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  • Preventing E-cadherin aberrant N-glycosylation at Asn-554 improves its critical function in gastric cancer

    Author(s)
    Carvalho, S
    Catarino, TA
    Dias, AM
    Kato, M
    Almeida, A
    Hessling, B
    Figueiredo, J
    Gaertner, F
    Sanches, JM
    Ruppert, T
    Miyoshi, E
    Pierce, M
    Carneiro, F
    Kolarich, D
    Seruca, R
    Yamaguchi, Y
    Taniguchi, N
    Reis, CA
    Pinho, SS
    Griffith University Author(s)
    Kolarich, Daniel
    Year published
    2016
    Metadata
    Show full item record
    Abstract
    E-cadherin is a central molecule in the process of gastric carcinogenesis and its posttranslational modifications by N-glycosylation have been described to induce a deleterious effect on cell adhesion associated with tumor cell invasion. However, the role that site-specific glycosylation of E-cadherin has in its defective function in gastric cancer cells needs to be determined. Using transgenic mice models and human clinical samples, we demonstrated that N-acetylglucosaminyltransferase V (GnT-V)-mediated glycosylation causes an abnormal pattern of E-cadherin expression in the gastric mucosa. In vitro models further indicated ...
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    E-cadherin is a central molecule in the process of gastric carcinogenesis and its posttranslational modifications by N-glycosylation have been described to induce a deleterious effect on cell adhesion associated with tumor cell invasion. However, the role that site-specific glycosylation of E-cadherin has in its defective function in gastric cancer cells needs to be determined. Using transgenic mice models and human clinical samples, we demonstrated that N-acetylglucosaminyltransferase V (GnT-V)-mediated glycosylation causes an abnormal pattern of E-cadherin expression in the gastric mucosa. In vitro models further indicated that, among the four potential N-glycosylation sites of E-cadherin, Asn-554 is the key site that is selectively modified with β1,6 GlcNAc-branched N-glycans catalyzed by GnT-V. This aberrant glycan modification on this specific asparagine site of E-cadherin was demonstrated to affect its critical functions in gastric cancer cells by affecting E-cadherin cellular localization, cis-dimer formation, molecular assembly and stability of the adherens junctions and cell–cell aggregation, which was further observed in human gastric carcinomas. Interestingly, manipulating this site-specific glycosylation, by preventing Asn-554 from receiving the deleterious branched structures, either by a mutation or by silencing GnT-V, resulted in a protective effect on E-cadherin, precluding its functional dysregulation and contributing to tumor suppression.
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    Journal Title
    Oncogene
    Volume
    35
    Issue
    13
    DOI
    https://doi.org/10.1038/onc.2015.225
    Subject
    Clinical sciences
    Oncology and carcinogenesis
    Oncology and carcinogenesis not elsewhere classified
    Publication URI
    http://hdl.handle.net/10072/339683
    Collection
    • Journal articles

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