Differential Expression of O-glycoprotein Glycans in Cholangiocarcinoma Cell Lines

Talabnin, Krajang; Talabnin, Chutima; Ishihara, Mayumi; Azadi, Parastoo; Wongkham, Sopit; Sripa, Banchob

doi:10.7314/apjcp.2016.17.2.691

Cited by 7 publications

(10 citation statements)

References 17 publications

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“… 12 Notably, a lectin microarray-based sero-biomarker has been reported for the detection of O -linked glycosylation in patients with cholangiocarcinoma; 13 cholangiocarcinoma cell lines exhibit differential expression of O -glycans, based on the histological type of cholangiocarcinoma. 14 Our prior research revealed elevated expression of N -linked glycoprotein glycans in serum from patients with cholangiocarcinoma, compared with healthy controls; 15 elevated glycosphingolipid levels have also been associated with shorter survival in patients with cholangiocarcinoma. 16 …”

Section: Introductionmentioning

confidence: 93%

Ganglioside GM2: a potential biomarker for cholangiocarcinoma

Talabnin

Kumagai

et al. 2020

J Int Med Res

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Objective To investigate the expression of glycosphingolipids in serum and tissue from patients with cholangiocarcinoma compared with healthy controls. Methods Nanospray ionization-linear ion trap mass spectrometry (NSI-MSn) was used to demonstrate the comparative structural glycomics of glycosphingolipids in serum from patients with cholangiocarcinoma (n=15), compared with healthy controls (n = 15). GM2 expression in cholangiocarcinoma tissues (n = 60) was evaluated by immunohistochemistry. Results Eleven glycosphingolipids were detected by NSI-MSn: CMH (ceramide monohexose), Lac-Cer (galactose (Gal)β1-4 glucose (Glc)β1-1'-ceramide), Gb3 (Galα1-4Galβ1-4Glcβ1-1'-ceramide), Gb4/Lc4 (N-acetylgalactosamine (GalNAc)β1-3Galα1-4Galβ1-4Glcβ1-1'-ceramide/Galβ1-4 N-acetylglucosamine (GlcNAc)β1-3Galβ1-4Glcβ1-1'-ceramide), GM3 (N-acetylneuraminic acid (NeuAc)2-3Galβ1-4Glcβ1-1'-ceramide), GM2 (GalNAcβ1-4[NeuAc2-3]Galβ1-4Glcβ1-1'-ceramide), GM1 (Galβ1-3GalNAcβ1-4[NeuAc2-3]Galβ1-4Glcβ1-1'-ceramide), hFA (hydroxylated fatty acid)-CMH, hFA-Lac-Cer, hFA-Gb3, and hFA-GM3. Lac-Cer was the most abundant structure among the lactosides and globosides (normal, 24.40% ± 0.11%; tumor, 24.61% ± 2.10%), while GM3 predominated among the gangliosides (normal, 29.14% ± 1.31%; tumor, 30.53% ± 4.04%). The two glycosphingolipids that significantly differed between healthy controls and patients with cholangiocarcinoma were Gb3 and GM2. High expression of GM2 was associated with vascular invasion in tissue from patients with cholangiocarcinoma. Conclusions Altered expression of glycosphingolipids in tissue and serum from patients with cholangiocarcinoma may contribute to tumor growth and progression. The ganglioside GM2, which significantly increased in the serum of patients with cholangiocarcinoma, represents a promising target as a biomarker for cholangiocarcinoma.

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Section: Introductionmentioning

confidence: 93%

Ganglioside GM2: a potential biomarker for cholangiocarcinoma

Talabnin

Kumagai

et al. 2020

J Int Med Res

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“…Permethylation is currently the most popular derivatization method for sialylated O ‐glycans, which has been used for the O ‐glycosylation profiling of recombinant glycoproteins, mucins, and proteins from serum or cells . Excluding permethylation, the derivatization methods commonly used in sialylated N ‐glycan analysis have not been widely employed for sialylated O ‐glycans.…”

Section: Oligosaccharidesmentioning

confidence: 99%

“…Permethylation is currently the most popular derivatization method for sialylated O-glycans, which has been used for the Oglycosylation profiling of recombinant glycoproteins, mucins, and proteins from serum or cells. [262][263][264][265][266] Excluding permethylation, the mode. 270 The analyte-ILM mixture shows homogeneity well on the target plate, which may be useful for automated and quantitative analysis using MALDI-MS.…”

Section: Amidationmentioning

confidence: 99%

Mass spectrometry for protein sialoglycosylation

Zhang

Wang

et al. 2017

Mass Spectrometry Reviews

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Sialic acids are a family of structurally unique and negatively charged nine-carbon sugars, normally found at the terminal positions of glycan chains on glycoproteins and glycolipids. The glycosylation of proteins is a universal post-translational modification in eukaryotic species and regulates essential biological functions, in which the most common sialic acid is N-acetyl-neuraminic acid (2-keto-5-acetamido-3,5-dideoxy-D-glycero-D-galactononulopyranos-1-onic acid) (Neu5NAc). Because of the properties of sialic acids under general mass spectrometry (MS) conditions, such as instability, ionization discrimination, and mixed adducts, the use of MS in the analysis of protein sialoglycosylation is still challenging. The present review is focused on the application of MS related methodologies to the study of both N- and O-linked sialoglycans. We reviewed MS-based strategies for characterizing sialylation by analyzing intact glycoproteins, proteolytic digested glycopeptides, and released glycans. The review concludes with future perspectives in the field.

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“…It has been demonstrated that the lectin microarray-based sero-biomarker is able to detect O -linked glycosylation in CCA ( 14 ). Furthermore, using different CCA cell lines, it has been revealed that different histological types of CCA exhibit differential expression levels of O -glycans ( 15 ). In-depth characterization of the glycans expressed in the serum of patients with CCA may facilitate the identification of potential CCA biomarkers.…”

Section: Introductionmentioning

confidence: 99%

Increased expression of the high‑mannose M6N2 and NeuAc3H3N3M3N2F tri‑antennary N‑glycans in cholangiocarcinoma

Talabnin

Ishihara

et al. 2017

Oncol Lett

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Changes in protein glycosylation have been reported in various types of cancer, including cholangiocarcinoma (CCA). Nanospray ionization-linear ion trap mass spectrometry (NSI-MSn) was used in the present study to determine the comparative structural glycomics of the N-linked glycans in the serum of patients with CCA compared with healthy controls. A total of 5 high-mannose and 4 complex N-linked glycans were detected. Mannose7-N-acetyl-glucosamine2 was the most abundant structure among the high-mannose types (control 12.12±2.54 vs. CCA 9.27±2.66%), whereas NeuAc2H2N2M3N2 predominated the complex types (control 61.17±2.55 vs. CCA 64.68±4.23%). The expression of 3 different N-glycans differed significantly between the CCA cases and controls. These included mannose6-N-acetyl-glucosamine2 (P=0.044), mannose9-N-acetyl-glucosamine2 (Ρ=0.030) and NeuAc3H3N3M3N2F (Ρ=0.002). These three glycan structures may therefore be associated with tumor progression in CCA and may be useful for its diagnosis.

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Differential Expression of O-glycoprotein Glycans in Cholangiocarcinoma Cell Lines

Cited by 7 publications

References 17 publications

Ganglioside GM2: a potential biomarker for cholangiocarcinoma

Ganglioside GM2: a potential biomarker for cholangiocarcinoma

Mass spectrometry for protein sialoglycosylation

Increased expression of the high‑mannose M6N2 and NeuAc3H3N3M3N2F tri‑antennary N‑glycans in cholangiocarcinoma

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