Evaluation of the pattern of human serum glycoproteins in prostate cancer

Abstract

Glycoprotein profiling at the level of cells, tissues and biological fluids is aimed at discovering new cancer biomarkers and also at finding specific cancer-related structural alterations of known tumor markers. In this study we comparatively evaluated the glycoprotein patterns of human prostate cancer (PCa)- and normal human sera regarding sialylation and fucosylation as structural characteristics relevant for cancer progression. Glycoproteins were isolated using affinity chromatography on Sambucus nigra agglutinin- and Lens culinaris agglutinin-columns and subsequently characterized by SDS-PAGE and on-chip normal phase-surface capture combined with surface-enhanced laser/desorption ionization time of flight mass spectrometry. Comparative analysis of the glycoproteins purified from healthy and PCa sera indicated differences and redundancy of the isolated molecules in terms of the microheterogeneity of counterpart glycans, the relative abundance and the presence/absence of particular molecular species. In PCa there was a general increase in sialylation and decrease in fucosylation of human serum glycans compared to normal sera. Taken together, the results obtained indicated that an affinity-approach based on the use of lectins of narrow specificity reduced the complexity of the examined samples and at this discovery-phase of our study pointed to specific glyco-changes that may be relevant for improving the monitoring of PCa progression.