ADP-ribosylation of Rho enhances adhesion of U937 cells to fibronectin via the alpha 5 beta 1 integrin receptor

FEBS Letters
M Aepfelbacher

Abstract

To examine the role of Rho GTP binding proteins in the adhesion of monocytic cells to fibronectin we used the C3 exoenzyme of Clostridium botulinum which ADP-ribosylates and inactivates Rho proteins in situ. Treatment of human monocytic U937 cells with C3 exoenzyme (10 micrograms/ml, 24 h) increased adhesion to fibronectin 2-fold but had no effect on adhesion to collagen or huamn serum albumin. The increase in fibronectin adhesion was prevented by antibodies against the alpha 5 and beta 1 integrin subunits, but surface expression of beta 1 and alpha 5 was not altered. These results suggest that Rho proteins regulate the interaction of the monocyte alpha 5 beta 1 integrin receptor with fibronectin by post receptor mechanisms.

References

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Citations

Jun 9, 2001·Biochemical and Biophysical Research Communications·Y FurukawaY Nakamura
Feb 6, 1998·Biochimie·B Z Katz, K M Yamada
Feb 1, 1997·Current Opinion in Cell Biology·K M Yamada, B Geiger
Sep 16, 2003·Molecular and Cellular Biology·Violaine MoreauElisabeth Génot
Jan 1, 1996·Annual Review of Cell and Developmental Biology·K Burridge, M Chrzanowska-Wodnicka
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Aug 1, 1996·Trends in Cell Biology·L M Machesky, A Hall

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