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Vascular endothelial cells that express dystroglycan are involved in angiogenesis

¹ Center for Cardiovascular Research, University of Rochester School of Medicine and Dentistry, Rochester NY 14642-8679, USA
² Department of Neurobiology, Tottori University Faculty of Medicine, Yonago 683, Japan
³ Department of Pathology, Tottori University Faculty of Medicine, Yonago 683, Japan
⁴ National Cardiovascular Center Research Institute, Osaka 565, Japan

Author for correspondence (e-mail: Keigi_Fugiwara{at}urmc.rochester.edu )

Accepted 21 December 2001

We have earlier shown that dystroglycan (DG) is a lamininbinding protein and as such is a cell adhesion molecule. DG is a heterodimer of and ß DG subunits. ß-dystroglycan (ßDG) is the membrane spanning subunit, whereas the subunit is bound to the extracellular domain of ßDG. To study physiological function of the protein, we expressed full-length DG (FL-DG) and the cytoplasmic domain of ßDG (ßDG) in bovine aortic endothelial cells (BAE) and examined their effects on cell adhesion, migration, proliferation and tube formation. FL-DG enhanced adhesion of BAE to laminin-1, whereas ßDG inhibited it. Cell migration was inhibited by overexpressing ßDG in these cells, although it was not affected by FL-DG overexpression. In a proliferation assay, FL-DG decreased the growth rate, and it also caused cells to extensively spread. ßDG caused opposite effects; it increased the growth rate and reduced the cell surface area. In a tube formation assay on Matrigel, FL-DG caused an obvious inhibition, whereas ßDG accelerated tube formation. These results suggest a potential role of endothelial dystroglycan in the control of angiogenesis. Anti-ßDG immunohistochemistry indicated increased expression of DG in vascular endothelial cells within malignant tumors. By contrast, the antibody failed to stain endothelial cells in normal tissues. In cultured BAE, the level of ßDG was low in serum-deprived quiescent cells and was upregulated in proliferating cells. Our results suggest that the expression of DG in endothelial cells is under a dynamic regulation and may play a role in angiogenesis.

Key words: angiogenesis, dystroglycan, endothelium, laminin

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