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J Biol Chem, Vol. 275, Issue 20, 15321-15329, May 19, 2000
From the Tumor-derived adhesion factor/angiomodulin (AGM)
is accumulated in tumor blood vessels and on the endothelial cell
surface (Akaogi, K., Okabe, Y., Sato, J., Nagashima, Y., Yasumitsu, H., Sugahara, K., and Miyazaki, K. (1996) Proc. Natl. Acad. Sci.
U. S. A. 93, 8384-8389). In cell culture, it promotes cell
adhesion and morphological changes to form cord-like structures of the human bladder carcinoma cell line ECV-304. The cord formation is
prevented by heparin, which inhibits the binding of AGM to ECV-304
cells. This observation suggests that AGM interacts with cell surface
heparan sulfate (HS) proteoglycans. In this study, HS
glycosaminoglycans and core proteins of integral transmembrane proteoglycans, syndecan-1 and -4, were identified by
immunocytochemistry on ECV-304 cells, and the structural requirements
for the interaction of HS with AGM were characterized. Inhibition
experiments with sulfated polysaccharides and chemically modified
heparin derivatives indicated that sulfate groups were essential for
both AGM-HS binding and cord-like structure formation and that the rank
order of the different sulfate groups in terms of their contribution
was N-sulfate > 6-O-sulfate > 2-O-sulfate. The minimum size of heparin, a chemical analog
of HS, required for the binding to AGM was a dodecasaccharide as
determined by competition experiments using size-defined heparin oligosaccharides. Thus, a specific sulfation pattern in the HS of cell
surface syndecans of ECV-304 cells is required for AGM binding and the
morphological changes.
Structural Requirements of Heparan Sulfate for the Binding to the
Tumor-derived Adhesion Factor/Angiomodulin That Induces Cord-like
Structures to ECV-304 Human Carcinoma Cells*
,,,¶
Department of Biochemistry, Kobe
Pharmaceutical University, Higashinada-ku, Kobe 658-8558 and the
§ Division of Cell Biology, Kihara Institute for Biological
Research, Yokohama City University, Yokohama 244-0813, Japan
*
This work was supported in part by the Research Foundation
for Pharmaceutical Sciences (Japan) (to S. Y.), the Science
Research Promotion Fund from Japan Private School Promotion Foundation, a grant from Hyogo Science and Technology Association (to K. S.), and Grants-in-Aid for Encouragement of Young Scientists 11771474 (to
S. Y.), Scientific Research (B) 09470509 (to K. S.), and
Scientific Research on Priority Areas 10178102 (to K. S.) from the
Ministry of Education, Science, Culture, and Sports of Japan.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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