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Blood, Vol. 95 No. 8 (April 15), 2000:
pp. 2586-2592
Factor XIIIa supports microvascular endothelial cell adhesion and
inhibits capillary tube formation in fibrin
Susan M. Dallabrida,
Lisa A. Falls, and
David H. Farrell
From the Department of Biochemistry and Molecular Biology,
Pennsylvania State University College of Medicine, Hershey, PA;
Children's Hospital, Harvard Medical School, and Center for
Hemostasis and Thrombosis Research, Beth Israel Deaconess Medical
Center and Harvard Medical School, Boston, MA; and Department of Oral
Molecular Biology, School of Dentistry, Oregon Health Sciences
University, Portland, OR.
Coagulation factor XIIIa is a transglutaminase that catalyzes
covalent cross-link formation in fibrin clots. In this report, we
demonstrate that factor XIIIa also mediates adhesion of endothelial cells and inhibits capillary tube formation in fibrin. The adhesive activity of factor XIIIa was not dependent on the transglutaminase activity, and did not involve the factor XIIIb-subunits. The adhesion was inhibited by 99% using a combination of monoclonal antibodies directed against integrin  v 3 and
1-containing integrins, and was dependent on
Mg2+ or Mn2+. Soluble factor XIIIa also
bound to endothelial cells in solution, as detected by flow cytometry.
In addition, factor XIIIa inhibited endothelial cell capillary tube
formation in fibrin in a dose-dependent manner. Furthermore, the extent
of inhibition differed in 2 types of fibrin. The addition of 10 to 100 µg/mL factor XIIIa produced a dose-dependent reduction in capillary
tube formation of 60% to 100% in  A/A fibrin, but only a 10% to
37% decrease in A/' fibrin. These results show that factor
XIIIa supports endothelial cell adhesion in an integrin-dependent
manner and inhibits capillary tube formation.
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