Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (32)
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Seberger, P. J.
Right arrow Articles by Chaney, W. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Seberger, P. J.
Right arrow Articles by Chaney, W. G.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Glycobiology, Vol 9, 235-241, Copyright © 1999 by Oxford University Press


ORIGINAL ARTICLES

Control of metastasis by Asn-linked, beta1-6 branched oligosaccharides in mouse mammary cancer cells

PJ Seberger and WG Chaney
Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, NE 68198-4525, USA.

Studies in cell lines and malignant human tissues have shown that increased cell-surface Asn-linked beta1-6(GlcNAcbeta1-6Man) branching is associated with increased tumorigenic and metastatic properties. In this study, three mouse mammary cancer cell lines were transfected with an expression vector containing the mouse cDNA for N- acetylglucosaminyltransferase V (GlcNAcT-V EC 2.4.1.155), the glycosyltransferase responsible for initiating beta1-6 branching on Asn- linked carbohydrates. The cell lines were screened for increased cytotoxicity to L-PHA, a lectin specific for beta1-6 branching structures. Cell lines exhibiting increased L-PHA cytotoxicity expressed increased levels of beta1-6 branching structures. Northern blots detected the presence of GlcNAcT-V transcribed from the expression vector in the L-PHA sensitive cell lines. After injection into the tail veins of mice, transfected cell lines with increased beta1-6 branching on the cell surface formed elevated levels of lung tumors relative to control transfected cell lines (P < 0.002). Western blots of membrane proteins from GlcNAcT-V transfected and control cells probed with the lectins DSA and WGA did not show an increase in polyN- acetyllactosamine and sialic acid content in the transfected cell lines. These results demonstrate that a specific increase in beta1-6 branching due to an elevation in GlcNAcT-V expression increases metastatic potential.
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
Y. Zhao, T. Nakagawa, S. Itoh, K.-i. Inamori, T. Isaji, Y. Kariya, A. Kondo, E. Miyoshi, K. Miyazaki, N. Kawasaki, et al.
N-Acetylglucosaminyltransferase III Antagonizes the Effect of N-Acetylglucosaminyltransferase V on {alpha}3beta1 Integrin-mediated Cell Migration
J. Biol. Chem., October 27, 2006; 281(43): 32122 - 32130.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
H.-B. Guo, I. Lee, M. Kamar, and M. Pierce
N-Acetylglucosaminyltransferase V Expression Levels Regulate Cadherin-associated Homotypic Cell-Cell Adhesion and Intracellular Signaling Pathways
J. Biol. Chem., December 26, 2003; 278(52): 52412 - 52424.
[Abstract] [Full Text] [PDF]


Home page
Cancer Res.Home page
H.-B. Guo, I. Lee, M. Kamar, S. K. Akiyama, and M. Pierce
Aberrant N-Glycosylation of {beta}1 Integrin Causes Reduced {alpha}5{beta}1 Integrin Clustering and Stimulates Cell Migration
Cancer Res., December 1, 2002; 62(23): 6837 - 6845.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
S. Ihara, E. Miyoshi, J. H. Ko, K. Murata, S. Nakahara, K. Honke, R. B. Dickson, C.-Y. Lin, and N. Taniguchi
Prometastatic Effect of N-Acetylglucosaminyltransferase V Is Due to Modification and Stabilization of Active Matriptase by Adding beta 1-6 GlcNAc Branching
J. Biol. Chem., May 3, 2002; 277(19): 16960 - 16967.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. A. Skinner and A. G. Wildeman
Suppression of Tumor-related Glycosylation of Cell Surface Receptors by the 16-kDa Membrane Subunit of Vacuolar H+-ATPase
J. Biol. Chem., December 14, 2001; 276(51): 48451 - 48457.
[Abstract] [Full Text] [PDF]


Home page
Clin. Cancer Res.Home page
K. Murata, E. Miyoshi, M. Kameyama, O. Ishikawa, T. Kabuto, Y. Sasaki, M. Hiratsuka, H. Ohigashi, S. Ishiguro, S. Ito, et al.
Expression of N-Acetylglucosaminyltransferase V in Colorectal Cancer Correlates with Metastasis and Poor Prognosis
Clin. Cancer Res., May 1, 2000; 6(5): 1772 - 1777.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
K. Sasai, Y. Ikeda, T. Tsuda, H. Ihara, H. Korekane, K. Shiota, and N. Taniguchi
The Critical Role of the Stem Region as a Functional Domain Responsible for the Oligomerization and Golgi Localization of N-Acetylglucosaminyltransferase V. THE INVOLVEMENT OF A DOMAIN HOMOPHILIC INTERACTION
J. Biol. Chem., January 5, 2001; 276(1): 759 - 765.
[Abstract] [Full Text] [PDF]



Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.