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- W2783291839 abstract "2433 Glycosylation is highly sensitive to the biochemical environment and is involved in various biological processes including differentiation, motility, and intracellular signaling, as well as oncogenesis and metastasis. Therefore the tumor specific alterations in protein glycosylation on the cell surface and in body fluids might be potential targets for the new cancer diagnostics and therapeutics. We here report our new approach to identification of carbohydrate-targeting serum tumor markers for lung cancer based on 3 key technologies: 1) removal of 14 abundant proteins from serum, 2) Lectin-coupled ProteinChip System, and 3) use of the acidic glycoprotein-compatible matrix for SELDI-TOF MS analysis. We pre-treated serum samples with immunodepletion-HPLC column to remove 14 abundant proteins (constituting 94% of serum protein), because only a limited number of proteins could be detected by previous ProteinChip-based approaches using crude serum samples. These low-abundant serum components were sequentially processed on Jacalin- or SNA-lectin chips, recognizing glycoproteins with pan-O-type glycans or Neu5Ac (α2, 6) Gal/GalNAc structures, respectively, followed by SELDI-TOF MS analysis. Since current SELDI-TOF MS analysis with general matrices (CHCA, DHB, SPA, etc.) has a major problem for the quantitative analysis of acidic glycoproteins due to heterolytic disassembly of neuraminic acid moieties, we overcame the problem by use of 2, 4, 6-Trihydroxyacetophenone in ammonium citrate solution as a matrix, which allowed quantitative and reproducible profiling of sialylated glycoproteins without decay of neuraminic acid moieties. In this study, we identified a protein peak with m/z = 9850 as a candidate carbohydrate-targeting tumor marker, in which significant loss of Neu5Ac (α2, 6) Gal/GalNAc structure was observed in 10 lung adenocarcinoma patients’ sera, but not in 10 healthy controls. We determined this candidate as Apolipoprotein C-III (APOC3) by MALDI-QIT-TOF MS/MS analysis, and successfully identified its O-glycosylation site by MALDI-QIT-TOF MS³ analysis. Further enzymatic and mass spectrometric experiments revealed that APOC3 protein had disialyrated and monosialyrated forms in human serum. Importantly APOC3 with the monosialyrated glycan structure was significantly more dominant in lung cancer patients’ sera than in normal sera. These results were validated by western blotting and mass spectrometry-based glycan structure analysis using the same set of serum samples. Our Lectin-coupled ProteinChip System will provide a wide range of applications with high-throughput and reproducible profiling of cancer-specific alterations of glycan structures on multiple serum proteins, which should be valuable for biomarker development and the study of variations in glycan structures in any type of human disease." @default.
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- W2783291839 date "2008-05-01" @default.
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- W2783291839 title "A novel glycoproteomic approach for the discovery of carbohydrate-targeting serum tumor markers for lung cancer using Lectin-coupled ProteinChip system" @default.
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