Modulation of E-cadherin function and dysfunction by N-glycosylation

• Tipo: Outra Publicação em Revista Científica Internacional
• Data: 2011

Autores

Pinho, SS (Autor) Outra; Seruca, R (Autor) FMUP; Gaertner, F (Autor) Outra; Yamaguchi, Y (Autor) Outra; Gu, JG (Autor) Outra; Taniguchi, N (Autor) Outra; Celso Reis (Autor) ICBAS

Revista

Título: Cellular and Molecular Life Sciences

Vol. 68

Páginas: 1011-1020

ISSN: 1420-682X

Editora: Springer Nature

Indexação

ISI Web of Knowledge - 110 Citações

Scopus - 117 Citações

Outras Informações

ID Authenticus: P-002-TXG

DOI: 10.1007/s00018-010-0595-0

Abstract (EN): Several mechanisms have been proposed to explain the E-cadherin dysfunction in cancer, including genetic and epigenetic alterations. Nevertheless, a significant number of human carcinomas have been seen that show E-cadherin dysfunction that cannot be explained at the genetic/epigenetic level. A substantial body of evidence has appeared recently that supports the view that other mechanisms operating at the post-translational level may also affect E-cadherin function. The present review addresses molecular aspects related to E-cadherin N-glycosylation and evidence is presented showing that the modification of N-linked glycans on E-cadherin can affect the adhesive function of this adhesion molecule. The role of glycosyltransferases involved in the remodeling of N-glycans on E-cadherin, including N-acetylglucosaminyltransferase III (GnT-III), N-acetylglucosaminyltransferase V (GnT-V), and the alpha 1,6 fucosyltransferase (FUT8) enzyme, is also discussed. Finally, this review discusses an alternative functional regulatory mechanism for E-cadherin operating at the post-translational level, N-glycosylation, that may underlie the E-cadherin dysfunction in some carcinomas.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 10