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Glycobiology Advance Access published online on September 21, 2005
Glycobiology, doi:10.1093/glycob/cwj042
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© The Author 2005. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org
Received July 27, 2005
Revised September 14, 2005
Accepted September 16, 2005

Article

Different glycan structures in prostate-specific antigen (PSA) from prostate cancer sera in relation to seminal plasma PSA

Glòria Tabarés 1, Catherine M. Radcliffe 2, Sílvia Barrabés 3, Manel Ramírez 4, R. Núria Aleixandre 4, Wolfgang Hoesel 5, Raymond A. Dwek 2, Pauline M. Rudd 2*, Rosa Peracaula 3, and Rafael de Llorens 3

1 Unitat de Bioquímica i Biologia Molecular, Departament de Biologia, Universitat de Girona, Campus de Montilivi s/n. 17071, Girona, Spain; Laboratori ICS Girona, Hospital Universitari Dr. Josep Trueta, Avinguda de França s/n. 17007, Girona, Spain
2 Glycobiology Institute, Department of Biochemistry, Oxford University, Oxford OX1 3QU, United Kingdom
3 Unitat de Bioquímica i Biologia Molecular, Departament de Biologia, Universitat de Girona, Campus de Montilivi s/n. 17071, Girona, Spain
4 Laboratori ICS Girona, Hospital Universitari Dr. Josep Trueta, Avinguda de França s/n. 17007, Girona, Spain
5 Roche Diagnostics GmbH, Nonnenwaldstrasse 2, 82372 Penzberg, Germany

* To whom correspondence should be addressed.
Pauline M. Rudd, E-mail: pauline.rudd{at}bioch.ox.ac.uk


  Abstract

Prostate-specific antigen (PSA), the tumour marker currently used for prostate cancer (PCa), is not specific enough to distinguish between PCa and benign prostate hyperplasia (BPH). Glycosylation of PSA from seminal plasma (normal) differs from that of PSA secreted by the tumour prostate cell line LNCaP. We report the detailed glycan analysis of PSA from sera of PCa patients to determine whether glycosylation differences compared to normal PSA could be employed for diagnostic purposes. Sequencing of the glycans of whole serum from a PCa patient was also carried out.PSA glycans from PCa patients’ sera, seminal plasma and secreted by LNCaP cells were further compared using lectin detection, GISA (Glycosylation immunosorbent assay) and two-dimensional electrophoresis (2-DE).By glycan sequencing, the fucose content of PSA from a PCa patient serum was lower than that from seminal plasma and sialic acid, which was found in PSA from both samples, presented a lower ratio {alpha}2,3/ {alpha}2,6 in PSA from serum PCa. Using lectin analysis and GISA some of these glycan differences were detected. 2-DE showed less sialylated PSA glycans from PCa patients’ sera than in normal PSA. Differences have also been found in the whole serum glycosylation between the PCa patient and the control.Glycosylation differences between normal PSA and from PCa patients’ sera were detected using the reported methodologies. Further studies on the PSA glycosylation of more PCa and BPH sera will be required in order to determine the utility of these glycan differences to specifically discriminate between benign and malignant prostate states.

Keywords: Lectins/N-Glycosylation/Prostate Cancer/Prostate-specific antigen (PSA)/Two-dimensional electrophoresis.
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