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 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.

Novel polymorphisms and haplotypes in the human coagulation factor XIII A-subunit gene

1996 ◽  
Vol 98 (4) ◽  
pp. 393-395 ◽  
Author(s):  
K. Suzuki ◽  
Jürgen Henke ◽  
Misa Iwata ◽  
Lotte Henke ◽  
Hiroko Tsuji ◽  
...  
Keyword(s):  
Factor Xiii ◽  
Coagulation Factor ◽  
Subunit Gene ◽  
Coagulation Factor Xiii ◽  
A Subunit ◽  
Human Coagulation Factor Xiii

Expression of Functional Coagulation Factor XIII in Escherichia coli

1990 ◽  
Vol 63 (02) ◽  
pp. 235-240 ◽  
Author(s):  
P G Board ◽  
K Pierce ◽  
M Coggan
Keyword(s):  
Escherichia Coli ◽  
Factor Xiii ◽  
Blood Clotting ◽  
Coagulation Factor ◽  
E Coli ◽  
Thrombin Cleavage ◽  
Coagulation Factor Xiii ◽  
Clotting Cascade ◽  
Tac Promoter ◽  
A Subunit

SummaryCoagulation factor XIII is a zymogen that can be activated by thrombin cleavage to a transglutaminase that catalyses the formation of covalent crosslinks between fibrin chains in the final stages of the blood clotting cascade. Although circulating factor-XIII is composed of A and B subunits the catalytic activity is a property of the A subunits. In this study we have constructed a plasmid (pKKF13A) that contains a cDNA encoding the A subunit positioned downstream of a tac promoter. Escherichia coli containing this plasmid produce A subunit protein when grown in the presence of IPTG. The cloned A subunit has been partially purified and characterized. Comparison with A subunits purified from plasma showed that the cloned A subunits were of the same size, assembled as dimers, and had the same native electrophoretic mobility. The cloned A subunits expressed transglutaminase activity with putrescine, dansylcadaverine and casein as substrates, and were able to crosslink fibrin in clots formed from A subunit deficient plasma. These studies have demonstrated that functional recombinant factor XIII A subunit can be produced in E. coli and suggest that recombinant factor XIII can potentially provide a safe and inexhaustible supply for therapeutic use.

scholarly journals Impaired dimer assembly and decreased stability of naturally recurring R260C mutant A subunit for coagulation factor XIII

2012 ◽  
Vol 152 (5) ◽  
pp. 471-478 ◽  
Author(s):  
S. Maeda ◽  
W. G. Zhang ◽  
M. Souri ◽  
V. C. Yee ◽  
A. Ichinose
Keyword(s):  
Factor Xiii ◽  
Coagulation Factor ◽  
Coagulation Factor Xiii ◽  
A Subunit

scholarly journals Deficiency in the A-subunit of coagulation factor XIII: two novel point mutations demonstrate different effects on transcript levels

Blood ◽  
1994 ◽  
Vol 84 (2) ◽  
pp. 517-525 ◽  
Author(s):  
H Mikkola ◽  
M Syrjala ◽  
V Rasi ◽  
E Vahtera ◽  
E Hamalainen ◽  
...  
Keyword(s):  
Factor Xiii ◽  
Solid Phase ◽  
Stop Codon ◽  
Point Mutations ◽  
Premature Stop Codon ◽  
Coagulation Factor ◽  
Mrna Levels ◽  
Coagulation Factor Xiii ◽  
Stop Mutation ◽  
A Subunit

Abstract Congenital deficiency in coagulation factor XIII is a rare autosomal recessive bleeding disorder. Although the defect was characterized over 30 years ago, little is known about the molecular basis of the disorder. Here, we show two novel point mutations in the gene of the A- subunit of factor XIII in the genetically isolated population of Finland. All eight factor XIII-deficient families identified in Finland were studied. The exons of the gene of A-subunit were amplified individually by polymerase chain reaction and subsequently screened by single-strand conformation polymorphism. Sequence analysis of the abnormally migrating fragments showed two point mutations resulting in an amino acid alteration. A C-to-T transition at Arg-661 in exon XIV created a premature stop codon. This mutation was detected in six of the eight families, thus being the major alteration causing FXIII deficiency in Finland. In two of the six families, the patients were compound heterozygotes with the Arg-661-Stop mutation in one allele and either a T-to-C point mutation in exon VI or a thus far uncharacterized mutation in the other allele. The T-to-C transition in exon VI resulted in a substitution of threonine for methionine 242. The transition was found in one family only, where it was in the heterozygote form combined with the Arg-661-Stop mutation. To evaluate the consequences of these mutations, steady-state FXIII mRNA levels were quantitated by solid-phase minisequencing. In addition to the termination of translation 70 amino acids before the initial stop codon, the Arg-661- Stop mutation causes a 10- to 30-fold reduction in FXIII mRNA levels. This is also likely to result in a low translation level in the truncated polypeptide. In contrast, Met-242-Thr mutation does not seem to affect the level of mRNA. Here, the absence of a functional and immunodetectable protein is probably caused by an altered conformation of the mutant polypeptide, resulting in early degradation of the defective protein.

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