ArticleThe Journal of biological chemistry2016
Mammalian α-1,6-Fucosyltransferase (FUT8) Is the Sole Enzyme Responsible for the N-Acetylglucosaminyltransferase I-independent Core Fucosylation of High-mannose N-Glycans.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed.
- Suppressing α-1,6-Fucosyltransferase With a Novel Small Molecule Inhibitor Ameliorates Inflammation in Murine T-Cell-Mediated Colitis Models.Cellular and molecular gastroenterology and hepatology · 2026Article
- The glycobiology of prostate cancer: an update.Oncogene · 2026Review
- Pairing of high-mannose glycans in human IgE-Fc: implications for secretion and stability.Clinical proteomics · 2026Article
- FUT8-mediated core fucosylation of receptor APN drives entry of multiple alphacoronaviruses.PLoS pathogens · 2026Article
- Exploiting human fucosyltransferase 8 allostery with a covalent inhibitor for core fucosylation suppression.Nature communications · 2026Article
- Fucose metabolism as a central axis linking inflammation, immunity, and cancer in the gut.Frontiers in immunology · 2026Review
- Cell Engineering for Increasing Production of Recombinant Proteins in Mammalian Cells.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2026Review
- FUT8 Is a Critical Driver of Prostate Tumour Growth and Can Be Targeted Using Fucosylation Inhibitors.Cancer medicine · 2025Article
- Targeting fucosyltransferase FUT8 as a prospective therapeutic approach for DLBCL.Oncogenesis · 2025Article
- The Calicophoron daubneyi genome provides new insight into mechanisms of feeding, eggshell synthesis and parasite-microbe interactions.BMC biology · 2025Article
- Article
- The Multifaceted Role of FUT8 in Tumorigenesis: From Pathways to Potential Clinical Applications.International journal of molecular sciences · 2024Review
- FDW028, a novel FUT8 inhibitor, impels lysosomal proteolysis of B7-H3 via chaperone-mediated autophagy pathway and exhibits potent efficacy against metastatic colorectal cancer.Cell death & disease · 2023Article
- Core Fucosylation Mediated by the FucT-8 Enzyme Affects TRAIL-Induced Apoptosis and Sensitivity to Chemotherapy in Human SW480 and SW620 Colorectal Cancer Cells.International journal of molecular sciences · 2023Article
- Article
- Head and neck cancer N-glycome traits are cell line and HPV status-dependent.Analytical and bioanalytical chemistry · 2022Article
- The ulcerative colitis-associated gene FUT8 regulates the quantity and quality of secreted mucins.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Origin of cytoplasmic GDP-fucose determines its contribution to glycosylation reactions.The Journal of cell biology · 2022Article
- Positive association of serum FUT8 activity with renal tubulointerstitial injury in IgA nephropathy patients.Immunity, inflammation and disease · 2022Article
- Inhibition of α(1,6)fucosyltransferase: Effects on Cell Proliferation, Migration, and Adhesion in an SW480/SW620 Syngeneic Colorectal Cancer Model.International journal of molecular sciences · 2022Article
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Authors and funding
2 authors.
Funding
Abstract
Understanding the biosynthetic pathway of protein glycosylation in various expression cell lines is important for controlling and modulating the glycosylation profiles of recombinant glycoproteins. We found that expression of erythropoietin (EPO) in a HEK293S N-acetylglucosaminyltransferase I (GnT I)(-/-) cell line resulted in production of the Man5GlcNAc2 glycoforms, in which more than 50% were core-fucosylated, implicating a clear GnT I-independent core fucosylation pathway. Expression of GM-CSF and the ectodomain of FcγIIIA receptor led to ∼30% and 3% core fucosylation, suggesting that the level of core fucosylation also depends on the nature of the recombinant proteins. To elucidate the GnT I-independent core fucosylation pathway, we generated a stable HEK293S GnT I(-/-) cell line with either knockdown or overexpression of FUT8 by a highly efficient lentivirus-mediated gene transfer approach. We found that the EPO produced from the FUT8 knockdown cell line was the pure Man5GlcNAc2 glycoform, whereas that produced from the FUT8-overexpressing cell line was found to be fully core-fucosylated oligomannose glycan (Man5GlcNAc2Fuc). These results provide direct evidence that FUT8, the mammalian α1,6-fucosyltransferase, is the sole enzyme responsible for the GnT I-independent core fucosylation pathway. The production of the homogeneous core-fucosylated Man5GlcNAc2 glycoform of EPO in the FUT8-overexpressed HEK293S GnT I(-/-) cell line represents the first example of production of fully core-fucosylated high-mannose glycoforms.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.