Author's reply to Weijers et al. 'Fibrin beta(15-42) domain is cryptic in intact fibrinogen: comment on the study by A. Sahni et al.'.

摘要

We thank Drs. Weijers, Koolwijk, van Hinsbergh and van Nieuw Amerongen for their interest in our recent publication, "The VE-cadherin binding domain of fibrinogen induces endothelial barrier permeability and enhances transendo-thelial migration of malignant breast epithelial cells" that appeared in the August 1st issue of the International Journal of Cancer in 2009.1 Moreover, we appreciate the concerns raised by Weijers et al.2 that the effects we observed on endothelial permeability and malignant breast epithelial cell trans-endothelial cell migration were due to thrombin/proteolytic conversion of the exogenously added fibrinogen to fibrin monomer and/or fibrin(ogen) degradation products and not due to the exposure of the cryptic vascular endothelial (VE)-cadherin binding domain located at residues 15-42 on the fS chain of intact fibrinogen. Although a role for VE-cadherin in regulating endothelial cell permeability is well established,3 a role for intact fibrinogen in the absence of its conversion to fibrin and/or fibrin(ogen) degradation products to promote endothelial cell permeability would be unexpected.