Glycobiology Advance Access originally published online on January 17, 2007
Glycobiology 2007 17(4):388-400; 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
3 Unitat de Bioquímica i Biologia Molecular, Departament de Biologia, Universitat de Girona, Campus de Montilivi, Girona 17071, Spain
4 Department of Biochemistry, Glycobiology Institute, Oxford University, Oxford OX1 3QU, UK
5 Unitat de Digestiu, Hospital Universitari Dr Josep Trueta, Girona 17007, Spain
6 INSERM, E113, Université Bordeaux 1, 33405 Talence Cedex, France
1 To whom correspondence should be addressed; Tel: +34 972418370; Fax: +34 972418370; e-mail: rosa.peracaula{at}udg.es or Tel: +353 17166728; Fax: +353 17166713; 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, whereas RNase 1 from PaC cell lines contained sialylated structures. To determine whether these glycan tumor cell-associated changes were also characteristic of serum RNase 1 and could be used as a marker of PaC, we have analyzed 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 was purified and the glycans analyzed by high-performance liquid chromatography (HPLC)-based sequencing and mass spectrometry. Although normal and tumor serum RNase 1 contained the same glycan structures, there was an increase of 40% in core fucosylation in the main sialylated biantennary glycans in the PaC serum RNase 1. This change in proportion would be indicative of a subset of tumor-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, human umbilical vein endothelial cells (HUVEC), human mammary microvessel endothelial cells (HuMMEC), and human lung microvessel endothelial cells (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
2 Present address: Dublin–Oxford Glycobiology Laboratory, NIBRT, Conway Institute, University College Dublin, Belfield, Dublin 4, Ireland
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