Asian Pacific Journal of Cancer Prevention

Asian Pacific Journal of Cancer Prevention (아시아태평양암예방학회)
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Differential Expression of O-glycoprotein Glycans in Cholangiocarcinoma Cell Lines

  • Talabnin, Krajang (School of Pathology, Institute of Medicine, Suranaree University of Technology) ;
  • Talabnin, Chutima (School of Biochemistry, Institute of Science, Suranaree University of Technology) ;
  • Ishihara, Mayumi (Complex Carbohydrate Research Center, The University of Georgia) ;
  • Azadi, Parastoo (Complex Carbohydrate Research Center, The University of Georgia) ;
  • Wongkham, Sopit (Department of Biochemistry, Faculty of Medicine, Khon Kaen University) ;
  • Sripa, Banchob (Department of Pathology, Faculty of Medicine, Khon Kaen University)
  • Published : 2016.03.07
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Abstract

Protein glycosylation is the most common posttranslational modification in mammalian cells. Aberrant protein glycosylation has been reported in various diseases, including cancer. We identified and quantified the glycan structures of O-linked glycoprotein from cholangiocarcinoma (CCA) cell lines from different histological types and compared their profiles by nanospray ionization-linear ion trap mass spectrometry (NSI-$MS^n$). Five human CCA cell lines, K100, M055, M139, M213 and M214 were characterized. The results showed that the O-linked glycans of the CCA cell lines comprised tri- to hexa-saccharides with terminal galactose and sialic acids: NeuAc1Gal1GalNAc1, Gal2GlcNAc1GalNAc1, NeuAc2Gal1GalNAc1 NeuAc1Gal2GlcNAc1GalNAc1 and NeuAc2Gal2GlcNAc1GalNAc1 All five CCA cell lines showed a similar glycan pattern, but with differences in their quantities. NeuAc1Gal1GalNAc1 proved to be the most abundant structure in poorly differentiated adenocarcinoma (K100; 57.1%), moderately differentiated adenocarcinoma (M055; 42.6%) and squamous cell carcinoma (M139; 43.0%), while moderately to poorly differentiated adenocarcinoma (M214; 40.1%) and adenosquamous cell carcinoma (M213; 34.7%) appeared dominated by $NeuA_{c2}Gal_1GalNA_{c1}$. These results demonstrate differential expression of the O-linked glycans in the different histological types of CCA. All five CCA cell lines have abundant terminal sialic acid (NeuAc) O-linked glycans, suggesting an important role for sialic acid in cancer cells. Our structural analyses of glycans may provide important information regarding physiology of disease-related glycoproteins in CCA.

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