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Glycobiology Advance Access published online on January 3, 2003
Glycobiology, doi:10.1093/glycob/cwg041
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Submitted on October 23, 2002
Revised on November 29, 2002
Accepted on December 12, 2002

© 2003 Oxford University Press

ORIGINAL ARTICLES

Altered glycosylation pattern allows the distinction between Prostate Specific Antigen (PSA) from normal and tumour origins

Rosa Peracaula 1, Glòria Tabarés 2, Louise Royle 3, David J. Harvey 3, Raymond A. Dwek 3, Pauline M. Rudd 3*, Rafael de Llorens 2*

1 Unitat de Bioquímica i Biologia Molecular, Departament de Biologia, Universitat de Girona, Campus de Montilivi s/n. 17071. Girona, Spain; Glycobiology Institute, Department of Biochemistry, Oxford University, Oxford OX1 3QU, United Kingdom
2 Unitat de Bioquímica i Biologia Molecular, Departament de Biologia, Universitat de Girona, Campus de Montilivi s/n. 17071. Girona, Spain
3 Glycobiology Institute, Department of Biochemistry, Oxford University, Oxford OX1 3QU, United Kingdom

* To whom correspondence should be addressed. E-mail: rafael.llorens{at}udg.es.

Abstract

Prostate Specific Antigen (PSA) is a glycoprotein secreted by prostate epithelial cells. PSA is currently used as a marker of prostate carcinoma, as high levels of PSA are indicative of a tumour situation. However, PSA tests still suffer from a lack of specificity to distinguish between benign prostate hyperplasia and prostate cancer. To determine whether PSA glycosylation could provide a means of differentiating between PSA from normal and tumour origins, N-glycan characterization of PSA from seminal fluid and prostate cancer cells (LNCaP cell line) by sequencing analysis and mass spectrometry was carried out. Glycans from normal PSA (that correspond to low and high pI PSA fractions) were sialylated biantennary complex structures, being half of them di-sialylated in the low pI PSA fraction and mostly mono-sialylated in the high pI PSA. PSA from LNCaP cells was purified to homogeneity and its glycan analysis showed a significant different pattern, especially in the outer ends of the biantennary complex structures. In contrast to normal PSA glycans, that were sialylated, LNCaP PSA oligosaccharides were all neutral and contained a higher fucose content. In 10-15% of the structures fucose was linked {alpha}1-2 to galactose, forming the H2 epitope, absent in normal PSA. GalNAc was increased in LNCaP glycans to 65% while in normal PSA it was only present in 25% of the structures. These carbohydrate differences allow a distinction to be made between PSA from normal and tumour origins and suggest a valuable biochemical tool for diagnosis and follow-up purposes.


Key words: N-glycosylation, LNCaP cells, prostate cancer, Prostate Specific Antigen (PSA), tumour marker
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