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

• Type: Another Publication in an International Scientific Journal
• Date: 2011

Authors

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

Journal

Title: Cellular and Molecular Life Sciences

Vol. 68

Pages: 1011-1020

ISSN: 1420-682X

Publisher: Springer Nature

Indexing

ISI Web of Knowledge - 110 Citations

Scopus - 117 Citations

Other information

Authenticus ID: 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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 10