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[Cancer Research 62, 1944-1947, April 1, 2002]
© 2002 American Association for Cancer Research

Advances in Brief

Endostatin Regulates Endothelial Cell Adhesion and Cytoskeletal Organization1

Johan Dixelius, Michael Cross, Taro Matsumoto, Takako Sasaki, Rupert Timpl and Lena Claesson-Welsh2

Department of Genetics and Pathology, Uppsala University, Rudbeck Laboratory, 751 85 Uppsala, Sweden [J. D., M. C., T. M., L. C-W.], and Max-Planck-Institute, Department of Protein Chemistry, Martinsried an München, D-82152 Germany [T. S., R. T.]

Endostatin, an endogenous angiogenesis inhibitor, attenuates endothelial cell migration through an unknown mechanism. We show that endostatin induced tyrosine phosphorylation of focal adhesion kinase and paxillin, and promoted formation of focal adhesions and actin stress fibers, similar to fibroblast growth factor-2 (FGF-2). In cells cotreated with endostatin and FGF-2, focal adhesions and actin stress fibers were decreased, indicating that endostatin disturbs cell-matrix adhesion. Reduced tyrosine phosphorylation and cytoplasmic relocalization of ß-catenin in cells treated with FGF-2 and endostatin indicates that loosening of cell-cell adhesion is also disturbed by endostatin. These data provide a molecular basis both for the lack of effect of endostatin on the normal, quiescent vasculature, and its antagonistic effects on stimulated tumor vessels.




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Copyright © 2002 by the American Association for Cancer Research.