ArticleBlood2014
Interaction of factor XIII subunits.
Article in Blood, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed.
- Beyond complement: comprehensive assessment of factor XIII plasma dynamics and genetics in atypical hemolytic uremic syndrome.Research and practice in thrombosis and haemostasis · 2026Article
- Preparative leukapheresis impairs autologous donor hemostasis and platelet function.Research and practice in thrombosis and haemostasis · 2026Observational
- Factor XIII Supplementation in Postpartum Hemorrhage: From Biological Rationale to Clinical Implementation.American journal of hematology · 2026Review
- Factor XIII Deficiency: A Review of Biology, Testing, and Treatment.Clinical hematology international · 2026Review
- The role of transglutaminase 2 in stabilizing fibrin clots and supporting hemostasis.PloS one · 2026Article
- Review
- Coagulation Factor XIII - Last to think about?Blood transfusion = Trasfusione del sangue · 2025Article
- Article
- [Gene diagnosis of a family with coagulation factor ⅩⅢ deficiency caused by large deletion of F13A1 gene].Zhonghua xue ye xue za zhi = Zhonghua xueyexue zazhi · 2023Article
- Fibrinogen and Factor XIII in Venous Thrombosis and Thrombus Stability.Arteriosclerosis, thrombosis, and vascular biology · 2022Review
- Exploring the function of factor XIII free B subunit: Interactions with complement factors and a novel approach to identify potential binding partners.Research and practice in thrombosis and haemostasis · 2022Article
- Factor XIII-A: An Indispensable "Factor" in Haemostasis and Wound Healing.International journal of molecular sciences · 2021Review
- Factor XIII and Fibrin Clot Properties in Acute Venous Thromboembolism.International journal of molecular sciences · 2021Review
- Clinical Validation of an Automated Fluorogenic Factor XIII Activity Assay Based on Isopeptidase Activity.International journal of molecular sciences · 2021Article
- A journey upstream: Fluctuating platelet-specific genes in cell-free plasma as proof-of-concept for using ribonucleic acid sequencing to improve understanding of postinjury platelet biology.The journal of trauma and acute care surgery · 2020Observational
- The Plasma Factor XIII Heterotetrameric Complex Structure: Unexpected Unequal Pairing within a Symmetric Complex.Biomolecules · 2019Article
- Factor XIII topology: organization of B subunits and changes with activation studied with single-molecule atomic force microscopy.Journal of thrombosis and haemostasis : JTH · 2019Article
- Disruption of Structural Disulfides of Coagulation FXIII-B Subunit; Functional Implications for a Rare Bleeding Disorder.International journal of molecular sciences · 2019Article
- Fibrinogen and factor XIII: newly recognized roles in venous thrombus formation and composition.Current opinion in hematology · 2018Review
- Factor XIII in plasma, but not in platelets, mediates red blood cell retention in clots and venous thrombus size in mice.Blood advances · 2018Article
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8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Coagulation factor XIII (FXIII) is a heterotetramer consisting of 2 catalytic A subunits (FXIII-A2) and 2 protective/inhibitory B subunits (FXIII-B2). FXIII-B, a mosaic protein consisting of 10 sushi domains, significantly prolongs the lifespan of catalytic subunits in the circulation and prevents their slow progressive activation in plasmatic conditions. In this study, the biochemistry of the interaction between the 2 FXIII subunits was investigated. Using a surface plasmon resonance technique and an enzyme-linked immunosorbent assay-type binding assay, the equilibrium dissociation constant (Kd) for the interaction was established in the range of 10(-10) M. Based on the measured Kd, it was calculated that in plasma approximately 1% of FXIII-A2 should be in free form. This value was confirmed experimentally by measuring FXIII-A2 in plasma samples immunodepleted of FXIII-A2B2. Free plasma FXIII-A2 is functionally active, and when activated by thrombin and Ca(2+), it can cross-link fibrin. In cerebrospinal fluid and tears with much lower FXIII subunit concentrations, >80% of FXIII-A2 existed in free form. A monoclonal anti-FXIII-B antibody that prevented the interaction between the 2 subunits reacted with the recombinant combined first and second sushi domains of FXIII-B, and its epitope was localized to the peptide spanning positions 96 to 103 in the second sushi domain.
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