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Updated: Sep 16, 2025

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
Published on: January 20, 2022
Altered Glycosylation of PSA in Prostate Cancer Tissue
Hannu Koistinen1, Ruusu-Maaria Merivirta1,2,3, Timo-Pekka Lehto2,3,4
1Department of Clinical Chemistry and Haematology, University of Helsinki and Helsinki University Hospital, Helsinki, Finland.
Background:
The glycosylation of proteins is commonly altered in cancer. This offers novel opportunities for cancer biomarker development. As prostate-specific antigen (PSA) is a glycoprotein, identification of cancer-specific PSA-glycoforms is feasible. Such PSA-glycoforms may provide valuable diagnostic and prognostic information.
Methods:
PSA-glycoforms were studied in tissues, using in situ proximity-ligation assay (PLA)-based detection with a PSA-specific antibody and 25 different glycan-binding lectins.
Results:
Using 25 different lectins and a small tissue microarray (TMA), we showed that glycosylation of PSA in cancerous tissues is different from that in benign prostate. In a larger TMA with samples from 162 patients, PSA-glycoforms detected by succinylated wheat germ (WGAsucc) and Vicia villosa (VVA) lectins were enriched in cancerous tissues as compared to adjacent benign tissues from the same patients (p < 10-4 for both, Kruskal-Wallis H test), although strong total PSA staining was more often found in benign tissues (p = 6*10-14).
Conclusions:
We showed here that glycosylation of PSA is changed in situ in prostate cancer. The identified lectins, showing preferential binding to cancer-associated PSA-glycoforms, will aid the future development of a diagnostic serum test of prostate cancer. Such a test has potential to revolutionize prostate cancer diagnostics.
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