Glycosylation of urinary prostate-specific antigen in benign hyperplasia and cancer: assessment by lectin-binding patterns

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 it oligosaccharide chain as a potential biomarker of these pathophysiological conditions. Design and methods: First morning urine voide 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 applutinin, 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. (C) 2004 The Canadian Society of Clinical Chemists. All rights reserved.