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Validated All-in-One™ qPCR Primer for FGA(NM_021871.4) Search again
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
The protein encoded by this gene is the alpha component of fibrinogen, a blood-borne glycoprotein comprised of three pairs of nonidentical polypeptide chains. Following vascular injury, fibrinogen is cleaved by thrombin to form fibrin which is the most abundant component of blood clots. In addition, various cleavage products of fibrinogen and fibrin regulate cell adhesion and spreading, display vasoconstrictor and chemotactic activities, and are mitogens for several cell types. Mutations in this gene lead to several disorders, including dysfibrinogenemia, hypofibrinogenemia, afibrinogenemia and renal amyloidosis. Alternative splicing results in two isoforms which vary in the carboxy-terminus. [provided by RefSeq].
Gene References into function
- genotypes are associated with plasma fibrinogen levels in Chinese
- The TaqI polymorphism is due to a 28bp duplication at 6587-6614.
- The new dysfunctional fibrinogen, San Giovanni Rotondo variant, a heterozygous single-base deletion at Ala499 in the Aalpha-chain gene, predicts AA changes encoded by the rest of exon V and a premature stop at 518 (Aalpha[499]Ala frameshift stop).
- variation of level following surgery predicts postoperative venous thromboembolism {D-DIMER; fibrin D-dimer}
- Four novel polymorphisms in the fibrinogen Aalpha gene are described: 2 SNPs at -3 and -1051 and a dinucleotide repeat at -946 and a TaqI polymorphism.
- Although the FGA mutation is the same in fibrinogen Rouen and fibrinogen Saint-Germain I, the latter shows a different thrombin-induced fibrinopeptide release pattern and a mild factor V deficiency.
- Fibrinogen isoform alpha C-domain consists of a compact globular cooperative unit attached to the bulk of the molecule by an extended NH2-terminal connector region with a helical poly(L-proline) type II conformation.
- dysfibrinogenemia caused by variation: amino acid substition in position 16 Arg-His
- Analysis of the IVS3delGTAA mutation showed exon 3 skipping in 99% of transcripts & exons 2 & 3 skipping in 1% of transcripts. In FGA intron 3 was preferentially spliced first, followed by intron 2, intron 4, & intron 1.
- review of details of the structure, binding interactions, and function of each of the fibrinogen chains, FGA, FGB, FGG
- Functional analysis of the fibrinogen Aalpha Thr312Ala polymorphism: effects on fibrin structure and function.
- newly identified nonsense mutation G4731T gives rise to a new stop codon at Aalpha-Glu 467; plasma clots from the patients were composed of very thin fibers, with increased fibrin density and reduced pore size
- Review. Genetic and environmental factors alter fibrin structure and function. This has implications for the clinical presentation of vascular disease.
- activated factor XIII incorporates thymosin beta(4) into the isolated gamma-module and alphaC-domain (fibrinogen A alpha); in fibrin the latter serves as the major incorporation site
- mechanism of the alphaC domain-mediated interaction of endothelial cells with fibrin and imply its potential involvement in cell migration
- Prepubertal obese boys exhibited impaired aerobic fitness compared with their normal weight peers irrespective of the TaqI alpha-fibrinogen genotypes that may be associated with fatness in boys.
- results of the present study provided insufficient evidence of the existence of a major [cleft lip/palate] susceptibility locus in the 4q region
- PAI-1 directly bound to the alpha(20-88) and thus concentrated in fibrinogen/fibrin
- Data show that SPARC binds to plasmin-cleaved fibrinogen, but not to native fibrinogen.
- Data indicated that functional genetic variants in FGA are risk factors for venous thromboembolism in Taiwanese populations, and determination of FGA genotypes will likely contribute to primary prevention of this condition.
- Hereditary systemic amyloidosis comprises several autosomal dominant diseases caused by mutations in a number of plasma proteins, including the fibrinogen Aalpha-chain.
- High plasma fibrinogen concentration was associated with non-small cell lung cancer
- In young adults, fibrinogen multi-locus genotypes are associated with plasma fibrinogen levels
- a significant gene-covariate interaction exists between the FXIII Val34Leu variant and fibrinogen levels
- analysis of novel missense mutation (Aa D496N) that may have a role in hypofibrinogenaemia
- Thus, apo(a) may interact with intact fibrin through the Lys-independent and Lys-dependent mechanisms, while the COOH-Lys-dependent mechanism may prevail in the presence of fibrinolytic activity.
- Both desA-fibrin with exposed A-knobs and desB-fibrin bearing B-knobs interacted with fragment D from the gammaD364H fibrinogen containing b-holes but no functional a-holes.
- Manganese and activators of the ERK pathway cooperated in HT29-D4 cell adhesion to fibrinogen.
- the identification of 8 novel mutations, confirming the relative importance of FGA in the molecular basis of fibrinogen deficiency
- the common -148 C/T polymorphism is associated with differences in the TNFalpha release in response to systemic LPS infusion in humans
- Fibrinogen and fibrin modulate the activity of tPA differently in regard to their activation of plasminogen and inhibition by PAI-1
- The Aalpha16 Arg mutationS resulted in an impaired fibrinopeptide A release
- REVIEW: the N-terminus of Bbeta, the C-terminus of Aalpha, and the splice variant gamma' modulate fibrin clot structure
- alpha-fibrinogen Thr312Ala is involved in the pathogenesis of VTE and its action may be modified by other VTE risk factors, BMI and the FXIII Val34Leu variant
- a role of the alphaC domain in the stabilization of fibrin gel
- The A alpha and B beta chains of fibrinogen, but not the gamma chains, are specifically recognized by Treponema denticola ATCC 35405, which may promote colonization and modulate hemostasis.
- Fibrinogen has a role in controlling human platelet fibronectin internalization and cell-surface retention
- Results provide the first direct evidence for the interaction between the alphaC-domains and the central E region through fibrinopeptide B, and indicate that fibrinopeptide A is also involved.
- VWF and fibrinogen are differentially packaged in human platelets
- The peptides GPRPam and GPRPYam, which are surrogate A-knobs, were tested for their influence on fibrin polymerization with fibrinogen from lamprey and humans.
- Results show that ex vivo fibrinogen Aalpha amyloid fibrils have a cross-beta structure similar to other chemical types of amyloid fibrils.
- Identify fibrinogen Aalpha mutations in patients evaluated for hypofibrinogenemia.
- Elevated un-degraded Fg may be a factor causing microvascular permeability that typically accompanies cardiovascular and cerebrovascular disorders.
- Results provide evidence for an association of common variation in the FGG and FGA genes with cerebral SVD.
- Homophenotypic Aalpha R16H fibrinogen (Kingsport) demonstrates altered polymerization with slower fibrinopeptide realease and gelation delay.
- The Thr312Ala variant of the alpha fibrinogen gene was associated with a decreased bleeding risk.
- fibrinogen Aalpha Thr312Ala genotype and allele frequencies are found in chronic thromboembolic pulmonary hypertension (CTEPH) subjects and controls. The presence of the alanine allele significantly increased the risk of CTEPH
- examined the association of haplotypes in the 50-kb fibrinogen gene region with myocardial infarction in 2 large case-control samples
- The Thr312Ala Aalpha chain variant was associated with approximately 20% higher plasma D-dimer levels in European Americans.
- Clumping factor B (ClfB) of Staphylococcus aureus binds to the alphaC-domain of human fibrinogen.
- While fibrinogen genetic variation was strongly associated with fibrinogen levels, there was less evidence of association with the more complex outcomes of cardiovascular disease.
- Direct evidence for the coiled alpha helices of fibrinogen to bring about fibrin elasticity.
- FGG/FGA haplotypes may have a role in ischemic stroke
- in 3 German amyloidosis patients, sequenced the FGA exon 5 and demonstrated heterozygosity for the p.Glu526Val mutation
- Study reports the mutational screening of two unrelated hypofibrinogenemic patients leading to the identification of two missense mutations, one hitherto unknown (alphaCys45Phe), and one previously described (gammaAsn345Ser).
- risk of ischemic stroke was higher in FGG + FGA H3 than in H1 haplotype
- Common single nucleotide polymorphisms and haplotypes explain the interindividual and intraindividual variability of fibrinogen levels, in patients with a history of myocardial infarction.
