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.

Physical linkage of the human genes coding for complement factor H and coagulation factor XIII B subunit

Genomics ◽  
1990 ◽  
Vol 7 (4) ◽  
pp. 644-646 ◽  
Author(s):  
Javier Rey-Campos ◽  
Domingo Baeza-Sanz ◽  
Santiago Rodriguez de Cordoba
Keyword(s):  
Factor Xiii ◽  
Coagulation Factor ◽  
Factor H ◽  
Complement Factor H ◽  
Complement Factor ◽  
B Subunit ◽  
Coagulation Factor Xiii ◽  
Human Genes ◽  
Physical Linkage

scholarly journals The Structure of Blood Coagulation Factor XIII Is Adapted to Oxidation

Biomolecules ◽  
2020 ◽  
Vol 10 (6) ◽  
pp. 914
Author(s):  
Alexandra Vasilyeva ◽  
Lyubov Yurina ◽  
Alexander Shchegolikhin ◽  
Maria Indeykina ◽  
Anna Bugrova ◽  
...  
Keyword(s):  
Blood Coagulation ◽  
Factor Xiii ◽  
Critical Role ◽  
Coagulation Factor ◽  
Amino Acid Residues ◽  
B Subunit ◽  
Covalent Crosslinking ◽  
Coagulation Factor Xiii ◽  
A Subunit ◽  
Enzymatic Activation

The blood coagulation factor XIII (FXIII) plays a critical role in supporting coagulation and fibrinolysis due to both the covalent crosslinking of fibrin polymers, rendering them resistant to plasmin lysis, and the crosslinking of fibrin to proteins of the fibrinolytic system. The hypochlorite-mediated oxidation of the blood coagulation factor XIII (FXIII) at the different stages of its enzymatic activation is studied for the first time in this paper. The consolidated results obtained with the aid of MS/MS, electrophoresis, and colorimetry demonstrate that in the process of FXIII’s conversion into FXIIIa, the vulnerability of FXIII to hypochlorite-induced oxidation increased as follows: native FXIII < FXIII + Ca2+ << FXIII + Ca2+/thrombin. The modification sites were detected among all the structural regions of the catalytic FXIII-A subunit, except for the activation peptide, and embraced several sushi domains of the FXIII-B subunit. Oxidized amino acid residues belonging to FXIII-A are surface-exposed residues and can perform an antioxidant role. The regulatory FXIII-B subunits additionally contribute to the antioxidant defense of the catalytic center of the FXIII-A subunits. Taken together, the present data along with the data from previous studies demonstrate that the FXIII proenzyme structure is adapted to oxidation.

Exploring the structural similarity yet functional distinction between coagulation factor XIII-B and complement factor H sushi domains

2019 ◽  
Vol 48 (1) ◽  
pp. 95-102 ◽  
Author(s):  
Mohammad Suhail Akhter ◽  
Sneha Singh ◽  
Hamideh Yadegari ◽  
Vytautas Ivaskevicius ◽  
Johannes Oldenburg ◽  
...  
Keyword(s):  
Factor Xiii ◽  
Coagulation Factor ◽  
Structural Similarity ◽  
Factor H ◽  
Complement Factor H ◽  
Complement Factor ◽  
Coagulation Factor Xiii

Coagulation Factor XIII and Cardiovascular Disease in UK Asian Patients Undergoing Coronary Angiography

2001 ◽  
Vol 85 (03) ◽  
pp. 408-411 ◽  
Author(s):  
Michael Mansfield ◽  
Peter Grant ◽  
Darren Warner
Keyword(s):  
Insulin Resistance ◽  
Cardiovascular Disease ◽  
Coronary Angiography ◽  
Factor Xiii ◽  
Coagulation Factor ◽  
Asian Population ◽  
B Subunit ◽  
Asian Patients ◽  
Coagulation Factor Xiii ◽  
The Uk

SummaryPossession of the coagulation factor XIII Val34Leu (FXIIIVal34Leu) polymorphism is associated with protection against myocardial infarction (MI) in Caucasians, in the absence of features of insulin resistance. The role of this polymorphism in the UK Asian population, with its high prevalence of insulin resistance and ischaemic heart disease, is unknown. We investigated the frequency of genotypes at this polymorphism, and measures of circulating FXIII in a group of UK Asians attending for coronary angiography. Genotype at the FXIIIVal34Leu polymorphism was not associated with MI. FXIII B-subunit levels correlated with waist: hip ratio (r = 0.19, p 0.005), HbA1c (r = 0.18, p 0.05), fasting triglycerides (r = 0.21, p 0.005), total cholesterol (r = 0.29, p 0.0005) and PAI-1 antigen (r = 0.24, p 0.005). An association between FXIIIVal34Leu and FXIII cross-linking activity was confirmed in these subjects (one-way ANOVA p 0.0005). This evidence does not support the hypothesis that FXIIIVal34Leu is protective against MI in the UK Asian population. FXIII B-subunit levels are strongly linked to risk factors for cardiovascular disease, suggesting an underlying association with insulin resistance.

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

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

ISOLATION AND CHARACTERIZATION OF THE GENES FOR THE a AND b SUBUNITS OF HUMAN COAGULATION FACTOR XIII

1987 ◽  
Author(s):  
A Ichinose ◽  
R E Bottenus ◽  
K R Loeb ◽  
E W Davie
Keyword(s):  
Amino Acid ◽  
Factor Xiii ◽  
Coagulation Factor ◽  
Amino Acid Sequences ◽  
Binding Region ◽  
Recombinant Phage ◽  
B Subunit ◽  
Isolation And Characterization ◽  
A Subunit ◽  
B Subunits

Factor XIII (plasma transglutaminase, fibrin stabilizing factor) is a plasma protein that plays an important role in the final stages of blood coagulation and fibrinolysis. The molecule occurs in blood as a tetramer (a2b2) consisting of two a. subunits and two b subunits. Recently, we have determined the amino acid sequences for both the a. and b subunits of human factor XIII by a combination of cDNA cloning and amino acid sequence analysis. cDNAs coding for the a (3.8 Kb) and b (2.2 Kb) subunits were used for the screening of human genomic DNA libraries. Among 12 × 106 recombinant phage, ∼30 have been shown to contain the sequences for the a subunit and ∼10 have been shown to contain the gene for the b subunit of factor XIII. The clones coding for the a. subunit span ∼90 Kb and have been characterized by restriction mapping. Southern blotting, and DNA sequencing. Both 5’ and 3’ ends of the genomic clones correspond to the 5’ and 3’portions of the cDNA for the a.subunit of factor XIII. The DNA sequence revealed that the activation peptide released ^thrombin (amino acid residues 137), the first putative Ca2+ binding region (around residue 251), the active Site Cys (amino acid residue 314), and the second putative Ca2+ binding region (around residue 473) are encoded by separate exons. Accordingly, the intervening sequences may separate the a subunit into functional and structural domains. The gene organization for the b subunit will also be presented. (Supported by NIH Grant HL 16919.)

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