Binding of Citrate to Normal Fibrinogen and to Metz Fibrinogen

Ladure, P.; Ricordel, Yvan; Soria, J; Soria, Claudine; Samama, M

doi:10.1515/9783110865325-016

Cited by 3 publications

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“…This process plays an important role in down‐regulating the rate of fibrinolysis . Using a homozygous case of dysfibrinogenemia characterized by an amino acid substitution located at the peptide bond on the Aα chain that is normally cleaved by thrombin, it was shown that clotting of fibrinogen may sometimes occur in absence of fibrinopeptide A release …”

Section: Introductionmentioning

confidence: 99%

“…7 Using a homozygous case of dysfibrinogenemia characterized by an amino acid substitution located at the peptide bond on the Aα chain that is normally cleaved by thrombin, it was shown that clotting of fibrinogen may sometimes occur in absence of fibrinopeptide A release. [8][9][10] Recently, it was evidenced that fibrinogen αC domain has several roles in coagulation, mediating its activity during various physiological and pathological processes. αC domain is composed of residues Aα 220-610 consisting of a flexible, unstructured αC connector (Aα 221-391) and a relatively compact C-terminal portion of fibrinogen Aα chain (Aα 392-610).…”

Section: Introductionmentioning

confidence: 99%

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Fibrinogen αC domain: Its importance in physiopathology

Mirshahi

Varin

et al. 2019

Research and Practice in Thrombosis and Haemostasis

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Essentials The C‐terminal domain of the fibrinogen α chain (αC domain) is implicated in different severe diseases via clotting abnormalities or amyloid deposits. Certain anomalies of the fibrinogen molecule lead to amyloid deposits in the kidney, inducing renal insufficiency. In contrast, in Alzheimer's disease, fibrinogen is normal, but due to an inflammatory process, fibrinogen crosses into the brain and interacts with Aβ, leading to formation of pathological deposits. Abstract Fibrinogen, involved in coagulation, is a soluble protein composed of two sets of disulfide‐bridged Aα, Bβ, and γ‐chains. In this review, we present the clinical implications of the αC domain of the molecule in Alzheimer's disease, hereditary renal amyloidosis and a number of thrombotic and hemorrhagic disorders. In Alzheimer's disease, amyloid beta peptide (Aβ) is increased and binds to the αC domain of normal fibrinogen, triggering increased fibrin(ogen) deposition in patients’ brain parenchyma. In hereditary renal amyloidosis, fibrinogen is abnormal, with mutations located in the fibrinogen αC domain. The mutant αC domain derived from fibrinogen degradation folds incorrectly so that, in time, aggregates form, leading to amyloid deposits in the kidneys. In these patients, no thrombotic tendency has been observed. Abnormal fibrinogens with either a point mutation in the αC domain or a frameshift mutation resulting in absence of a part of the αC domain are often associated with either thrombotic events or bleeding. Mutation of an amino acid into cysteine (as in fibrinogens Dusart and Caracas V) or a frameshift mutation yielding an unpaired cysteine in the αC domain is often responsible for thrombotic events. Covalent binding of albumin to the unpaired cysteine via a disulphide bridge leads to decreased accessibility to the fibrinolytic enzymes, hence formation of poorly degradable fibrin clots, which explains the high incidence of thrombosis. In contrast, anomalies due to a frameshift mutation in the αC connector of the molecule, provoking deletion of a great part of the αC domain, are associated with bleeding.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Fibrinogen αC domain: Its importance in physiopathology

Mirshahi

Varin

et al. 2019

Research and Practice in Thrombosis and Haemostasis

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Congenital dysfibrinogenemias. A review

Rocha

Páramo

Aranda

et al. 1985

La Ricerca in Clinica e in Laboratorio

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Human Fibrinogen

Scheraga

Shafer

Higgins³

1988

CRC Critical Reviews in Clinical Laboratory Sciences

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The structure and physical properties of human fibrinogen and fibrin are reviewed along with methods for the detection of products of their metabolism. Interactions of human fibrinogen with thrombin, factor XIII, plasminogen, glycoprotein IIb/IIIa, and other proteins are related to their relevance to thrombosis and hemostasis. To the extent information is available, the structural determinants of these interactions are delineated, and kinetic and thermodynamic parameters associated with the interactions are listed. Individual steps in the reaction pathway for the conversion of fibrinogen to cross-linked fibrin are characterized. The altered hemostatic properties of mutational variants of fibrinogen are related to their altered structure. The structures of the genes coding for the polypeptide chains of fibrinogen are discussed along with the current state of knowledge of the control and regulation of fibrinogen synthesis. Fibrinogen catabolism and fibrinolysis are also reviewed.

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Binding of Citrate to Normal Fibrinogen and to Metz Fibrinogen

Cited by 3 publications

References 0 publications

Fibrinogen αC domain: Its importance in physiopathology

Fibrinogen αC domain: Its importance in physiopathology

Congenital dysfibrinogenemias. A review

Human Fibrinogen

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