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N-glycosylation status of [beta]-haptoglobin in sera of patients with colon cancer, chronic inflammatory diseases and normal subjects
International Journal of Cancer, 09/14/09
Park S-Y et al. – The identified glycans were sialylated or nonsialylated, bi-antennary or tri-antennary structures, with or without terminal fucosylation.
Methods- 17 patients who were diagnosed as having colon cancer and 14 health controls were studied
- Blotting index of serum -haptoglobin with Aleuria aurantia lectin (AAL) was clearly higher for cancer patients than for healthy subjects
- The higher AAL binding of -haptoglobin in colon cancer patients than in healthy subjects appeared to be due to -L-fucosyl residue, since it was eliminated by bovine kidney -fucosidase treatment
- N-linked glycans of serum haptoglobin from colon cancer patients vs. healthy subjects were released by N-glycanase, fluorescence-labeled, and subjected to normal-phase high performance liquid chromatography (NP-HPLC)
- Glycan structures were determined based on glucose unit (GU) values and their changes upon sequential treatment with various exoglycosidases
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