Fibrinogen geneva II

Casini, Alessandro; Maistre, Emmanuel de; Casini-Stuppi, Virginie; Fontana, Pierre; Neerman-Arbez, Marguerite; Moerloose, Philippe de

doi:10.1097/mbc.0000000000000039

Cited by 6 publications

(3 citation statements)

References 13 publications

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“…[7] Similar results were reported by Casini et al [19] : FGA mutations affecting residue Arg16 (i.e., Arg16His and Arg16Cys) at the FpA thrombin cleavage site were frequent in 13.9% and 8.9% of patients, respectively. [24] The results indicate that the substitution of the Aα-chain residue Arg16His can prevent thrombin cleavage of the scissile Aα Arg16-Gly17 bond, thus delaying the release of FpA and disrupting of the initial alignment of fibrin monomers into protofibrils, and then these changes can impair the subsequent fibrin clot formation.…”

Section: Discussionsupporting

confidence: 80%

“…Many studies show that 1 characteristic of CD is normal fibrinogen antigen levels associated with disproportionately low functional activity. [7,8] The vast majority of cases are the result of heterozygous missense mutations in coding region of 1 of the 3 fibrinogen genes (FGA, FGB, or FGG). [9] Molecular defects are usually single-base mutations, leading to alterations in the release of fibrinopeptide, fibrin polymerization, fibrin cross-linking, or fibrinolysis of the fibrinogen.…”

Section: Introductionmentioning

confidence: 99%

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Three cases of congenital dysfibrinogenemia in unrelated Chinese families

Luo¹,

Deng

Xiang³

et al. 2016

Medicine

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Congenital dysfibrinogenemia (CD) is a qualitative fibrinogen disorder caused by an abnormal fibrinogen molecule structure, leading to dysfunctional blood coagulation. This study describes 3 cases of dysfibrinogenemia identified in the unrelated Chinese pedigrees.Routine coagulation screening tests were performed on the probands and their families. The antigens and functionality of fibrinogen was measured using an immunoturbidimetry assay and the Clauss method, respectively. To identify the genetic mutation responsible for these dysfibrinogens, genomic DNA extracted from the blood was analyzed using PCR amplification and direct sequencing. The presence of the mutant chains was determined using matrix-assisted laser desorption/ionization time of flight (MALDI-TOF) mass spectroscopy. Purified plasma fibrinogen of 3 probands was analyzed using SDS–PAGE, fibrinogen clottability, fibrin polymerization, fibrinopeptide release, and scanning electron microscopy (SEM).The 3 probands had a long thrombin time. Levels of functional fibrinogen were found to be very low, while the fibrinogen antigen was within the normal range. DNA sequencing revealed a heterozygous Arg16His substitution in the fibrinogen Aα chain (FGA). The mutant chains were found to be expressed using MALDI-TOF mass spectroscopy. SDS–PAGE did not reveal any difference in the molecular weights of 3 polypeptide chains between normal and abnormal fibrinogens. Fibrinogen clottability showed a slower fibrin clot formation than the healthy control. Fibrin polymerization, after addition of thrombin, showed a prolonged lag phase and decreased final turbidity. The kinetics of fibrinopeptides release revealed a decreased amount of the released fibrinopeptide A. SEM of the patient's fibrin clot was found to be abnormal.Results indicate that the 3 probands with dysfibrinogenemia were caused by mutations of Aα chain Arg16His. Mutation of this fibrinogen induced dysfunction of plasma fibrinogen.

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Section: Discussionsupporting

confidence: 80%

Section: Introductionmentioning

confidence: 99%

Three cases of congenital dysfibrinogenemia in unrelated Chinese families

Luo¹,

Deng

Xiang³

et al. 2016

Medicine

View full text Add to dashboard Cite

show abstract

“…In the first issue of 2024, STH republished the first paper that STH ever published, on the molecular structure of fibrinogen, 22 with an accompanying Commentary from Alessandro Casini and Marguerite Neerman-Arbez. 23 In the current issue of STH, we are republishing the most cited manuscript from STH according to Web of Science, 24 and an accompanying Commentary from authors. 25…”

Section: Tablementioning

confidence: 99%