoplasmic reticulum and golgi enzymes to glycosylate proteins targeted to plasma-membrane and secretion. Inhibition of O-linked glycosylation by ST045849 or N-linked glycosylation with tunicamycin decreased cell viability by 20%. In addition, tunicamycin inhibited the androgen-induced expression of AR target genes KLK3 and CaMKK2 by 50%. RTKs have been shown to enhance AR activity and we used an antibody array to identify changes in the phosphorylation status of RTKs in response to androgen stimulation. Hormone treatment increased the activity of Insulin like Growth Factor 1-Receptor (IGF-1R) ten-fold and this was associated with a concomitant increase in the N-linked glycosylation of the receptor, analyzed by lectin enrichment experiments. Glycosylation is known to be important for the processing and stability of RTKs. Inhibition of N-linked glycosylation resulted in accumulation of IGF-1R pro-receptor with altered mobility as shown by immunoprecipitation. Confocal imaging revealed that androgen induced plasma-membrane localization of IGF-1R was blocked by tunicamycin. In conclusion we have established that the glycosylation of IGF-1R is necessary for the full activation of the receptor in response to androgen treatment and that perturbing this process can break the feedback loop between AR and IGF-1R activation in prostate cells. Achieving similar results selectively in a clinical setting will be an important challenge in the future.
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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