Epigenetic, polymorphic and mutational (Αα167Arg→Lys) contribution to a functionally abnormal fibrinogen

Brennan, Stephen O.; Oliver, Jocelyn; Davis, Ryan L.

doi:10.1111/j.1538-7836.2011.04337.x

Journal of Thrombosis and Haemostasis

2011

DOI: 10.1111/j.1538-7836.2011.04337.x

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Epigenetic, polymorphic and mutational (Αα167Arg→Lys) contribution to a functionally abnormal fibrinogen

Stephen O. Brennan

Jocelyn Oliver

Ryan L. Davis

Abstract: To cite this article: Brennan SO, Oliver J, Davis RL. Epigenetic, polymorphic and mutational (Aa167Arg fi Lys) contribution to a functionally abnormal fibrinogen. J Thromb Haemost 2011; 9: 1410-2.

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Cited by 2 publications

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“…Increasing the sialic acid saturation increases the thrombin clotting time (TCT) through electrostatic repulsion between fibrin monomers (5). The presence of co-inherited polymorphisms can also influence functionality and TCT (6).…”

mentioning

confidence: 99%

Novel FGG variant (ү339C→S) confirms importance of the ү326–339 disulphide bond for plasma expression of newly synthesised fibrinogen

Brennan¹,

Laurie²,

Smith³

2015

Thromb Haemost

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Letter to the Editor Dear Sirs, Fibrinogen is synthesised in the liver from Aα, Bβ and γ chains. The protein is assembled from Aα-γ and Bβ-γ intermediates in the endoplasmic reticulum (1) and on acquiring an additional chain, Aα-Bβ-γ half-molecules dimerise and proceed to the Golgi for pruning and extension of N-linked oligosaccharides before secretion of the (Aα-Bβ-γ) 2 assembly into the circulation. The 340 kDa molecule has a linear D-E-D configuration with the central E domain connected to the peripheral D domains by a three-chain coiled coil. The D domains are formed from the independently folding C-terminal regions of the Bβ and γ chains (2). Disulphide bonding helps maintain the structural integrity of the molecule; each chain has its own internal S-S bridges, contributes to a pair of disulphide rings at either end of each coiled coil and is involved in S-S bonding between half molecules (3). Substitutions that affect the folding of chains can cause profound hypofibrinogenaemia if they perturb assembled dimers because they can affect 75 % of molecules in a heterozygous carrier. Substitution and posttranslational modification can also affect the functionality of fibrinogen. With biantennary oligosaccharide chains at

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mentioning

confidence: 99%

Novel FGG variant (ү339C→S) confirms importance of the ү326–339 disulphide bond for plasma expression of newly synthesised fibrinogen

Brennan¹,

Laurie²,

Smith³

2015

Thromb Haemost

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A novel mutation in the FGB: c.1105C>T turns the codon for amino acid Bβ Q339 into a stop codon causing hypofibrinogenemia

Marchi

Brennan

Meyer

et al. 2013

Blood Cells, Molecules, and Diseases

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Epigenetic, polymorphic and mutational (Αα167Arg→Lys) contribution to a functionally abnormal fibrinogen

Abstract: To cite this article: Brennan SO, Oliver J, Davis RL. Epigenetic, polymorphic and mutational (Aa167Arg fi Lys) contribution to a functionally abnormal fibrinogen. J Thromb Haemost 2011; 9: 1410-2.

Cited by 2 publications

References 14 publications

Novel FGG variant (ү339C→S) confirms importance of the ү326–339 disulphide bond for plasma expression of newly synthesised fibrinogen

Novel FGG variant (ү339C→S) confirms importance of the ү326–339 disulphide bond for plasma expression of newly synthesised fibrinogen

A novel mutation in the FGB: c.1105C>T turns the codon for amino acid Bβ Q339 into a stop codon causing hypofibrinogenemia

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