Glycobiology Advance Access published online on January 17, 2007
Glycobiology, doi:10.1093/glycob/cwm002
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Glycosylation of serum ribonuclease 1 indicates a major endothelial origin and reveals an increase in core fucosylation in pancreatic cancer
1 Unitat de Bioquímica i Biologia Molecular, Departament de Biologia, Universitat de Girona, Girona, 17071, Spain
2 Glycobiology Institute, Department of Biochemistry, Oxford University, Oxford OX1 3QU, United Kingdom
3 Unitat de Digestiu, Hospital Universitari Dr. Josep Trueta, Girona, 17007, Spain
4 INSERM, E113; Université Bordeaux 1, 33405 Talence Cedex, France
* Address correspondence to these authors at: Unitat de Bioquímica i Biologia Molecular, Departament de Biologia, Universitat de Girona, Campus de Montilivi s/n. 17071, Girona, Spain. Phone 34 972418370 Fax 34 972418370; e-mail: rosa.peracaula{at}udg.es. Or Dublin-Oxford Glycobiology Laboratory, NIBRT, Conway Institute, University College Dublin, Belfield, Dublin 4, Ireland. Phone 353 1 7166728 Fax 353 1 7166713 e-mail: pauline.rudd{at}nibrt.ie
Received on October 11, 2006; revised on December 11, 2006; accepted on January 9, 2007
Human pancreatic ribonuclease 1 (RNase 1) is a glycoprotein expressed mainly by the pancreas and also found in endothelial cells. The diagnosis of pancreatic cancer (PaC) remains difficult and therefore the search for sensitive and specific markers is required.
Previous studies showed that RNase 1 from human healthy pancreas contained only neutral glycans, while RNase 1 from PaC cell lines contained sialylated structures. To determine whether these glycan tumour-cell associated changes were also characteristic of serum RNase 1 and could be used as a marker of PaC, we have analysed the glycosylation of serum RNase 1. The origin of serum RNase 1 was also investigated.
Serum RNase 1 from two PaC patients and two controls were purified and the glycans analysed by HPLC-based sequencing and mass spectrometry. Although normal and tumour serum RNase 1 contained the same glycan structures, there was an increase of 40% in core fucosylation in the main sialylated bi-antennary glycans in the PaC serum RNase 1. This change in proportion would be indicative of a subset of tumour-associated glycoforms of RNase 1 which may provide a biomarker for PaC.
Two-dimensional electrophoresis of the RNase 1 from several endothelial cell lines, EA.hy926, HUVEC, HUMMEC and HULEC, showed basically the same pattern and was also very similar to that of serum RNase 1. RNase 1 from EA.hy926 was then purified and presented a glycosylation profile very similar to that from serum RNase 1, suggesting that endothelial cells are the main source of this enzyme.
Key words: Endothelial cell line EA.hy926 / N-Glycosylation / Pancreatic Cancer / Serum human pancreatic ribonuclease / Two Dimensional Electrophoresis
5 Current address: Dublin-Oxford Glycobiology Laboratory, NIBRT, Conway Institute, University College Dublin, Belfield, Dublin 4, Ireland.
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