Coagulation factor XIII activation peptide and subunit levels in patients with acute ischaemic stroke: A pilot study

2010 ◽  
Vol 126 (2) ◽  
pp. e122-e127 ◽  
Author(s):  
Verena Schroeder ◽  
Elisabeth Ortner ◽  
Marie-Luise Mono ◽  
Aekaterini Galimanis ◽  
Niklaus Meier ◽  
...  
Keyword(s):  
Pilot Study ◽  
Ischaemic Stroke ◽  
Acute Ischaemic Stroke ◽  
Factor Xiii ◽  
Coagulation Factor ◽  
Coagulation Factor Xiii ◽  
Activation Peptide

Coagulation factor XIII B subunit antigen, FXIIIVal34Leu genotype and ischaemic stroke in South Asians

2005 ◽  
Vol 93 (02) ◽  
pp. 394-395 ◽  
Author(s):  
John Young ◽  
John Bavington ◽  
John Bamford ◽  
Andrew Catto ◽  
Kirti Kain
Keyword(s):  
Ischaemic Stroke ◽  
Factor Xiii ◽  
South Asians ◽  
Coagulation Factor ◽  
B Subunit ◽  
Coagulation Factor Xiii

The Val34Leu Polymorphism in the A Subunit of Coagulation Factor XIII Contributes to the Large Normal Range in Activity and Demonstrates That the Activation Peptide Plays a Role in Catalytic Activity

Blood ◽  
1998 ◽  
Vol 92 (8) ◽  
pp. 2766-2770 ◽  
Author(s):  
S. Kangsadalampai ◽  
P.G. Board
Keyword(s):  
Factor Xiii ◽  
Direct Evidence ◽  
Coagulation Factor ◽  
Normal Range ◽  
Thrombin Cleavage ◽  
Coagulation Factor Xiii ◽  
A Subunit ◽  
Elevated Activity ◽  
Activation Peptide ◽  
American Society

There is a wide normal range of coagulation factor XIII activity that has never been adequately explained. A polymorphism substituting leucine for valine at position 34 in the activation peptide of the A subunit of factor XIII has recently been discovered in nondeficient individuals, and the present studies indicate that the leucine substitution results in a significant increase in transglutaminase activity. The frequency of the Leu34 allele in the Australian Caucasian population is 0.27, which is high enough to suggest that the inheritance of either the Val34 or Leu34 alleles may contribute to the wide normal range of activity. Although there has been structural evidence indicating that the activation peptide does not dissociate from the enzyme after thrombin cleavage, the discovery of elevated activity resulting from the Leu34 substitution is the first direct evidence that the activation peptide plays a continuing role in the function of factor XIII. © 1998 by The American Society of Hematology.

Coagulation factor XIII polymorphisms and the risk of myocardial infarction and ischaemic stroke in young women

2002 ◽  
Vol 116 (2) ◽  
pp. 376-382 ◽  
Author(s):  
Alexander P. Reiner ◽  
Michele B. Frank ◽  
Stephen M. Schwartz ◽  
Michael L. Linenberger ◽  
W. T. Longstreth ◽  
...  
Keyword(s):  
Myocardial Infarction ◽  
Ischaemic Stroke ◽  
Young Women ◽  
Factor Xiii ◽  
Coagulation Factor ◽  
Coagulation Factor Xiii ◽  
Stroke In Young

The Val34Leu Polymorphism in the A Subunit of Coagulation Factor XIII Contributes to the Large Normal Range in Activity and Demonstrates That the Activation Peptide Plays a Role in Catalytic Activity

Blood ◽  
1998 ◽  
Vol 92 (8) ◽  
pp. 2766-2770 ◽  
Author(s):  
S. Kangsadalampai ◽  
P.G. Board
Keyword(s):  
Factor Xiii ◽  
Direct Evidence ◽  
Coagulation Factor ◽  
Normal Range ◽  
Thrombin Cleavage ◽  
Coagulation Factor Xiii ◽  
A Subunit ◽  
Elevated Activity ◽  
Activation Peptide ◽  
American Society

Abstract There is a wide normal range of coagulation factor XIII activity that has never been adequately explained. A polymorphism substituting leucine for valine at position 34 in the activation peptide of the A subunit of factor XIII has recently been discovered in nondeficient individuals, and the present studies indicate that the leucine substitution results in a significant increase in transglutaminase activity. The frequency of the Leu34 allele in the Australian Caucasian population is 0.27, which is high enough to suggest that the inheritance of either the Val34 or Leu34 alleles may contribute to the wide normal range of activity. Although there has been structural evidence indicating that the activation peptide does not dissociate from the enzyme after thrombin cleavage, the discovery of elevated activity resulting from the Leu34 substitution is the first direct evidence that the activation peptide plays a continuing role in the function of factor XIII. © 1998 by The American Society of Hematology.

scholarly journals Activation peptide of the coagulation factor XIII (AP-F13A1) as a new biomarker for the screening of colorectal cancer

2018 ◽  
Vol 15 (1) ◽  
Author(s):  
Julien Peltier ◽  
Jean-Pierre Roperch ◽  
Stéphane Audebert ◽  
Jean-Paul Borg ◽  
Luc Camoin
Keyword(s):  
Colorectal Cancer ◽  
Factor Xiii ◽  
Coagulation Factor ◽  
Coagulation Factor Xiii ◽  
Activation Peptide

Coagulation factor XIII variants with altered thrombin activation rates

2009 ◽  
Vol 390 (12) ◽  
Author(s):  
Mette Dahl Andersen ◽  
Marianne Kjalke ◽  
Susanne Bang ◽  
Inger Lautrup-Larsen ◽  
Peter Becker ◽  
...  
Keyword(s):  
Factor Xiii ◽  
Coagulation Factor ◽  
Thrombin Cleavage ◽  
Coagulation Factor Xiii ◽  
Activation Rate ◽  
Fibrin Network ◽  
Thrombin Activation ◽  
Activation Peptide ◽  
Activation Rates ◽  
Fibrin Monomers

Abstract Coagulation factor XIII (FXIII) is activated by thrombin and catalyses crosslinking between fibrin monomers thereby providing mechanical strength to the fibrin network. V34L is a common FXIII-A polymorphism found in the activation peptide. FXIII-A V34L is activated faster by thrombin and provides formation of a tighter clot at fibrinogen concentrations in the low end of the physiological range. FXIII-A variants with potentially increased activation rates were generated. Introduction of an optimal thrombin cleavage site, V34L+V35T, increased the activation rate 7.6-fold and facilitated the formation of a fibrin network more resistant to fibrinolysis than obtained with wt FXIII-A. In contrast, introduction of fragments of fibrinopeptide A into the activation peptide resulted in severely impaired activation rates.

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