学術雑誌論文

学術雑誌論文

text

Journal of Biological Chemistry. 2004, 279(19), p. 19747-19754

Introduction of Bisecting GlcNAc into Integrin α5β1 Reduces Ligand Binding and Down-regulates Cell Adhesion and Cell Migration

American Society for Biochemistry and Molecular Biology

英語

text

2004-05

https://doi.org/10.1074/jbc.M311627200

This research was originally published in the Journal of Biological Chemistry. Tomoya Isaji, Jianguo Gu, Ryoko Nishiuchi, Yanyang Zhao, Motoko Takahashi, Eiji Miyoshi, Koichi Honke, Kiyotoshi Sekiguchi and Naoyuki Taniguchi. Introduction of Bisecting GlcNAc into Integrin α5β1 Reduces Ligand Binding and Down-regulates Cell Adhesion and Cell Migration. J. Biol. Chem. 2004; 279: 19747-19754 © the American Society for Biochemistry and Molecular Biology

The enzyme β1,4-N-acetylglucosaminyltransferase III (GnT-III) catalyzes the addition of a bisecting GlcNAc residue to glycoproteins, resulting in a modulation in biological function. Our previous studies showed that the transfection of the GnT-III gene into B16 melanoma cells results in a suppression of invasive ability and lung colonization. The suppression has been postulated to be due to an increased level of E-cadherin expression on the cell surface, which in turn leads to the up-regulation of cell-cell adhesion. In this study, we report on the effects of overexpression of GnT-III on cell-matrix adhesion. The overexpression of GnT-III, but not that of an enzymatic inactive GnT-III (D323A), inhibits cell spreading and migration on fibronectin, a specific ligand for integrin α5β1, and the focal adhesion kinase phosphorylation. E4-PHA lectin blot analyses showed that the levels of bisecting GlcNAc structures on the integrin α5 subunit as well as α2 and α3 subunits immunoprecipitated from GnT-III transfectants were substantially increased. In addition, the affinity of the binding of integrin α5β1 to fibronectin was significantly reduced by the introduction of the bisecting GlcNAc, to the α5 subunit. These findings suggest that the modification of N-glycan of integrin by GnT-III inhibits its ligand binding ability, subsequently leading to the down-regulation of integrin-mediated signaling.

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Introduction of Bisecting GlcNAc into Integrin α5β1 Reduces Ligand Binding and Down-regulates Cell Adhesion and Cell Migration

American Society for Biochemistry and Molecular Biology

英語

2004-05

Journal of Biological Chemistry

279

19

19747

19754

https://doi.org/10.1074/jbc.M311627200

https://hdl.handle.net/11094/71430