Coagulation factor XIII serves as protein disulfide isomerase

2009 ◽  
Vol 101 (05) ◽  
pp. 840-844 ◽  
Author(s):  
Zsuzsa Bagoly ◽  
Vera Sheptovitsky ◽  
Rima Dardik ◽  
Judith Lahav ◽  
Eli Karniel ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Protein Disulfide Isomerase ◽  
Factor Xiii ◽  
Tissue Transglutaminase ◽  
Coagulation Factor ◽  
Disulfide Isomerase ◽  
Coagulation Factor Xiii ◽  
A Subunit ◽  
Bond Rearrangement ◽  
Protein Disulfide

SummaryTissue transglutaminase was reported to act as protein disulfide isomerase (PDI). We studied whether plasma transglutaminase – coagulation factor XIII (FXIII) – has PDI activity as well. PDI activity was measured by determining the ability to renature reduced-denatured RNase (rdRNase). We found that FXIII can re-nature rdRNase, with efficiency comparable to commercial PDI. This PDI activity was inhibited by bacitracin. Like tissue transglu-taminase, FXIII-mediated PDI activity is independent of its transglutaminase activity and is located on the A subunit. Surface-associated PDI has been previously shown to catalyse two distinct functions: transnitrosation with subsequent release of intracellular nitric oxide and disulfide bond rearrangement during platelet integrin ligation. Our results imply that FXIII-PDI activity may have a role in platelet function.

The gene for coagulation factor XIII a subunit (F13A) is distal to HLA on chromosome 6

1984 ◽  
Vol 67 (4) ◽  
pp. 406-408 ◽  
Author(s):  
P. G. Board ◽  
M. Reid ◽  
S. Serjeantson
Keyword(s):  
Factor Xiii ◽  
Coagulation Factor ◽  
Chromosome 6 ◽  
Coagulation Factor Xiii ◽  
A Subunit

scholarly journals Factor XIII improves platelet adhesion to fibrinogen by protein disulfide isomerase-mediated activity

2013 ◽  
Vol 131 (4) ◽  
pp. 338-341 ◽  
Author(s):  
Judith Lahav ◽  
Ariella Tvito ◽  
Zsuzsa Bagoly ◽  
Rima Dardik ◽  
Aida Inbal
Keyword(s):  
Protein Disulfide Isomerase ◽  
Factor Xiii ◽  
Platelet Adhesion ◽  
Disulfide Isomerase ◽  
Protein Disulfide

scholarly journals Identification of Potential Novel Interacting Partners for Coagulation Factor XIII B (FXIII-B) Subunit, a Protein Associated with a Rare Bleeding Disorder

2019 ◽  
Vol 20 (11) ◽  
pp. 2682 ◽  
Author(s):  
Sneha Singh ◽  
Mohammad Suhail Akhter ◽  
Johannes Dodt ◽  
Peter Volkers ◽  
Andreas Reuter ◽  
...  
Keyword(s):  
Factor Xiii ◽  
Regulatory Protein ◽  
Coagulation Factor ◽  
Factor H ◽  
Complement C3 ◽  
Complement Factor ◽  
B Subunit ◽  
Coagulation Factor Xiii ◽  
A Subunit ◽  
Complement C1q

Coagulation factor XIII (FXIII) is a plasma-circulating heterotetrameric pro-transglutaminase complex that is composed of two catalytic FXIII-A and two protective/regulatory FXIII-B subunits. FXIII acts by forming covalent cross-links within a preformed fibrin clots to prevent its premature fibrinolysis. The FXIII-A subunit is known to have pleiotropic roles outside coagulation, but the FXIII-B subunit is a relatively unexplored entity, both structurally as well as functionally. Its discovered roles so far are limited to that of the carrier/regulatory protein of its partner FXIII-A subunit. In the present study, we have explored the co-presence of protein excipients in commercial FXIII plasma concentrate FibrogamminP by combination of protein purification and mass spectrometry-based verification. Complement factor H was one of the co-excipients observed in this analysis. This was followed by performing pull down assays from plasma in order to detect the putative novel interacting partners for the FXIII-B subunit. Complement system proteins, like complement C3 and complement C1q, were amongst the proteins that were pulled down. The only protein that was observed in both experimental set ups was alpha-2-macroglobulin, which might therefore be a putative interacting partner of the FXIII/FXIII-B subunit. Future functional investigations will be needed to understand the physiological significance of this association.

Spontaneous regression of the inhibitor against the coagulation factor XIII A subunit in acquired factor XIII deficiency

2010 ◽  
Vol 104 (12) ◽  
pp. 1284-1285 ◽  
Author(s):  
Kentaro Okubo ◽  
Toshiro Ito ◽  
Nobuo Okumura ◽  
Masayoshi Souri ◽  
Akitada Ichinose ◽  
...  
Keyword(s):  
Factor Xiii ◽  
Spontaneous Regression ◽  
Coagulation Factor ◽  
Factor Xiii Deficiency ◽  
Coagulation Factor Xiii ◽  
A Subunit

Alternative method of subtyping the A subunit of coagulation factor XIII (FXIIIA)

1997 ◽  
Vol 18 (5) ◽  
pp. 790-791
Author(s):  
Akira Kido ◽  
Masakazu Oya ◽  
Zeming Jin
Keyword(s):  
Factor Xiii ◽  
Coagulation Factor ◽  
Coagulation Factor Xiii ◽  
Alternative Method ◽  
A Subunit

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.

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