Glycoproteomics analysis to identify a glycoform on haptoglobin associated with lung cancer

Authors

  • Hsien-Yu Tsai,

    1. Institute of Biochemical Sciences, College of Life Science, National Taiwan University, Taipei, Taiwan
    2. Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan
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  • Kongsak Boonyapranai,

    1. Department of Chemistry, Faculty of Science, Chiang Mai University, Chiang Mai, Thailand
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  • Supawadee Sriyam,

    1. Department of Chemistry, Faculty of Science, Chiang Mai University, Chiang Mai, Thailand
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  • Chong-Jen Yu,

    1. Department of Internal Medicine, National Taiwan University Hospital, Taipei, Taiwan
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  • Sz-Wei Wu,

    1. NRPGM Core Facilities for Proteomics and Glycomics, Taipei, Taiwan
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  • Kay-Hooi Khoo,

    1. Institute of Biochemical Sciences, College of Life Science, National Taiwan University, Taipei, Taiwan
    2. Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan
    3. NRPGM Core Facilities for Proteomics and Glycomics, Taipei, Taiwan
    4. Genomics Research Center, Academia Sinica, Taipei, Taiwan
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  • Suree Phutrakul,

    1. Department of Chemistry, Faculty of Science, Chiang Mai University, Chiang Mai, Thailand
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  • Shui-Tein Chen

    Corresponding author
    1. Institute of Biochemical Sciences, College of Life Science, National Taiwan University, Taipei, Taiwan
    2. Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan
    3. Genomics Research Center, Academia Sinica, Taipei, Taiwan
    • Institute of Biological Chemistry, Academia Sinica, 128 Academia Road, Sec. 2, Nankang, Taipei 115, Taiwan Fax: +886-2-27883473
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  • Colour Online: See the article online to view Figs. 1 and 2 in colour.

Abstract

Glycosylation is a common protein modification that is of interest in current cancer research because altered carbohydrate moieties are often found during cancer progress. A search for biomarkers in human lung cancer serum samples using glycoproteomic approaches identified fucosylated haptoglobin (Hp) significantly increased in serum of each subtype of lung cancer compared to normal donors. In addition, MS provided evidence of an increase of Hp fucosylation; the glycan structure was determined to be an α 2,6-linked tri-sialylated triantennary glycan containing α1,3-linked fucose attached to the four-linked position of the three-arm mannose of N-linked core pentasaccharide. These preliminary findings suggest that the specific glycoform of Hp may be useful as a marker to monitor lung cancer progression.

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