Related Experiment Video
Updated: Aug 20, 2026
Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
Published on: January 20, 2022
Glycosylation of urinary prostate-specific antigen in benign hyperplasia and cancer: assessment by lectin-binding
Miroslava M Janković1, Maja M Kosanović
1Institute for the Application of Nuclear Energy--INEP, Belgrade, Serbia and Montenegro. miraj@inep.co.yu
Objectives:
In the present study, we examined the glycosylation of urinary prostate-specific antigen (PSA) from benign prostatic hyperplasia (BPH) and prostate cancer (PCa) subjects, specifically looking at alterations in its oligosaccharide chain as a potential biomarker of these pathophysiological conditions.
Design And Methods:
First morning urine voids were collected from subjects with PCa and BPH before initiation of any treatment. Urinary PSA was characterized by ion-exchange chromatography, followed by lectin affinity chromatography on the columns using immobilized plant lectins.
Results:
Four isoforms of urinary PSA from both BPH and PCa samples were separated by ion-exchange chromatography. The elution profiles from lectin-affinity columns reflected molecular heterogeneity of PSA isoforms and the main differences observed were in the reactivity to Ulex europaeus agglutinin, Aleuria aurantia agglutinin, Phaseolus vulgaris erythroagglutinin and Phaseolus vulgaris leukoagglutinin.
Conclusions:
The observed differences in the lectin reactivities between BPH PSA and PCa PSA may be of clinical importance in the evaluation of prostate health.
