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Thromb Haemost 2001; 85(03): 544-551
DOI: 10.1055/s-0037-1615619
Review Article
Schattauer GmbH

Factor XI Assembly and Activation on Human Umbilical Vein Endothelial Cells in Culture

Zia Shariat-Madar
1   Division of Hematology and Oncology, Department of Internal Medicine and Pathology
,
Fakhri Mahdi
1   Division of Hematology and Oncology, Department of Internal Medicine and Pathology
,
Alvin Schmaier
1   Division of Hematology and Oncology, Department of Internal Medicine and Pathology
2   University of Michigan, Ann Arbor, MI, USA
› Author Affiliations
Further Information

Publication History

Received 26 May 2000

Accepted after resubmission 28 September 2000

Publication Date:
08 December 2017 (online)

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Summary

Biotin-FXI optimally bound to HUVEC in the presence of 40 nM high molecular weight kininogen (HK) and ≥ ≥7 μM Zn2+. There was little specific FXI binding in the absence of added HK and at concentrations of Zn2+ <15 μM. FXI and prekallikrein, but not prothrombin, blocked biotin-FXI binding to HUVEC in the presence of HK with an IC50 of 18 nM and 180 nM, respectively. Monoclonal antibody HKL16 and peptide SDD31 also inhibited biotin-XI binding in the presence of HK with an IC50 of 4.7 nM and 50 μM, respectively. Alternatively, peptide T249-F260 of FXI’s apple domain 3 and heparin monosulfate were weak inhibitors of FXI binding to HUVEC. FXI bound to HUVEC with an apparent K d of 6.9 ± 3.0 nM and B max of 13 ± 2.6106 sites/cell. FXI bound to HK on HUVEC, but not prothrombin, became converted to FXIa. FXI activation on HUVEC resulted from tissue culture media bovine factor XIIa. HUVEC grown in human factor XII-deficient serum did not support FXI activation. FXI binding to HUVEC in culture was mostly mediated by HK and FXI activation on HUVEC is dependent on cell-associated factor XIIa.

Keywords

Factor XI - high molecular weight kininogen - factor XII - prekallikrein - prothrombin
 

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