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Status: Bibliographieeintrag

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Verfasst von:Carvalho, Silvia L. [VerfasserIn]   i
 Catarino, T. A. [VerfasserIn]   i
 Dias, A. M. [VerfasserIn]   i
 Kato, M. [VerfasserIn]   i
 Almeida, A. [VerfasserIn]   i
 Heßling, Bernd [VerfasserIn]   i
 Figueiredo, J. [VerfasserIn]   i
 Gärtner, F. [VerfasserIn]   i
 Sanches, J. M. [VerfasserIn]   i
 Ruppert, Thorsten [VerfasserIn]   i
 Miyoshi, E. [VerfasserIn]   i
 Pierce, M. [VerfasserIn]   i
 Carneiro, F. [VerfasserIn]   i
 Kolarich, D. [VerfasserIn]   i
 Seruca, R. [VerfasserIn]   i
 Yamaguchi, Y. [VerfasserIn]   i
 Taniguchi, N. [VerfasserIn]   i
 Reis, C. A. [VerfasserIn]   i
 Pinho, S. S. [VerfasserIn]   i
Titel:Preventing E-cadherin aberrant N -glycosylation at Asn-554 improves its critical function in gastric cancer
Verf.angabe:S. Carvalho, T.A. Catarino, A.M. Dias, M. Kato, A. Almeida, B. Hessling, J. Figueiredo, F. Gärtner, J.M. Sanches, T. Ruppert, E. Miyoshi, M. Pierce, F. Carneiro, D. Kolarich, R. Seruca, Y. Yamaguchi, N. Taniguchi, C.A. Reis and S.S. Pinho
Jahr:2016
Jahr des Originals:2015
Umfang:13 S.
Fussnoten:Published 20 July 2015 ; Gesehen am 29.04.2020
Titel Quelle:Enthalten in: Oncogene
Ort Quelle:London : Springer Nature, 1997
Jahr Quelle:2016
Band/Heft Quelle:35(2016), 13, Seite 1619-1631
ISSN Quelle:1476-5594
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 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.
DOI:doi:10.1038/onc.2015.225
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

Volltext ; Verlag: https://doi.org/10.1038/onc.2015.225
 Volltext: https://www.nature.com/articles/onc2015225
 DOI: https://doi.org/10.1038/onc.2015.225
Datenträger:Online-Ressource
Sprache:eng
K10plus-PPN:1696834171
Verknüpfungen:→ Zeitschrift

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