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

• Main Authors: Tsai H.-Y., Boonyapranai K., Sriyam S., Yu C.-J., Wu S.-W., Khoo K.-H., Phutrakul S., Chen S.-T.
• Format: Article
• Language: English
• Published: 2014
• Online Access: http://www.scopus.com/inward/record.url?eid=2-s2.0-79956282745&partnerID=40&md5=4135aab5ef152a8a30e8c7611946762b; http://cmuir.cmu.ac.th/handle/6653943832/6545
• Institution: Chiang Mai University

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. © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.