Thromb Haemost 2007; 98(01): 105-108
DOI: 10.1160/TH07-04-0274
Anniversary Issue Contribution
Schattauer GmbH

Update on antithrombin I (fibrin)

Michael W. Mosesson
1   The Blood Research Institute, BloodCenter of Wisconsin, Milwaukee, Wisconsin, USA
› Author Affiliations
Further Information

Correspondence to:

Michael W. Mosesson
The Blood Research Institute
BloodCenter of Wisconsin
PO Box 2178, Milwaukee, WI 53201–2178, USA
Phone: +1 414 937 3811   
Fax: +1 414 937 6784   

Publication History

Received 13 April 2007

Accepted 11 May 2007

Publication Date:
29 November 2017 (online)

 

Summary

Antithrombin I (fibrin) is an important inhibitor of thrombin generation that functions by sequestering thrombin in the forming fibrin clot, and also by reducing the catalytic activity of fibrinbound thrombin. Thrombin binding to fibrin takes place at two classes of non-substrate sites: 1) in the fibrin E domain (two per molecule) through interaction with thrombin exosite 1; 2) at a single site on each γ’ chain through interaction with thrombin exosite 2. The latter reaction results in allosteric changes that down-regulate thrombin catalytic activity. Antithrombin I deficiency (afibrinogenemia), defective thrombin binding to fibrin (antithrombin I defect) found in certain dysfibrinogenemias (e.g. fibrinogen Naples 1), or a reduced plasma γ’ chain content (reduced antithrombin I activity), predispose to intravascular thrombosis.


 



Correspondence to:

Michael W. Mosesson
The Blood Research Institute
BloodCenter of Wisconsin
PO Box 2178, Milwaukee, WI 53201–2178, USA
Phone: +1 414 937 3811   
Fax: +1 414 937 6784