ArticleScientific reports2015
Specific N-glycans of Hepatocellular Carcinoma Cell Surface and the Abnormal Increase of Core-α-1, 6-fucosylated Triantennary Glycan via N-acetylglucosaminyltransferases-IVa Regulation.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers, 1 of them a synthesis that pooled it.
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Who cites it
30 citing papers in PubMed, 1 synthesis or guideline pooled it, 55 citations in OpenAlex.
- Expression of genes that control core fucosylation in hepatocellular carcinoma: Systematic review.World journal of gastroenterology · 2019Pooled it
- Targeting MGAT4A-Mediated N-Glycosylation as a Therapeutic Strategy to Inhibit Glioblastoma Stem Cell Invasion.Exploration (Beijing, China) · 2026Article
- Serum N-glycan NA3Fb identified as a prognostic biomarker of poor outcome in HBV-related hepatocellular carcinoma.Cancer cell international · 2026Article
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- Alcohol induces α2-6sialo mucin O-glycans that kill U937 macrophages mediated by sialic acid-binding immunoglobulin-like lectin 7 (Siglec 7).FEBS open bio · 2025Article
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- Protein glycosylation alterations in hepatocellular carcinoma: function and clinical implications.Oncogene · 2023Review
- Structure-function correlates of fibrinogen binding byProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Mass spectrometry based biomarkers for early detection of HCC using a glycoproteomic approach.Advances in cancer research · 2023Review
- Modeling and integration of N-glycan biomarkers in a comprehensive biomarker data model.Glycobiology · 2022Article
- N-glycosylation, a leading role in viral infection and immunity development.Molecular biology reports · 2022Review
- Discovery of a lectin domain that regulates enzyme activity in mouse N-acetylglucosaminyltransferase-IVa (MGAT4A).Communications biology · 2022Article
- Precision N-glycoproteomics reveals elevated LacdiNAc as a novel signature of intrahepatic cholangiocarcinoma.Molecular oncology · 2022Article
- Imaging Mass Spectrometry Reveals Alterations in N-Linked Glycosylation That Are Associated With Histopathological Changes in Nonalcoholic Steatohepatitis in Mouse and Human.Molecular & cellular proteomics : MCP · 2022Article
- Serum N-glycan profiling as a diagnostic biomarker for the identification of hepatitis B virus-associated hepatocellular carcinoma.Journal of gastrointestinal oncology · 2022Article
- High-dimensionality reduction clustering of complex carbohydrates to study lung cancer metabolic heterogeneity.Advances in cancer research · 2022Article
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- Article
- FUT8 Alpha-(1,6)-Fucosyltransferase in Cancer.International journal of molecular sciences · 2021Review
- [Application of serum N -glycan profiling diagnostic model in evaluation of liver fibrosis in patients with hepatitis C].Zhonghua gan zang bing za zhi = Zhonghua ganzangbing zazhi = Chinese journal of hepatology · 2020Article
Corrections and comments
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Authors and funding
12 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glycosylation alterations of cell surface proteins are often observed during the progression of malignancies. The specific cell surface N-glycans were profiled in hepatocellular carcinoma (HCC) with clinical tissues (88 tumor and adjacent normal tissues) and the corresponding serum samples of HCC patients. The level of core-α-1,6-fucosylated triantennary glycan (NA3Fb) increased both on the cell surface and in the serum samples of HCC patients (p < 0.01). Additionally, the change of NA3Fb was not influenced by Hepatitis B virus (HBV)and cirrhosis. Furthermore, the mRNA and protein expression of N-acetylglucosaminyltransferase IVa (GnT-IVa), which was related to the synthesis of the NA3Fb, was substantially increased in HCC tissues. Knockdown of GnT-IVa leads to a decreased level of NA3Fb and decreased ability of invasion and migration in HCC cells. NA3Fb can be regarded as a specific cell surface N-glycan of HCC. The high expression of GnT-IVa is the cause of the abnormal increase of NA3Fb on the HCC cell surface, which regulates cell migration. This study demonstrated the specific N-glycans of the cell surface and the mechanisms of altered glycoform related with HCC. These findings lead to better understanding of the function of glycan and glycosyltransferase in the tumorigenesis, progression and metastasis of HCC.
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