|
|
 Previous Article | Table of Contents | Next Article 
Covalent crosslinking of von Willebrand factor to fibrin
M Hada, M Kaminski, P Bockenstedt and J McDonagh
Factor XIIIa crosslinks a limited number of substrates via
epsilon(gamma-glutamyl)-lysyl bond formation. It crosslinks fibrin to
itself, alpha 2-plasmin inhibitor and fibronectin to fibrin, and
fibronectin to collagen. Results presented here show that plasma von
Willebrand factor (vWF) is a substrate for factor XIIIa and can be
crosslinked to fibrin during gel formation. vWF-fibrin crosslinking was
studied in purified systems and in plasma with 125I-vWF and 131I-
fibrinogen. vWF incorporation into fibrin increased with time or increasing
factor XIIIa. After electrophoresis of dissolved clots, distribution of
125I and 131I was measured and showed that vWF was crosslinked to the alpha
chain of fibrin and entered the high-mol-wt alpha polymer. vWF-fibrin
crosslinking decreased the initial rate of alpha polymer formation.
Crosslinking of vWF polymer to itself could not be demonstrated under
physiologic conditions but occurred if vWF was reduced first. Factor XIIIa
catalyzed incorporation of putrescine into both monomeric and polymeric
vWF. Altogether, these studies indicate that factor XIIIa can readily form
covalent bonds between glutamine in vWF and lysine in fibrin alpha chains.
This reaction occurs readily in vitro when plasma clotting is slow and may
occur in vivo under similar conditions.
Volume 68,
Issue 1,
pp. 95-101,
07/01/1986
Copyright © 1986 by The American Society of Hematology
 CiteULike  Connotea  Del.icio.us  Digg  Reddit  Technorati What's this?
This article has been cited by other articles:
|
|
|
|
 
J. F. W. Keuren, D. Baruch, P. Legendre, C. V. Denis, P. J. Lenting, J.-P. Girma, and T. Lindhout
Von Willebrand factor C1C2 domain is involved in platelet adhesion to polymerized fibrin at high shear rate
Blood,
March 1, 2004;
103(5):
1741 - 1746.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
R. A. S. Ariens, T.-S. Lai, J. W. Weisel, C. S. Greenberg, and P. J. Grant
Role of factor XIII in fibrin clot formation and effects of genetic polymorphisms
Blood,
July 18, 2002;
100(3):
743 - 754.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
K. F. Standeven, R. A.S. Ariens, P. Whitaker, A. E. Ashcroft, J. W. Weisel, and P. J. Grant
The Effect of Dimethylbiguanide on Thrombin Activity, FXIII Activation, Fibrin Polymerization, and Fibrin Clot Formation
Diabetes,
January 1, 2002;
51(1):
189 - 197.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
R. A. S. Ariens, H. Philippou, C. Nagaswami, J. W. Weisel, D. A. Lane, and P. J. Grant
The factor XIII V34L polymorphism accelerates thrombin activation of factor XIII and affects cross-linked fibrin structure
Blood,
August 1, 2000;
96(3):
988 - 995.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
R. A. S. Ariens, H. P. Kohler, M. W. Mansfield, and P. J. Grant
Subunit Antigen and Activity Levels of Blood Coagulation Factor XIII in Healthy Individuals : Relation to Sex, Age, Smoking, and Hypertension
Arterioscler Thromb Vasc Biol,
August 1, 1999;
19(8):
2012 - 2016.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
Z. Valnickova and J. J. Enghild
Human Procarboxypeptidase U, or Thrombin-activable Fibrinolysis Inhibitor, Is a Substrate for Transglutaminases. EVIDENCE FOR TRANSGLUTAMINASE-CATALYZED CROSS-LINKING TO FIBRIN
J. Biol. Chem.,
October 16, 1998;
273(42):
27220 - 27224.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
