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Int J Mass Spectrom. 2011 Aug 15;305(2):185-198. doi: 10.1016/j.ijms.2010.11.007.

Glycomic Alterations in the Highly-abundant and Lesser-abundant Blood Serum Protein Fractions for Patients Diagnosed with Hepatocellular Carcinoma.

International journal of mass spectrometry

Pilsoo Kang, Milan Madera, William R Alley, Radoslav Goldman, Yehia Mechref, Milos V Novotny

Affiliations

  1. National Center for Glycomics and Glycoproteomics ; Department of Chemistry, Bloomington, IN, USA, 47405.

PMID: 23788846 PMCID: PMC3685172 DOI: 10.1016/j.ijms.2010.11.007

Abstract

Hepatocellular cancer is a serious human disease with an unfortunately low survival rate. It further poses a significant epidemic threat to our society through its viral vectors associated with cirrhosis conditions preceding the cancer. A search for biomarkers of these diseases enlists analytical glycobiology, in general, and quantitative biomolecular mass spectrometry (MS), in particular, as valuable approaches to cancer research. The recent advances in quantitative glycan permethylation prior to MALDI-MS oligosaccharide profiling has enabled us to compare the glycan quantitative proportions in the small serum samples of cancer and cirrhotic patients against control individuals. We were further able to fractionate the major serum proteins from the minor components and compare statistically their differential glycosylation, elucidating some causes of quantitatively unusual glycosylation events. Numerous glycan structures were tentatively identified and connected with the origin proteins, with a particular emphasis on sialylated and fucosylated glycans.

Keywords: MALDI-TOF MS; glycans; glycomics; hepatocellular carcinoma; immunoaffinity fractionation; permethylation

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