ArticleThe Journal of biological chemistry2014
Coagulation factor XIIIa substrates in human plasma: identification and incorporation into the clot.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed.
- Human Transglutaminases: Updated Insights into Activation Mechanisms, Allosteric Regulation and Disease.International journal of molecular sciences · 2026Review
- Increased number of crosslinking sites for factor XIII counteracts the mechanical and lytic destabilization of fibrin caused by citrullination of fibrinogen.Frontiers in immunology · 2026Article
- The role of transglutaminase 2 in stabilizing fibrin clots and supporting hemostasis.PloS one · 2026Article
- Fetal Defects in Mice Treated With Integrase Strand Transfer Inhibitors: Comparison of Dolutegravir, Raltegravir, Bictegravir, and Cabotegravir.The Journal of infectious diseases · 2025Article
- Review
- Complement-Coagulation Cross-talk: Factor H-mediated regulation of the Complement Classical Pathway activation by fibrin clots.Frontiers in immunology · 2024Article
- Antioxidant role of methionine-containing intra- and extracellular proteins.Biophysical reviews · 2023Review
- IgE-binding monocytes upregulate the coagulation cascade in allergic horses.Genes and immunity · 2023Article
- The luminal domain ofFrontiers in parasitology · 2023Article
- Mast cell-derived factor XIIIA contributes to sexual dimorphic defense against group B streptococcal infections.The Journal of clinical investigation · 2022Article
- 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 is a newly identified binding partner for platelet collagen receptor GPVI-dimer-An interaction that may modulate fibrin crosslinking.Research and practice in thrombosis and haemostasis · 2022Article
- Functionalizing Fibrin Hydrogels with Thermally Responsive Oligonucleotide Tethers for On-Demand Delivery.Bioengineering (Basel, Switzerland) · 2022Article
- Coagulation, inflammation, and CD46 transgene expression in neonatal porcine islet xenotransplantation.Xenotransplantation · 2021Article
- Factor XIII-A: An Indispensable "Factor" in Haemostasis and Wound Healing.International journal of molecular sciences · 2021Review
- F13A1 transglutaminase expression in human adipose tissue increases in acquired excess weight and associates with inflammatory status of adipocytes.International journal of obesity (2005) · 2021Article
- Role, Laboratory Assessment and Clinical Relevance of Fibrin, Factor XIII and Endogenous Fibrinolysis in Arterial and Venous Thrombosis.International journal of molecular sciences · 2021Review
- Quantitative proteomics analysis of Angiostrongylus vasorum-induced alterations in dog serum sheds light on the pathogenesis of canine angiostrongylosis.Scientific reports · 2021Article
- Factor XIIIa inhibitors as potential novel drugs for venous thromboembolism.European journal of medicinal chemistry · 2020Review
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Coagulation factor XIII (FXIII) is a transglutaminase with a well defined role in the final stages of blood coagulation. Active FXIII (FXIIIa) catalyzes the formation of ε-(γ-glutamyl)lysine isopeptide bonds between specific Gln and Lys residues. The primary physiological outcome of this catalytic activity is stabilization of the fibrin clot during coagulation. The stabilization is achieved through the introduction of cross-links between fibrin monomers and through cross-linking of proteins with anti-fibrinolytic activity to fibrin. FXIIIa additionally cross-links several proteins with other functionalities to the clot. Cross-linking of proteins to the clot is generally believed to modify clot characteristics such as proteolytic susceptibility and hereby affect the outcome of tissue damage. In the present study, we use a proteomic approach in combination with transglutaminase-specific labeling to identify FXIIIa plasma protein substrates and their reactive residues. The results revealed a total of 147 FXIIIa substrates, of which 132 have not previously been described. We confirm that 48 of the FXIIIa substrates were indeed incorporated into the insoluble fibrin clot during the coagulation of plasma. The identified substrates are involved in, among other activities, complement activation, coagulation, inflammatory and immune responses, and extracellular matrix organization.
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