Fig. 4: GALNT7 can modify O-glycosylation in prostate cancer cells.
From: Upregulation of GALNT7 in prostate cancer modifies O-glycosylation and promotes tumour growth
A Lectin flow cytometry shows PC3 cells with upregulated GALNT7 have increased binding to SBA lectin (which recognises terminal GalNAc or Tn antigen). B Detection of the cancer-associated Tn antigen by immunofluorescence in DU145 cells show upregulation of GALNT7 promotes increased expression of the Tn antigen. C Analysis of extracellular vesicles (EVs) in conditioned media from LNCaP and DU145 cells with knockdown or overexpression of GALNT7 suggests a correlation between GALNT7 and the Tn antigen in the prostate cancer secretome. D Detection of glycosylation of secreted proteins in samples from PC3 control cells or GALNT7-KO cells using GALNT7 bump-and-hole engineering. The active site of GALNT7 was engineered by mutation (IIe and Leu to 2xAla). The mutant (termed BH) uses a chemically modified analogue of the native substrate UDP-GalNAc. Following glycosylation, the chemical modification can be traced by methods of click chemistry.
