Glycan characterization of PSA 2-DE subforms from serum and seminal plasma

Autor: Niaobh O'Donoghue, Pauline M. Rudd, Rafael de Llorens, Ariadna Sarrats, Josep Comet, Rosa Peracaula, Radka Saldova
Rok vydání: 2010
Předmět:
Male
Glycan
Glycosylation
Molecular Sequence Data
Antígen prostàtic específic
urologic and male genital diseases
Biochemistry
Pàncrees -- Càncer -- Investigació
chemistry.chemical_compound
Prostate cancer
Antigen
Exoglycosidase
Polysaccharides
Semen
Genetics
medicine
Biomarkers
Tumor
Carbohydrate Conformation
Animals
Humans
Protein Isoforms
Electrophoresis
Gel
Two-Dimensional
Amino Acid Sequence
Molecular Biology
Pancreas -- Cancer -- Research
Chromatography
High Pressure Liquid
Glycoproteins
chemistry.chemical_classification
biology
Prostatic Neoplasms
Prostate-Specific Antigen
medicine.disease
Prostate-specific antigen
Sialic acid
carbohydrates (lipids)
chemistry
Carbohydrate Sequence
Spectrometry
Mass
Matrix-Assisted Laser Desorption-Ionization
biology.protein
Molecular Medicine
Glycoprotein
Glicoproteïnes
Biotechnology
Zdroj: © OMICS A Journal of Integrative Biology, 2010, vol. 14, núm. 4, p. 465-474
Articles publicats (D-B)
DUGiDocs – Universitat de Girona
instname
Recercat. Dipósit de la Recerca de Catalunya
ISSN: 1557-8100
Popis: 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.
Databáze: OpenAIRE
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