Glycobiology Advance Access originally published online on November 26, 2002
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Glycobiology, 2003, Vol. 13, No. 4 227-244
© 2003 Oxford University Press
Glycosylation of human pancreatic ribonuclease: differences between normal and tumor states
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
Received on June 18, 2002; revised on September 6, 2002; accepted on September 23, 2002
Characterization of the N-glycans from human pancreatic ribonuclease (RNase 1) isolated from healthy pancreas and from pancreatic adenocarcinoma tumor cells (Capan-1 and MDAPanc-3) revealed completely different glycosylation patterns. RNase 1 from healthy cells contained neutral complex biantennary structures, with smaller amounts of tri- and tetraantennary compounds, and glycans with poly-N-acetyllactosamine extensions, all extensively fucosylated. In contrast, RNase 1 glycans from tumor cells (Capan-1) were fucosylated hybrid and complex biantennary glycans with GalNAc-GlcNAc antennae. RNase 1 glycans from Capan-1 and MDAPanc-3 cells also contained sialylated structures completely absent in the healthy pancreas. Some of these features provide distinct epitopes that were clearly detected using monoclonal antibodies against carbohydrate antigens. Thus monoclonal antibodies to Lewisy reacted only with normal pancreatic RNase 1, whereas, in contrast, monoclonal antibodies to sialyl-Lewisx and sialyl-Lewisa reacted only with RNase 1 secreted from the tumor cells. These glycosylation changes in a tumor-secreted protein, which reflect fundamental changes in the enzymes involved in the glycosylation pathway, open up the possibility of using serum RNase 1 as a tumor marker of pancreatic adenocarcinoma.
1 To whom correspondence should be addressed; e-mail: rafael.llorens{at}udg.es and pauline.rudd{at}bioch.ox.ac.uk
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