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

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 (H...

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Bibliographic Details
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
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Institution: Chiang Mai University
Language: English
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Summary: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.