Thromb Haemost 2003; 89(06): 1089-1097
DOI: 10.1055/s-0037-1613412
Cellular Proteolysis and Oncology
Schattauer GmbH

Fibrinogen mediates bladder cancer cell migration in an ICAM-1-dependent pathway

Yann Roche
1   Unité INSERM 578, Institut Albert Bonniot, Grenoble, France
,
Dominique Pasquier
1   Unité INSERM 578, Institut Albert Bonniot, Grenoble, France
,
Jean-Jacques Rambeaud
1   Unité INSERM 578, Institut Albert Bonniot, Grenoble, France
,
Daniel Seigneurin
1   Unité INSERM 578, Institut Albert Bonniot, Grenoble, France
,
Alain Duperray
1   Unité INSERM 578, Institut Albert Bonniot, Grenoble, France
› Author Affiliations
Financial support: This work was supported by the Association pour la Recherche sur le Cancer and ARECA Grenoble.
Further Information

Publication History

Received 25 October 2002

Accepted after revision 24 March 2003

Publication Date:
08 December 2017 (online)

Summary

Fibrinogen (fg), present in tumor matrices, has been demonstrated to be determinant in metastatic potential. We have recently shown that fg/ICAM-1 interactions are involved in leukocyte migration across endothelial cell monolayers. Using bladder transitional cell carcinoma as a model, we will show in this study that bladder high grade tumor cell lines express ICAM-1, and that this expression induces an fg-mediated migration. This phenomenon was dependent on ICAM-1/fg interaction as well as RhoA activity. ICAM-1 was concentrated in focal adhesion plaques when tumor cells were allowed to adhere on immobilized fg, suggesting a role in cell migration. The addition of fg induced a 3- to 6-fold enhancement of bladder tumor cell migration through HUVEC monolayers. This process was inhibited by an anti-ICAM-1 antibody blocking fg binding, demonstrating that ICAM-1/fg interaction was involved in the extravasation process. Finally, immunohistological studies revealed that the expression of ICAM-1 was closely associated with an infiltrative histological phenotype.

Part of this paper was originally presented as part of the joint meetings of the 16th International Congress of the International Society of Fibrinolysis and Proteolysis (ISFP) and the 17th International Fibrinogen Workshop of the International Fibrinogen Research Society (IFRS) held in Munich, Germany, September, 2002.

 
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