Asian Pacific Journal of Cancer Prevention

  • 제17권2호
  • /
  • Pages.691-695
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  • 2016
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  • 1513-7368(pISSN)
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  • 2476-762X(eISSN)
아시아태평양암예방학회 (Asian Pacific Journal of Cancer Prevention)
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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)
  • 발행 : 2016.03.07
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초록

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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피인용 문헌

  1. Mass spectrometry for protein sialoglycosylation pp.02777037, 2017, https://doi.org/10.1002/mas.21555