Thrombin Activity Is Unaltered by N-Terminal Truncation of Factor XIII Activation Peptides†

Biochemistry ◽  
2004 ◽  
Vol 43 (14) ◽  
pp. 4150-4159 ◽  
Author(s):  
Giulia Isetti ◽  
Muriel C. Maurer
Keyword(s):  
Factor Xiii ◽  
Thrombin Activity ◽  
Activation Peptides

scholarly journals Design of Factor XIII V34X activation peptides to control ability to interact with thrombin mutants

2011 ◽  
Vol 1814 (12) ◽  
pp. 1955-1963 ◽  
Author(s):  
Madhavi A. Jadhav ◽  
R. Cory Lucas ◽  
Whitney N. Goldsberry ◽  
Muriel C. Maurer
Keyword(s):  
Factor Xiii ◽  
Activation Peptides

scholarly journals Screening cleavage of Factor XIII V34X Activation Peptides by thrombin mutants: A strategy for controlling fibrin architecture

2017 ◽  
Vol 1865 (10) ◽  
pp. 1246-1254 ◽  
Author(s):  
Madhavi A. Jadhav ◽  
Whitney N. Goldsberry ◽  
Sara E. Zink ◽  
Kelsey N. Lamb ◽  
Katelyn E. Simmons ◽  
...  
Keyword(s):  
Factor Xiii ◽  
Activation Peptides

Intracranial Hemorrhage in Systemic Lupus Erythematosus Associated with an Autoantibody against Factor XIII

2002 ◽  
Vol 88 (12) ◽  
pp. 919-923 ◽  
Author(s):  
Pauline Velasco ◽  
John Hill ◽  
Karen Hoffmeister ◽  
Fredric Kaye ◽  
Laszlo Lorand
Keyword(s):  
Systemic Lupus Erythematosus ◽  
Family History ◽  
Conformational Change ◽  
Young Woman ◽  
Intracranial Hemorrhage ◽  
Lupus Erythematosus ◽  
Factor Xiii ◽  
Systemic Lupus ◽  
History Of ◽  
Activation Peptides

SummaryIntracranial hemorrhage in a young woman with systemic lupus erythematosus necessitated two surgical evacuations. In the absence of a family history of bleeding, clot solubility in urea suggested a factor XIII (FXIII) inhibitor. The patient’s IgG bound well to the virgin and the thrombin-modified zymogen ensemble (A2B2 and A2’B2) and to the free rA2 but reacted poorly with the thrombin-modified rA2’. Since the IgG did not block the thrombin-catalyzed proteolysis of A subunits nor the dissociation of the A2’B2, its action might be to interfere with the release of activation peptides from the thrombincleaved zymogen, hindering the conformational change necessary for generating FXIIIa.Treatment with cryoprecipitate and cyclophosphamide arrested the hemorrhage and almost neutralized the antibody so that the patient’s clot became insoluble in urea and showed a close to normally cross-linked γ-γ and αn fibrin chain profile. Nevertheless, she still has detectable anti-FXIII antibody and may be at risk for hemorrhage.

Impaired inactivation by antithrombin and hirudin and preserved fibrinogen-clotting activity of thrombin in complex with antithrombin antibody from a patient with antiphospholipid syndrome

2005 ◽  
Vol 94 (07) ◽  
pp. 82-87 ◽  
Author(s):  
István Léránt ◽  
Judit Skopál ◽  
Anna Kelemen ◽  
Zoltán Nagy ◽  
Raymund Machovich ◽  
...  
Keyword(s):  
Protective Effect ◽  
Blood Plasma ◽  
Antiphospholipid Syndrome ◽  
Immunoglobulin G ◽  
Factor Xiii ◽  
Protein C ◽  
Amidolytic Activity ◽  
Fab Fragment ◽  
Thrombin Activity ◽  
Activation Assay

SummaryImmunoglobulin G (IgG) isolated from the blood plasma of a patient with secondary antiphospholipid syndrome (APS) expresses fibrinogen-clotting and amidolytic activity (the thrombin activity in 20 μmole IgG is equivalent to approximately 5 nmole pure thrombin), and activates factor XIII. Hirudin (1 μM) decreases the intrinsic thrombin activity of the APS IgG by only 25%, whereas it inhibits completely pure thrombin with equivalent activity. Under conditions, when antithrombin inactivates 60% of the thrombin activity in the presence of normal IgG, the APS IgG protects almost completely the added thrombin against inactivation by antithrombin. Heparin, however, partially relieves this protective effect and at the same time it facilitates the inhibition of the intrinsic thrombin activity by antithrombin. The APS IgG reduces the thrombin activity in protein C activation assay by 50% compared to the activity in the presence of normal IgG. All described properties are related to the Fab fragment of the antibody. The IgG preserving the fibrin-generating activity of thrombin with concomitant protection against inhibitors unravels a new aspect of the thrombotic mechanism in APS. This condition is probably rare: only one out of 23 examined patients with primary or secondary APS expresses IgG with the described properties.

Radiolabeled r-Hirudin as a Measure of Thrombin Activity at, or within, the Rabbit Aorta Wall In Vitro and In Vivo

1994 ◽  
Vol 71 (04) ◽  
pp. 499-506 ◽  
Author(s):  
Mark W C Hatton ◽  
Bonnie Ross-Ouellet
Keyword(s):  
Rabbit Aorta ◽  
Balloon Injury ◽  
Recombinant Hirudin ◽  
Aorta Wall ◽  
Thrombin Activity ◽  
Before And After ◽  
The Matrix

SummaryThe behavior of 125I-labeled recombinant hirudin towards the uninjured and de-endothelialized rabbit aorta wall has been studied in vitro and in vivo to determine its usefulness as an indicator of thrombin activity associated with the aorta wall. Thrombin adsorbed to either sulfopropyl-Sephadex or heparin-Sepharose bound >95% of 125I-r-hirudin and the complex remained bound to the matrix. Binding of 125I-r-hirudin to the exposed aorta subendothelium (intima-media) in vitro was increased substantially if the tissue was pre-treated with thrombin; the quantity of l25I-r-hirudin bound to the de-endothelialized intima-media (i.e. balloon-injured in vitro) correlated positively with the quantity of bound 131I-thrombin (p <0.01). Aortas balloon-injured in vivo were measured for thrombin release from, and binding of 125I-r-hirudin to, the de-endothelialized intimal surface in vitro; 125I-r-hirudin binding correlated with the amount of active thrombin released (p <0.001). Uptake of 125I-r-hirudin by the aorta wall in vivo was proportional to the uptake of 131I-fibrinogen (as an indicator of thrombin activity) before and after balloon injury. After 30 min in the circulation, specific 125I-r-hirudin binding to the uninjured and de-endo- thelialized (at 1.5 h after injury) aorta wall was equivalent to 3.4 (± 2.5) and 25.6 (±18.1) fmol of thrombin/cm2 of intima-media, respectively. Possibly, only hirudin-accessible, glycosaminoglycan-bound thrombin is measured in this way.

Plasminogen-Plasmin System IX. Specific Binding of Tranexamic Acid to Plasmin

1975 ◽  
Vol 33 (03) ◽  
pp. 573-585 ◽  
Author(s):  
Masahiro Iwamoto
Keyword(s):  
Tranexamic Acid ◽  
Affinity Chromatography ◽  
Dissociation Constant ◽  
Factor Xiii ◽  
Specific Binding ◽  
The Other ◽  
Inhibitory Mechanism ◽  
Binding Studies ◽  
Similar Affinity ◽  
Fibrin Structure

SummaryInteractions between tranexamic acid and protein were studied in respect of the antifibrinolytic actions of tranexamic acid. Tranexamic acid did neither show any interaction with fibrinogen or fibrin, nor was incorporated into cross-linked fibrin structure by the action of factor XIII. On the other hand, tranexamic acid bound to human plasmin with a dissociation constant of 3.5 × 10−5 M, which was very close to the inhibition constant (3.6 × 10−5 M) for this compound in inhibiting plasmin-induced fibrinolysis. The binding site of tranexamic acid on plasmin was not the catalytic site of plasmin, because TLCK-blocked plasmin also showed a similar affinity to tranexamic acid (the dissociation constant, 2.9–4.8 × 10−5 M).In the binding studies with the highly purified plasminogen and TLCK-plasmin preparations which were obtained by affinity chromatography on lysine-substituted Sepharose, the molar binding ratio was shown to be 1.5–1.6 moles tranexamic acid per one mole protein.On the basis of these and other findings, a model for the inhibitory mechanism of tranexamic acid is presented.

New Families with Hereditary Hemorrhagic Trait due to Deficiency of Fibrin Stabilizing Factor (F. XIII)

1968 ◽  
Vol 20 (03/04) ◽  
pp. 534-541 ◽  
Author(s):  
O Egeberg
Keyword(s):  
Factor Xiii ◽  
Family Members ◽  
Recessive Inheritance ◽  
Factor Xiii Deficiency ◽  
History Of ◽  
Congenital Factor

SummarySevere hemorrhagic disorder due to congenital factor XIII deficiency is described in two unrelated Norwegian girls.Plasma cephalin time was for both patients extraordinarily short during episodes of bleeding and hematomas. No such hyperactivity reaction was demonstrable in unaffected condition some months later.Estimations of blood factor XIII levels revealed a partial defect in the parents of both children, and also in some other family members, consistent with an autosomal incompletely recessive inheritance of the defect. Some of the presumptive heterozygotes had a history of light bleeding phenomenons; whether this was related to their partial lack of factor XIII is so far uncertain.

Plasma Factor XIII and Platelet Factor XIII in Hyperlipaemia

1976 ◽  
Vol 36 (03) ◽  
pp. 542-550 ◽  
Author(s):  
Mircea P. Cucuianu ◽  
K Miloszewski ◽  
D Porutiu ◽  
M. S Losowsky
Keyword(s):  
Factor Xiii ◽  
Significant Contribution ◽  
Quantitative Assay ◽  
Factor Xii ◽  
Platelet Factor ◽  
Type Iv ◽  
Plasma Factor ◽  
Hepatic Synthesis

SummaryPlasma factor XIII activity measured by a quantitative assay was found to be significantly higher in hypertriglyceridaemic patients (type IV and combined hyperlipoproteinaemia), as compared to normolipaemic controls. No such elevation in plasma factor XIII activity was found in patients with type IIa hyperlipaemia. Plasma pseudocholinesterase was found to parallel the elevated factor XIII activity in hypertriglyceridaemic subjects.In contrast, platelet factor XIII activity was not raised in hyperlipaemic subjects, and plasma factor XIII was found to be normal in a normolipaemic subject with throm-bocythaemia.It was concluded that there is no significant contribution from platelets to plasma factor XIII activity, and that the observed increase in plasma factor XII in hypertriglyceridaemia results from enhanced hepatic synthesis of the enzyme.

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