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model predicts that small vesicles promote activation of FX by the extrinsic tenase significantly better than large vesicles
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miR-24 was overexpressed in major trauma-induced coagulopathy (TIC) patients. The negative correlation of miR-24 with FX suggested the possibility that miR-24 might inhibit the synthesis of FX during TIC.
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this study demonstrated that thrombin and factor Xa cleavage sites on HEV pORF1 are obligatory for HEV replication.
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zymogen-like factor Xa variants are conformationally dynamic and ligands such as its cofactor, factor Va, stabilize the molecule rescuing procoagulant activity. At the site of vascular injury, the variants in the presence of factor Va serve as effective prohemostatic agents.
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Data suggest that, for all coagulation proteins tested (prothrombin, factor X, activated factor VII, activated protein C), tighter binding to lipid bilayers (lower Kd) is observed as the proportion of anionic phospholipid increases. These studies were conducted in high-throughput screening using phospholipid bilayers in nanodiscs with multiplexed silicon photonic sensor (micro-ring resonator) array technology.
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A coagulation initiating pathway is revealed in which the TF-FVIIa-nascent FXa complex activates FVIII apart from thrombin feedback.
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Data suggest oxidized lipid vesicles with phosphatidylserine/polyunsaturated fatty acids promote inactivation of ZPI-PZ complex or free ZPI; binding of PZ-complexed or free ZPI to oxidized vesicles mediates inactivation of ZPI (an inhibitor of FXa); blocking heparin- (anticoagulant-)binding site on ZPI interferes with binding to lipid or PZ. (ZPI = protein Z-dependent protease inhibitor; PZ = protein Z; FXa = factor Xa)
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Factor Va reduced by 100-fold the apparent Kd of myosin for factor Xa (Kd approximately 0.48 nM), primarily by reducing koff, indicating formation of a stable ternary complex of myosin:Xa:Va.
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PTX2 was identified PTX2 as a novel partner for FX, and both proteins cooperated to prevent their SR-AI-mediated uptake by macrophages.
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annexin A2 contributes to lung injury and fibrotic disease by mediating the fibrogenic actions of FXa.
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Individuals suffering from relapsing-remitting and secondary progressive multiple sclerosis had significantly higher prothrombin and factor X levels than healthy donors, whereas levels were unchanged in primary progressive MS and neuromyelitis optica patients.
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Low concentrations of TF and exogenous FXIa, each too low to elicit a burst in thrombin production alone, act synergistically when in combination to cause substantial thrombin production.
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A family with factor X deficiency from Argentina displayed a compound heterozygous proband having the combination of a new mutation with an already known one, and homozygous children.
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analysis of how physiological concentrations of Tissue factor pathway inhibitor inhibit FXa
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According to our study, compounds 1a, 1g and 1s displayed evident FXa inhibitory activity and excellent selectivity over thrombin in in vitro inhibition activities studies.
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This study was conducted to assess the spectrum of factor X gene mutation in Iranian patients with congenital factor X deficiency (FXD). Most molecular studies found a diversity in factor X disease causing mutations in Iranian patients. Like other parts of the world, the majority of mutations in Iranian patients were missense mutations, but splice-site mutations were relatively common. [review]
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Large deletions play a minor but essential role in the mutational spectrum of the F7 and F10 genes. Copy number analyses (e. g. MLPA) should be considered if sequencing cannot clarify the underlying reason of an observed coagulopathy. Of note, in cases of combined FVII/FX deficiency, a deletion of the two contiguous genes might be part of a larger chromosomal rearrangement.
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The Ala275Val substitution is a pathogenic mutation that causes the inherited FX deficiency.
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homozygous mutation g.27881G>A(p.Val298Met) of the F10 gene has been identified, which probably accounts for the low FX concentrations in this pedigree
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Establish FXa as a potentially important asthma mediator, stimulating airway smooth muscle function through actions requiring PAR-1 and annexin A2 and involving integrin coactivation.
