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Branched N-glycans regulate the biological functions of integrins and cadherins.
- Source :
- FEBS Journal; May2008, Vol. 275 Issue 9, p1939-1948, 10p, 2 Black and White Photographs, 2 Diagrams
- Publication Year :
- 2008
-
Abstract
- Glycosylation is one of the most common post-translational modifications, and approximately 50% of all proteins are presumed to be glycosylated in eukaryotes. Branched N-glycans, such as bisecting GlcNAc, β-1,6-GlcNAc and core fucose (α-1,6-fucose), are enzymatic products of N-acetylglucosaminyltransferase III, N-acetylglucosaminyltransferase V and α-1,6-fucosyltransferase, respectively. These branched structures are highly associated with various biological functions of cell adhesion molecules, including cell adhesion and cancer metastasis. E-cadherin and integrins, bearing N-glycans, are representative adhesion molecules. Typically, both are glycosylated by N-acetylglucosaminyltransferase III, which inhibits cell migration. In contrast, integrins glycosylated by N-acetylglucosaminyltransferase V promote cell migration. Core fucosylation is essential for integrin-mediated cell migration and signal transduction. Collectively, N-glycans on adhesion molecules, especially those on E-cadherin and integrins, play key roles in cell–cell and cell–extracellular matrix interactions, thereby affecting cancer metastasis. [ABSTRACT FROM AUTHOR]
- Subjects :
- CADHERINS
CELL adhesion molecules
GLYCOPROTEINS
GLYCOSYLATION
INTEGRINS
Subjects
Details
- Language :
- English
- ISSN :
- 1742464X
- Volume :
- 275
- Issue :
- 9
- Database :
- Complementary Index
- Journal :
- FEBS Journal
- Publication Type :
- Academic Journal
- Accession number :
- 31728830
- Full Text :
- https://doi.org/10.1111/j.1742-4658.2008.06346.x