Search our Database of Scientific Publications and Authors

I’m looking for a
    Aberrant Glycosylation in Cancer: A Novel Molecular Mechanism Controlling Metastasis.
    Cancer Cell 2017 06;31(6):733-735
    Institute for Research and Innovation in Health (i3S), University of Porto, 4200-135 Porto, Portugal; Institute of Molecular Pathology and Immunology of the University of Porto (IPATIMUP), 4200-135 Porto, Portugal; Instituto de Ciências Biomédicas Abel Salazar (ICBAS), University of Porto, 4050-313 Porto, Portugal; Faculty of Medicine of the University of Porto, 4200-319 Porto, Portugal. Electronic address:
    Glycosylation alterations are involved in several steps of human cancer pathogenesis. In this issue of Cancer Cell, Agrawal et al. identified the glycosyltransferase FUT8 as a previously unrecognized mediator of melanoma metastasis, establishing core fucosylation as a potential therapeutic target for prevention and treatment of metastatic tumors.

    Similar Publications

    A Systems Biology Approach Identifies FUT8 as a Driver of Melanoma Metastasis.
    Cancer Cell 2017 Jun;31(6):804-819.e7
    Department of Pathology, New York University School of Medicine, New York, NY 10016, USA; Interdisciplinary Melanoma Cooperative Group, Perlmutter Cancer Center, New York University School of Medicine, New York, NY 10016, USA. Electronic address:
    Association of aberrant glycosylation with melanoma progression is based mainly on analyses of cell lines. Here we present a systems-based study of glycomic changes and corresponding enzymes associated with melanoma metastasis in patient samples. Upregulation of core fucosylation (FUT8) and downregulation of α-1,2 fucosylation (FUT1, FUT2) were identified as features of metastatic melanoma. Read More
    Mammalian α-1,6-Fucosyltransferase (FUT8) Is the Sole Enzyme Responsible for the N-Acetylglucosaminyltransferase I-independent Core Fucosylation of High-mannose N-Glycans.
    J Biol Chem 2016 May 23;291(21):11064-71. Epub 2016 Mar 23.
    From the Department of Chemistry and Biochemistry, University of Maryland College Park, College Park, Maryland 20742
    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. Read More
    Loss of α1,6-Fucosyltransferase Decreases Hippocampal Long Term Potentiation: IMPLICATIONS FOR CORE FUCOSYLATION IN THE REGULATION OF AMPA RECEPTOR HETEROMERIZATION AND CELLULAR SIGNALING.
    J Biol Chem 2015 Jul 15;290(28):17566-75. Epub 2015 May 15.
    From the Division of Regulatory Glycobiology and
    Core fucosylation is catalyzed by α1,6-fucosyltransferase (FUT8), which transfers a fucose residue to the innermost GlcNAc residue via α1,6-linkage on N-glycans in mammals. We previously reported that Fut8-knock-out (Fut8(-/-)) mice showed a schizophrenia-like phenotype and a decrease in working memory. To understand the underlying molecular mechanism, we analyzed early form long term potentiation (E-LTP), which is closely related to learning and memory in the hippocampus. Read More
    Core fucosylation regulates epidermal growth factor receptor-mediated intracellular signaling.
    J Biol Chem 2006 Feb 29;281(5):2572-7. Epub 2005 Nov 29.
    Department of Biochemistry, Osaka University Graduate School of Medicine, Japan.
    alpha1,6-Fucosyltransferase (Fut8) catalyzes the transfer of a fucose residue to N-linked oligosaccharides on glycoproteins via an alpha1,6-linkage to form core fucosylation in mammals. We recently found that disruption of the Fut8 gene induces severe growth retardation and early postnatal death. To investigate the molecular mechanism involved, we have established embryonic fibroblasts of Fut8+/+ and Fut8-/-, derived from wild-type and Fut8-null mice, respectively. Read More