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Glycan Characterization of PSA 2-DE Subforms from Serum and Seminal Plasma

Prostate-specific antigen (PSA) two-dimensional electrophoresis (2-DE) subforms (F1–F5) have been described to be altered in prostate cancer (PCa) compared to benign prostatic hyperplasia (BPH). To understand their molecular differences, characterization of these subforms from PCa serum and seminal plasma, namely, at the glycan level, was performed. PSA 2-DE subforms from two serum PCa samples and seminal plasma were analyzed by N-glycan sequencing using high-performance liquid chromatography (HPLC) combined with exoglycosidase array digestions and by mass spectrometry. F1, F2, and F3 subforms showed the same N-glycan pattern, which contained higher levels of sialic acid than the F4 subform, whereas the F5 subform was unglycosylated. When comparing PSA subforms from PCa with seminal plasma, a decrease in sialylation was observed. Furthermore, the analysis of F3, the more abundant PSA subform, showed a higher proportion of alpha 2–3 sialic acid and a decrease in core fucosylated glycans in the PCa sample. These N-glycan changes in PCa PSA subforms highlight the importance of glycosylation as an indicator of PCa disease

© OMICS A Journal of Integrative Biology, 2010, vol. 14, núm. 4, p. 465-474

Mary Ann Liebert, Inc

Autor: Sarrats Carbó, Ariadna
Saldova, Radka
Comet i Batlle, Josep
O’Donoghue, Niaobh
Llorens Duran, Rafael de
Rudd, Pauline M.
Peracaula Miró, Rosa
Data: 2010
Resum: Prostate-specific antigen (PSA) two-dimensional electrophoresis (2-DE) subforms (F1–F5) have been described to be altered in prostate cancer (PCa) compared to benign prostatic hyperplasia (BPH). To understand their molecular differences, characterization of these subforms from PCa serum and seminal plasma, namely, at the glycan level, was performed. PSA 2-DE subforms from two serum PCa samples and seminal plasma were analyzed by N-glycan sequencing using high-performance liquid chromatography (HPLC) combined with exoglycosidase array digestions and by mass spectrometry. F1, F2, and F3 subforms showed the same N-glycan pattern, which contained higher levels of sialic acid than the F4 subform, whereas the F5 subform was unglycosylated. When comparing PSA subforms from PCa with seminal plasma, a decrease in sialylation was observed. Furthermore, the analysis of F3, the more abundant PSA subform, showed a higher proportion of alpha 2–3 sialic acid and a decrease in core fucosylated glycans in the PCa sample. These N-glycan changes in PCa PSA subforms highlight the importance of glycosylation as an indicator of PCa disease
Format: application/pdf
ISSN: 1536-2310 (versió paper)
1557-8100 (versió electrònica)
Accés al document: http://hdl.handle.net/10256/7483
Llenguatge: eng
Editor: Mary Ann Liebert, Inc
Col·lecció: Reproducció digital del document publicat a: http://dx.doi.org/10.1089/omi.2010.0050
Articles publicats (D-B)
És part de: © OMICS A Journal of Integrative Biology, 2010, vol. 14, núm. 4, p. 465-474
Drets: Tots els drets reservats. This is a copy of an article published in the OMICS A Journal of Integrative Biology © 2010 Mary Ann Liebert, Inc.; OMICS A Journal of Integrative Biology is available online at: http://www.liebertonline.com.
Matèria: Pàncrees -- Càncer -- Investigació
Pancreas -- Cancer -- Research
Glicoproteïnes
Glycoproteins
Antígen prostàtic específic
Prostate-specific antigen
Títol: Glycan Characterization of PSA 2-DE Subforms from Serum and Seminal Plasma
Tipus: info:eu-repo/semantics/article
Repositori: DUGiDocs

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