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Human Factor VII Protein expressed in Human Cells - ABIN2004310
Li, Wang, Long, Su, Bukhory, Dai, Jin, Huang, Jia, Li, Fan, Liu, Wang: Novel antibody against a glutamic acid-rich human fibrinogen-like protein 2-derived peptide near Ser91 inhibits hfgl2 prothrombinase activity. in PLoS ONE 2014
Hepsin (show HPN Proteins) plays a physiologically important role in factor VII (show TH Proteins) activation and hemostasis in zebrafish.
study reports the full-length cDNA sequences of rhesus monkey FVII; deduced protein sequence of FVII indicates the functional domains; comparison of three-dimensional protein structure with human shows high conservation between them
The current meta-analysis suggested that polymorphism of R353Q in factor VII (show TH Proteins) was not associated with the MI risk.
FVIIa-antithrombin (show SERPINC1 Proteins) levels in early and late preeclampsia
Using protein C-factor VII (show TH Proteins) chimera demonstrate that APC (show APC Proteins) light chain amino acid residues outside the EPCR (show PROCR Proteins)-binding site enable cytoprotective PAR1 (show MARK2 Proteins) signaling.
Report a good correlation between the type of F7 mutation and/or polymorphisms and FVII:C levels, without a direct link between FVII:C and bleeding tendency in factor VII (show TH Proteins) deficiencies.
Polymorphism rs6046 of the FVII gene is associated with the development of fetal growth retardation in Central Russia.
A common pathogenic mechanism, possibly a defective folding of the mutant proteins, was triggered by the FVII mutations. The misfolded state led to impaired trafficking of these proteins causing Endoplasmic reticulum retention, which would explain the low to very low FVII plasma levels observed in patients carrying these mutations.
FVIIa-antithrombin (show SERPINC1 Proteins) but not FVIIa is a ligand for LRP1 (show LRP1 Proteins), and LRP1 (show LRP1 Proteins) contributes to the clearance of FVIIa-antithrombin (show SERPINC1 Proteins) in vivo
Data suggest that, for all coagulation proteins tested (prothrombin, factor X, activated factor VII, activated protein C), tighter binding to lipid bilayers (lower Kd) is observed as the proportion of anionic phospholipid increases. These studies were conducted in high-throughput screening using phospholipid bilayers in nanodiscs with multiplexed silicon photonic sensor (micro-ring resonator) array technology.
A coagulation initiating pathway is revealed in which the TF-FVIIa-nascent FXa (show F10 Proteins) complex activates FVIII (show F8 Proteins) apart from thrombin (show F2 Proteins) feedback.
Data suggest activation of PAR2 (show F2RL1 Proteins) via FVIIA/TF signaling activates PI3K (show PIK3CA Proteins)/AKT (show AKT1 Proteins) signaling, inactivates GSK3b signaling, leads to accumulation of beta-catenin (show CTNNB1 Proteins), and promotes tumor cell migration/invasion. (PAR2 (show F2RL1 Proteins) = protease-activated receptor 2 (show F2RL1 Proteins); FVIIA = coagulation factor VIIa; TF = tissue factor/thromboplastin (show F3 Proteins); PI3K (show PIK3CA Proteins) = phosphatidylinositol 3-kinase; AKT (show AKT1 Proteins) = proto-oncogene (show RAB1A Proteins) protein c-akt (show AKT1 Proteins); GSK3b = glycogen synthase kinase 3 beta)
Leu8 (show SELL Proteins) is crucial for FVIIa-EPCR (show PROCR Proteins) binding; this study characterizes its interaction in vivo in mice
FVIIa binding to EPCR (show PROCR Proteins) leads to a barrier protective effect in vivo
FVIIa binding to EPCR (show PROCR Proteins) on the endothelium facilitates the transport of FVIIa from circulation to extravascular tissues where TF resides
RNA interference of Serpinc1 (show SERPINC1 Proteins) and/or Proc allows for evaluation of the function of these genes in vivo and provides a novel, controlled mouse model for spontaneous venous thrombosis.
Murine FVIIa binds poorly to murine EPCR (show PROCR Proteins).
Conclude that the fVII-targeted verteporfin photodynamic therapy that we report here is a novel and effective therapeutic with improved selectivity for the treatment of breast cancer.
The participation of Egr-1 (show EGR1 Proteins) in FVIIa-mediated regulation of keratinocyte function was confirmed by use of Egr-1 (show EGR1 Proteins)-deficient mice, wherein a significant delay in skin wound healing after injury was observed, relative to WT mice.
Recombinant FVIIa readily associates with the vascular endothelium and subsequently enters into extravascular spaces where it is likely to bind to tissue factor (show F3 Proteins) and is retained for extended time periods.
Gene targeting of tissue factor (show F3 Proteins), factor X, and factor VII (show TH Proteins) in mice: their involvement in embryonic development
This gene encodes coagulation factor VII which is a vitamin K-dependent factor essential for hemostasis. This factor circulates in the blood in a zymogen form, and is converted to an active form by either factor IXa, factor Xa, factor XIIa, or thrombin by minor proteolysis. Upon activation of the factor VII, a heavy chain containing a catalytic domain and a light chain containing 2 EGF-like domains are generated, and two chains are held together by a disulfide bond. In the presence of factor III and calcium ions, the activated factor then further activates the coagulation cascade by converting factor IX to factor IXa and/or factor X to factor Xa. Defects in this gene can cause coagulopathy. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
coagulation factor VII
, serum prothrombin conversion accelerator
, clotting factor
, FVII coagulation protein
, eptacog alfa
, anti-thrombin 3
, serine (or cysteine) proteinase inhibitor, clade C (antithrombin), member 1
, serpin C1
, serpin peptidase inhibitor, clade C, member 1