Skip Navigation



Glycobiology Advance Access published online on November 1, 2009
Glycobiology, doi:10.1093/glycob/cwp168
This Article
Right arrow Advance Access manuscript (PDF)
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 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 arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Wu, L. H.
Right arrow Articles by Wu, X. Z.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Wu, L. H.
Right arrow Articles by Wu, X. Z.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Author 2009. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Fucosylated glycan inhibition of human hepatocellular carcinoma cell migration through binding to chemokine receptors

Li Hui Wu1,2, Bi Zhi Shi1, Lei Qian Zhao2 and Xing Zhong Wu1,*

1 Department of Biochemistry, Shanghai Medical College, Fudan University, 138 Yi Xue Yuan Road, Shanghai 200032, P.R. China
2 Yuying Children's Hospital of Wenzhou Medical College, 109 Xueyuan Road, Wenzhou, Zhejiang, 325003, P.R. China

* Correspondence to Xing Zhong Wu, MD, PhD, Department of Biochemistry, Shanghai Medical College, Fudan University, 138 Yi Xue Yuan Road, Shanghai 200032, P.R. China, E-mail: xz_wu{at}shmu.edu.cn, Tel & Fax: 8621 54237697

Received on November 23, 2008; accepted on October 19, 2009

SMMC-7721 hepatocellular carcinoma cells (HCC) were incubated with fucosylated glycoproteins that had been isolated from retinoic acid-treated cells by affinity chromatography. HCC migration was significantly inhibited by AAL- and LCA-glycoproteins. Glycopeptides, obtained by digestion of the glycoproteins with trypsin and papain, were found to have a similar inhibitory effect on HCC migration as the corresponding glycoproteins. The inhibitory actions of the glycoproteins were almost abolished after digestion with {alpha}-L-1,3/4- or {alpha}-L-1,2-fucosidase. Induction of HCC migration with chemokines including interleukin-8 (IL-8), lymphotactin, monocyte chemoattractant protein-1, and stroma cell-derived factor-1 was examined and IL-8 was found to be the most potent. Interestingly, the isolated glycoproteins significantly inhibited HCC migration and F-actin aggregation induced by IL-8, whereas the glycans themselves did not induce F-actin assembly. From receptor binding analysis AAL-glycan was found to bind IL-8 receptors especially CXCR2 directly and such binding could be blocked by 3'- or 2'-fucosyllactose. After CXCR2 silence by target RNAi, the cells almost lost the response to AAL-glycan inhibition. Our findings suggest that fucosylation plays an important role in the interaction between IL-8 and its receptors inducing HCC migration.

Key words: fucosylation / cell migration / Interleukin 8


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




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.