Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2022 Jul 26;6(14):4297-4300.
doi: 10.1182/bloodadvances.2022006992.

Pediatric patient with fibrinogen Villeurbanne II presenting with an unprovoked portal vein thrombosis

Brenton J Francisco  1 , Bal Krishan Sharma  2 , Hannah M Russell  3 , Leah Rosenfeldt  2 , A Phillip Owens  3   4 , Matthew J Flick  5 , Eric S Mullins  2 , Joseph Palumbo  1
Affiliations

Pediatric patient with fibrinogen Villeurbanne II presenting with an unprovoked portal vein thrombosis

Brenton J Francisco et al. Blood Adv. .
No abstract available

PubMed Disclaimer

Figures

Figure 1.
Figure 1.
Fibrinogen Villeurbanne II forms abnormal-appearing polymer. Shown are SEM micrographs taken at the same magnification of fibrin clots produced from a 1.77-mg/mL fibrinogen solution purified from plasma obtained from a healthy donor (A) and the patient (B). Size bars, 20 μm. The patient’s fibrin clot was poorly formed, consisting of long, thin fibers with little bundling and irregularly spaced branch points. (C) Quantitative analyses of a 40-μm × 40-μm section of the micrograph show that the patient’s fibrils are significantly thinner than the control. The data represent the mean and SEM. The P value was generated using a Mann-Whitney U test. (D) Shown are the results of a turbidimetric fibrinolytic assay performed using the patient’s and control (normal) plasma. OD, optical density.
Figure 2.
Figure 2.
Fibrinogen Villeurbanne II forms aggregates with albumin in plasma. (A) The patient’s fibrinogen and fibrinogen from a healthy control appeared similar when blotted under reducing and nonreducing conditions. (B) Western blot analyses of fibrinogen coimmunoprecipitation demonstrating an interaction between the patient’s fibrinogen and albumin (at 66 kDa; arrow) that was not observed in fibrinogen from a healthy control, suggesting that the mutant fibrinogen forms aggregates with albumin. IgG, immunoglobulin G.
See this image and copyright information in PMC

Similar articles

See all similar articles

References

    1. Casini A, Blondon M, Tintillier V, et al. . Mutational epidemiology of congenital fibrinogen disorders. Thromb Haemost. 2018;118(11):1867-1874. - PubMed
    1. Hanss M, Biot F. A database for human fibrinogen variants. Ann N Y Acad Sci. 2001;936(1):89-90. - PubMed
    1. Redman CM, Xia H. Fibrinogen biosynthesis. Assembly, intracellular degradation, and association with lipid synthesis and secretion. Ann N Y Acad Sci. 2001;936(1):480-495. - PubMed
    1. Soya K, Terasawa F, Okumura N. Fibrinopeptide A release is necessary for effective B:b interactions in polymerisation of variant fibrinogens with impaired A:a interactions. Thromb Haemost. 2013;109(2):221-228. - PubMed
    1. Kaido T, Yoda M, Kamijo T, Taira C, Higuchi Y, Okumura N. Heterozygous variant fibrinogen γA289V (Kanazawa III) was confirmed as hypodysfibrinogenemia by plasma and recombinant fibrinogens. Int J Lab Hematol. 2020;42(2):190-197. - PubMed