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. Author manuscript; available in PMC: 2010 Dec 1.
Published in final edited form as: Curr Opin Chem Biol. 2009 Sep 21;13(5-6):601–607. doi: 10.1016/j.cbpa.2009.08.015

Table 1.

Changes in glycosylation and potential N- and O-glycan biomarkers for several types of cancer. The arrows indicate either an increase (↑) or a decrease (↓) in intensity levels of the biomarker or glycosylation change.

Cancer Biological Sample Glycosylation Change/Potential Glycan Biomarker ↑ or ↓
General ▪ Branched N-glycans [54], specifically β1–6 GlcNAc branching
▪ Truncated O-glycans [54]
▪ Sialic acids – amount, linkage, acetylation and expression[54] ↑ or ↓

Prostate Sera[11,45,52] ▪ Complex N-glycans[11] ↑ or ↓
▪ High-mannose glycans/mannosylation[44] ↑ and ↓
▪ Total fucosylation[44]
▪ Fucose and α(2,3)-linked sialic acid content of PSA[50]

Breast Cell Lines[54]
Sera[32,51,28]
▪ An α(1,3)-fucosylated monogalactosylated triantennary glycan[31]
▪ High mannose N-glycans[53] ↑ or ↓
▪ N-glycan branching
▪ Hybrid structures
▪ Fucosylation in O-glycans
▪ N-glycan sialylation and fucosylation[27, 53] ↓ and ↑
▪ Core 1 type O-glycans[50] ↑ or ↓
▪ O-glycan sialylation[50]

Liver Cell Lines[49]
Sera[43,46,53]
▪ Core fucosylated structures[48]
▪ Outer-arm fucosylation in highly branched glycans[52]
▪ A branched α(1,3)-fucosylated triantennary N-glycan[45]

Ovarian Sera[50] ▪ Core fucosylated, agalactosyl biantennary glycans and sialyl Lewis x[49]

Pancreatic Cell Lines[47]
Sera[48]
▪ Fucosylation[46,47]

Gastric Cell Lines[44] ▪ Free complex-type N-glycans[43]
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