ZBiotech’s lectin array system enables researchers to identify distinct glycosylation patterns associated with GALNT7 overexpression in prostate cancer.

Aberrant glycosylation is a hallmark of cancer, contributing significantly to tumor growth, metastasis, and immune evasion. One primary driver of this aberrant glycosylation is the dysregulated expression of glycosylation enzymes in cancer cells. Despite its importance, the expression of these enzymes in prostate cancer, the most prevalent cancer among men, remains underexplored. A recent groundbreaking study addresses this knowledge gap by demonstrating that the upregulation of GALNT7 in prostate cancer alters O-glycosylation and promotes tumor growth. This pivotal investigation was led by a team of distinguished glycobiology researchers, including Nobel Prize laureate Carolyn R. Bertozzi from Stanford University, USA, and Jennifer Munkley from the Newcastle University Institute of Biosciences, UK.

In this study, the researchers identified that GALNT7 upregulation is characteristic of prostate cancer and is observed in urine and blood samples from affected men. Intriguingly, they also discovered that GALNT7 levels remain elevated in castrate-resistant prostate cancer, suggesting that GALNT7 could serve as a biomarker for those at risk of relapse. On a mechanistic level, the study demonstrated that GALNT7 modifies O-glycosylation in prostate cancer cells, and aberrant O-glycosylation may promote tumor growth while correlating with cell cycle and immune signaling pathways.

To elucidate the types of glycan expression driven by GALNT7, the researchers overexpressed the enzyme in PC3 cells and screened them using ZBiotech’s lectin array system, comprising 37 plant-derived lectins with validated binding specificities. The initial screening pinpointed SBA lectin, which recognizes terminal GalNAc or Tn antigen, as one of the lectins exhibiting strong binding to PC3 cells. This finding was corroborated through lectin flow cytometry analysis, demonstrating that PC3 cells with upregulated GALNT7 display increased binding to SBA lectin. The live-cell-based lectin array analysis allowed the researchers to identify O-glycosylation as a potential target of GALNT7 in prostate cancer cells, establishing a foundation for future mechanistic investigations of aberrant O-glycosylation in this disease.

ZBiotech’s advanced lectin array platform, in conjunction with its comprehensive analysis services, offers a robust tool for characterizing glycosylation profiles in a wide range of biological samples, such as proteins, antibodies, cells, cell lysates, serum, vesicles, bacteria, and viral particles. This all-encompassing service facilitates target identification and validation, thereby enabling researchers to expedite their innovative glycobiology findings while maintaining the rigor and precision required for scientific publications.