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A505G
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naturally occurring polymorphism
A93V
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mutant is comparably to wild-type activated by thrombin, mutant is slightly less activated by thrombin in the presence of thrombomodulin, kcat (1/sec) (p-anisylazoformyl-L-arginine, activated by thrombin in the presence of thrombomodulin): 0.205, Km (mM) (p-anisylazoformyl-L-arginine, activated by thrombin in the presence of thrombomodulin): 0.000169, mutation shows no effect on the activation by plasmin, kcat (1/sec) (hippuryl-arginine, activated by plasmin): 0.00043, Km (mM) (hippuryl-arginine, activated by plasmin): 0.00001, intrinsic stability of activated TAFI (half-life): 6.3 min
D87A
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activated with similar kinetics as wild-type enzyme by thrombin-thrombomodulin. Increase in activation by plasmin. Thermal inactivation at 37°C is similar to that of the wild-type enzyme
I182R
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site-directed mutagenesis, the mutant shows reduced activition by thrombin but similar fibrinogen and plasminogen binding capacitiy compared to the wild-type enzyme
I183E
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site-directed mutagenesis, the mutant shows reduced activition by thrombin but similar fibrinogen and plasminogen binding capacitiy compared to the wild-type enzyme
I325I
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a higher frequency of the most stable Ile325Ile proCPU is seen among carriers of FII G20210A mutation compared to the control group in comparison to Thr325Thr and Thr325Ile proCPU. In addition, proCPU as a risk factor for thrombosis is evaluated. In heterozygous carriers of FV Leiden or FII G20210A high levels of proCPU confers to an almost 4fold increased risk for spontaneous onset thrombosis. The more stable Ile325Ile proCPU seems to impose a higher risk for clinical manifestation of the thrombophilic condition
S305C/T329I
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generation of a stable activated thrombin activable fibrinolysis inhibitor variant by site-directed mutagenesis, the mutant's half-life is 11fold increased compared to the wild-type enzyme, the mutant also shows about 3fold higher fibrin clot lysis activityoverview
S90A
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activated with similar kinetics as wild-type enzyme by thrombin-thrombomodulin. Increase in activation by plasmin. Thermal inactivation at 37°C is similar to that of the wild-type enzyme
S90D/S94V/S90D
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mutant is not activated by thrombin or by thrombin in the presence of thrombomodulin, mutant is weakly activated by plasmin, kcat (1/sec) (hippuryl-arginine, activated by plasmin): 0.00004, Km (mM) (hippuryl-arginine, activated by plasmin): 0.000005, intrinsic stability of activated TAFI (half-life): 5.9 min
S94V
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mutant is considerably more effectively activated by thrombin, mutant is also activated by thrombin in the presence of thrombomodulin, kcat (1/sec) (p-anisylazoformyl-L-arginine, activated by thrombin in the presence of thrombomodulin): 0.328, Km (mM) (p-anisylazoformyl-L-arginine, activated by thrombin in the presence of thrombomodulin): 0.000232, mutation shows no effect on the activation by plasmin, kcat (1/sec) (hippuryl-arginine, activated by plasmin): 0.0003, Km (mM) (hippuryl-arginine, activated by plasmin): 0.000006, intrinsic stability of activated TAFI (half-life): 6.1 min
T147A
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naturally occurring polymorphism
T325I/T329I/H333Y/H335Q
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inactive mutant has a 70fold increased half-life and a 3fold to 5fold increased antifibrinolytic function as compared to wild-type, mutant aggregates into large, insoluble complexes that can be removed by centrifugation
moe
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construction of enzyme-deficient mice by gene disruption, which is not lethal and does not cause a pathogenic phenotype, the mice show delayed wound healing, overview
P91S
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mutant exhibits specific impairment of activation by thrombin or thrombin-TM, thrombin alone, and thrombin alone or plasmin, respectively
P91S
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mutant is not activated by thrombin or by thrombin in the presence of thrombomodulin, mutant is weakly activated by plasmin, kcat (1/sec) (hippuryl-arginine, activated by plasmin): 0.00020, Km (mM) (hippuryl-arginine, activated by plasmin): 0.000007, intrinsic stability of activated TAFI (half-life): 6.3 min
R302Q
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specific activity with hippuryl-Arg is approximately half that of either recombinant wild-type enzyme or plasma derived enzymeR302Q-TAFIa is not proteolyzed by thrombin, even when 10times higher concentrations of thrombin/thrombomodulin are used
R302Q
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mutant aggregates similarly to wild-type protein
R92K
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mutant exhibits specific impairment of activation by thrombin or thrombin-TM, thrombin alone, and thrombin alone or plasmin, respectively
R92K
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mutant is not activated by thrombin, mutant is very efficiently activated by thrombin in the presence of thrombomodulin, kcat (1/sec) (p-anisylazoformyl-L-arginine, activated by thrombin in the presence of thrombomodulin): 0.215, Km (mM) (p-anisylazoformyl-L-arginine, activated by thrombin in the presence of thrombomodulin): 0.000229, mutant is activated by plasmin with similar kinetics as wild-type, kcat (1/sec) (hippuryl-arginine, activated by plasmin): 0.00039, Km (mM) (hippuryl-arginine, activated by plasmin): 0.000006, intrinsic stability of activated TAFI (half-life): 7.1 min
S90P
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mutant exhibits specific impairment of activation by thrombin or thrombin-TM, thrombin alone, and thrombin alone or plasmin, respectively
S90P
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mutant is not activated by thrombin, mutant is very efficiently activated by thrombin in the presence of thrombomodulin, kcat (1/sec) (p-anisylazoformyl-L-arginine, activated by thrombin in the presence of thrombomodulin): 0.377, Km (mM) (p-anisylazoformyl-L-arginine, activated by thrombin in the presence of thrombomodulin): 0.000162, mutant is weakly activated by plasmin, kcat (1/sec) (hippuryl-arginine, activated by plasmin): 0.00008, Km (mM) (hippuryl-arginine, activated by plasmin): 0.000009, intrinsic stability of activated TAFI (half-life): 5.5 min
T325I
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naturally occurring mutant showing a twofold increased stability compared to the wild-type enzyme
T325I
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naturally occurring polymorphism
T325I
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distribution of the Thr325Ile proCPU polymorphism in 193 patients with mucocutaneous bleeding of whom 116 are bleeders of unknown cause , and in 143 healthy, age and sex-matched controls is analyzed. ProCPU concentration is higher in women than in men, increases with age, and is significantly correlated with clot lysis time, platelet count, APTT, and PT. proCPU levels are unexpectedly higher in patients than in controls. The allele distribution of the Thr325Ile proCPU polymorphism is similar in both groups, with a low percentage of homozygous Ile/Ile
additional information
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generation of a TAFI a form with a highly stable activity by replacing a region in TAFI with the corresponding region in pancreatic CPB (carboxypeptidase B). TAFI-CPB(293-333) can be activated by thrombin-thrombomodulin, but not as efficient as wild-type TAFI. After activation, this chimeric enzyme is unstable and hardly able to prolong clot lysis of TAFI-deficient plasma. Binding of the mutant enzyme to both plasminogen and fibrinogen is normal compared to wild-type TAFI. TAFI-CPB(293-401) can be activated by thrombin-thrombomodulin, although at a lower rate compared with wild-type TAFI. The activated mutant displays a markedly prolonged half-life of 1.5 h. The chimeric enzyme does not bind plasminogen and fibrinogen and can prolong the clot lysis time in TAFI-deficient plasma, although not as efficiently as wild-type TAFI
additional information
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mutant with the fibrinogen Bbeta thrombin cleavage site Ala-Arg-Gly-His-Arg substituted into positions 91-95: activated with similar kinetics as wild-type enzyme by thrombin-thrombomodulin, activated by plasmin with the same kinetics as wild-type enzyme. Mutant enzyme with the protein C thrombin cleavage site Asp-Pro-Arg-Leu-Ile-Asp substituted into positions 90-95: no measurable activation by plasmin
additional information
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construction of chimeric proteins composed by wild-type TAFI isozymes Thr147 and Thr325, and carboxypeptidase B, CPB, fragments comprising residues 288-395 and 288-327, the chimeric mutants show increase stability and 32-34fold increased half-lives compared to the wild-type TAFI
additional information
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enzyme disorder phenotype, overview
additional information
immobilization of purified recombinnat Pro-CPU on Sepharose for specific antibody purification
additional information
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immobilization of purified recombinnat Pro-CPU on Sepharose for specific antibody purification
additional information
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the enzyme shows polymorphisms, e.g. at residue 325, genotypes, correlated diseases, overview
additional information
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circulating TAFI levels and carotid intima-media thickness (CIMT) in polycystic ovary syndrome (PCOS) patients and control subjects are analysed. Plasma TAFI levels are similarly in polycystic ovary syndrome patients compared with healthy controls. No difference is observed in the combined IMT among the studied groups
additional information
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coagulation and fibrinolytic parameters including TAFI and TFPI are assessed in patients with hypothyroidism: Factors V, VII, VIII activities, von Willebrand factor, protein C, protein S, thrombomodulin, TFPI, and TAFI are measured. Compared with the control subjects, factor VII activity, and thrombomodulin Ag and TAFI Ag levels are significantly increased in patients with hypothyroidism, whereas FV, FVIII, vWF, protein C and protein S activities, and TFPI Ag levels are significantly decreased
additional information
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HT1080 cells mediate activation of TAFI in plasma in the presence of soluble-type thrombomodulin through cell-dependent prothrombin activation. HT1080 cells stably expressing thrombomodulin (TM-HT1080) mediate plasma TAFI activation without added soluble-type thrombomodulin, wild-type cells and Mock-transfected HT1080 cells (Mock) do not. Production of TAFIa suppresses cell-mediated plasminogen activation. Cell invasion by TMHT1080 is partially enhanced by addition of a TAFIa/CPB inhibitor
additional information
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plasma TAFI and PAI-1 antigen levels are measured in pregnant women with gestational diabetes, pregnant women with normal glucose tolerance, and age-matched non-pregnant women with no history of gestational diabetes. Increased plasma TAFI antigen levels are found in pregnant women compared to non-pregnant controls. No statistically significant difference in TAFI antigen levels is observed between women with gestational diabetes and pregnant controls. Plasma PAI-1 antigen levels are higher in gestational diabetes than pregnant and non-pregnant controls
additional information
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proCPU levels in thrombophilia carriers and healthy subjects are assessed: Results show that patients with inherited thrombophilia have a tendency toward lower mean proCPU plasma levels compared to healthy controls. This difference is only significant in carriers of factor II G20210A
additional information
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TAFI activity status and the effect of L-thyroxin hormone replacement treatment on fibrinolytic system in patients with Hashimotos thyroiditis is analysed: In the control group, TAFI activity levels are 9.6 microgram/ml. In patients with L-thyroxin before and after treatment there are high levels of TAFI activity value of 14.2 and 12.9 microgram/ml, respectively. In the patient group, after L-thyroxin treatment TAFI activity levels are decreased but they are not statistically significant. When compared to the control group, high levels of TAFI activity are observed in the patient group
additional information
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the gastric intramucosal concentrations of TAFI are measured by enzyme immunoassay. This study comprises 65 patients with gastroduodenal disorders. The gastric levels of TAFI and plasminogen activator inhibitor-1 are significantly increased in patients with Helicobacter pylori compared to those without infection or cured Helicobacter pylori
additional information
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the levels of TAFI antigen and also its relationship with other hemostasis markers in a group of patients affected with polycystic ovary syndrome (PCOS)-under Diane-35 (ethinyl estradiol/cyproterone acetate) treatment or not compared with a group of healthy controls is analysed. TAFI antigen levels of groups A and B are significantly higher than in controls, but no difference is observed between them. All of the other coagulation and fibrinolysis parameters are comparable between the three groups
additional information
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variant mutants are constructed and expressed mutant variants that have key substitutions in the amino acids surrounding the scissile Arg92-Ala93 bond. Variants are identified that show patterns of resistance to specific activators. The variants that are tested also showed antifibrinolytic potentials that can be rationalized in terms of which enzymes are capable of activating them
additional information
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enzyme-deficient mice phenotype, overview
additional information
the development of immune complex-mediated glomerulonephritis in wild-type and TAFI-deficient mice is compared. After six weeks of treatment with horse spleen apoferritin and lipoplysaccharide to induce glomerulonephritis, mice deficient in TAFI have significantly better renal function as shown by lower concentrations of albumin in urine and blood urea nitrogen compared to wild-type mice. The activity of plasmin and matrix metalloproteinases is significantly increased, and mesangial matrix expansion and the deposition of collagen and fibrin in kidney tissues are significantly decreased in TAFI-knockout mice as compared to their wild-type counterparts