scholarly journals Neutralizing autoantibody against factor XIII A subunit resulted in severe bleeding diathesis with a fatal outcome - characterization of the antibody

2016 ◽  
Vol 14 (8) ◽  
pp. 1517-1520 ◽  
Author(s):  
K. Pénzes ◽  
K. Rázsó ◽  
É. Katona ◽  
A. Kerényi ◽  
M. Kun ◽  
...  
Keyword(s):  
Factor Xiii ◽  
Fatal Outcome ◽  
Severe Bleeding ◽  
Bleeding Diathesis ◽  
A Subunit

scholarly journals Factor XIII-A: An Indispensable “Factor” in Haemostasis and Wound Healing

2021 ◽  
Vol 22 (6) ◽  
pp. 3055
Author(s):  
Fahad S. M. Alshehri ◽  
Claire S. Whyte ◽  
Nicola J. Mutch
Keyword(s):  
Bone Marrow ◽  
Wound Healing ◽  
Crucial Role ◽  
Factor Xiii ◽  
Severe Bleeding ◽  
Bleeding Diathesis ◽  
Unknown Mechanism ◽  
Protein Substrates ◽  
Physiological Processes ◽  
Isopeptide Bonds

Factor XIII (FXIII) is a transglutaminase enzyme that catalyses the formation of ε-(γ-glutamyl)lysyl isopeptide bonds into protein substrates. The plasma form, FXIIIA2B2, has an established function in haemostasis, with fibrin being its principal substrate. A deficiency in FXIII manifests as a severe bleeding diathesis emphasising its crucial role in this pathway. The FXIII-A gene (F13A1) is expressed in cells of bone marrow and mesenchymal lineage. The cellular form, a homodimer of the A subunits denoted FXIII-A, was perceived to remain intracellular, due to the lack of a classical signal peptide for its release. It is now apparent that FXIII-A can be externalised from cells, by an as yet unknown mechanism. Thus, three pools of FXIII-A exist within the circulation: plasma where it circulates in complex with the inhibitory FXIII-B subunits, and the cellular form encased within platelets and monocytes/macrophages. The abundance of this transglutaminase in different forms and locations in the vasculature reflect the complex and crucial roles of this enzyme in physiological processes. Herein, we examine the significance of these pools of FXIII-A in different settings and the evidence to date to support their function in haemostasis and wound healing.

Pharmacokinetic characterization of recombinant factor XIII (FXIII)-A2 across age groups in patients with FXIII A-subunit congenital deficiency

Haemophilia ◽  
2015 ◽  
Vol 21 (3) ◽  
pp. 380-385 ◽  
Author(s):  
B. Brand-Staufer ◽  
M. Carcao ◽  
B. A. Kerlin ◽  
A. Will ◽  
M. Williams ◽  
...  
Keyword(s):  
Factor Xiii ◽  
Age Groups ◽  
Congenital Deficiency ◽  
A Subunit

Alloantibody developed in a factor XIII A subunit deficient patient during substitution therapy; characterization of the antibody

Haemophilia ◽  
2015 ◽  
Vol 22 (2) ◽  
pp. 268-275 ◽  
Author(s):  
K. Pénzes ◽  
C. Vezina ◽  
Z. Bereczky ◽  
É. Katona ◽  
M. Kun ◽  
...  
Keyword(s):  
Factor Xiii ◽  
Substitution Therapy ◽  
Deficient Patient ◽  
A Subunit

scholarly journals Phenotype-genotype characterization of 10 families with severe a subunit factor XIII deficiency

2003 ◽  
Vol 23 (1) ◽  
pp. 98-98 ◽  
Author(s):  
Flora Peyvandi ◽  
Liliana Tagliabue ◽  
Marzia Menegatti ◽  
Mehran Karimi ◽  
Istvan Komáromi ◽  
...  
Keyword(s):  
Factor Xiii ◽  
Factor Xiii Deficiency ◽  
A Subunit

Severe Bleeding Diathesis From Acquired Factor XIII Inhibitor Secondary to SLE

CHEST Journal ◽  
2013 ◽  
Vol 144 (4) ◽  
pp. 924A
Author(s):  
Ian Lee ◽  
Jo Persoon-Gundy ◽  
Ching-Fei Chang
Keyword(s):  
Factor Xiii ◽  
Severe Bleeding ◽  
Bleeding Diathesis

scholarly journals Novel treatment for congenital FXIII deficiency

Blood ◽  
2012 ◽  
Vol 119 (22) ◽  
pp. 5060-5061 ◽  
Author(s):  
Hans P. Kohler
Keyword(s):  
Factor Xiii ◽  
Autosomal Recessive ◽  
Rare Disorder ◽  
Severe Bleeding ◽  
Bleeding Diathesis ◽  
Inherited Disease ◽  
Novel Treatment ◽  
Fxiii Deficiency ◽  
Congenital Factor

Congenital Factor XIII (FXIII) deficiency is a rare autosomal recessive inherited disease leading to severe bleeding diathesis. In this issue of Blood, Inbal and colleagues report on a safe and novel treatment of this rare disorder with recombinant FXIII (rFXIII).1

scholarly journals Molecular Mechanism of a Mild Phenotype in Coagulation Factor XIII (FXIII) Deficiency: A Splicing Mutation Permitting Partial Correct Splicing of FXIII A-Subunit mRNA

Blood ◽  
1997 ◽  
Vol 89 (4) ◽  
pp. 1279-1287 ◽  
Author(s):  
Hanna Mikkola ◽  
Laszlo Muszbek ◽  
Elina Laiho ◽  
Martti Syrjälä ◽  
Eija Hämäläinen ◽  
...  
Keyword(s):  
Molecular Mechanism ◽  
Factor Xiii ◽  
Splice Donor Site ◽  
Severe Bleeding ◽  
Minute Amount ◽  
Mild Phenotype ◽  
Stop Mutation ◽  
Mrna Transcripts ◽  
A Subunit ◽  
Fxiii Deficiency

AbstractCongenital factor XIII (FXIII) deficiency is potentially a severe bleeding disorder, but in some cases, the symptoms may be fairly mild. In this study, we have characterized the molecular mechanism of a mild phenotype of FXIII A-subunit deficiency in a Finnish family with two affected sisters, one of whom has even had two successful pregnancies without regular substitution therapy. In the screening tests for FXIII deficiency, no A-subunit could be detected, but by using more sensitive assays, a minute amount of functional A-subunit was seen. 3H-putrescine incorporation assay showed distinct FXIII activity at the level of 0.35% of controls, and also the fibrin cross-linking pattern in the patients clotted plasma showed partial γ-γ dimerization. In Western blot analysis, a faint band of full-length FXIII A-subunit was detected in the patients' platelets. The patients have previously been identified as heterozygotes for the Arg661 → Stop mutation. Here we report a T → C transition at position +6 of intron C in their other allele. The transition affected splicing of FXIII mRNA resulting in low steady state levels of several variant mRNA transcripts. One transcript contained sequences of intron C, whereas two transcripts resulted from skipping of one or two exons. Additionally, correctly spliced mRNA lacking the Arg661 → Stop mutation of the maternal allele could be detected. These results demonstrate that a mutation in splice donor site of intron C can result in several variant mRNA transcripts and even permit partial correct splicing of FXIII mRNA. Further, even the minute amount of correctly processed mRNA is sufficient for producing protein capable of γ-γ dimerization of fibrin. This is a rare example of an inherited functional human disorder in which a mutation affecting splicing still permits some correct splicing to occur and this has a beneficial effect to the phenotype of the patients.

Molecular characterization of a novel mutation in the factor XIII a subunit gene associated with a severe defect: importance of prophylactic substitution

2009 ◽  
Vol 20 (7) ◽  
pp. 605-606 ◽  
Author(s):  
Pierre Morange ◽  
Nawel Trigui ◽  
Corinne Frère ◽  
Hervé Chambost ◽  
Catherine Pouymayou ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Factor Xiii ◽  
Novel Mutation ◽  
Subunit Gene ◽  
A Subunit
Sign in / Sign up

Export Citation Format

Share Document