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Related Concept Videos

Anticoagulant Drugs: Low-Molecular-Weight Heparins01:30

Anticoagulant Drugs: Low-Molecular-Weight Heparins

Hemostasis is a crucial process that prevents excessive blood loss from damaged blood vessels. It involves various mechanisms such as vasoconstriction, platelet adhesion and activation, and fibrin formation. The importance of each mechanism depends on the type of vessel injury. In contrast, thrombosis is the abnormal formation of a blood clot within the blood vessels, leading to potential complications if the clot obstructs blood flow. Thrombosis can be caused by increased coagulability of the...
Anticoagulant Drugs: Vitamin K Antagonists and Direct Oral Anticoagulants01:18

Anticoagulant Drugs: Vitamin K Antagonists and Direct Oral Anticoagulants

Oral anticoagulants are vital tools in preventing and treating blood clotting disorders. This diverse class of medications can be categorized as vitamin K antagonists, exemplified by warfarin, and direct thrombin inhibitors (DTIs), such as dabigatran, as well as factor Xa inhibitors, including rivaroxaban.
Warfarin, a prominent vitamin K antagonist family member, exerts its effect by inhibiting the enzyme VKORC1 (vitamin K epoxide reductase complex 1). By hindering this enzyme, warfarin...
Extrinsic and Intrinsic Pathways of Hemostasis01:20

Extrinsic and Intrinsic Pathways of Hemostasis

Blood clotting or coagulation involves extrinsic and intrinsic pathways, which ultimately merge into the common pathway, forming a fibrin clot.
The Extrinsic Pathway
The extrinsic pathway of coagulation is typically initiated by tissue damage that exposes blood to tissue factor (TF), a protein released by the damaged tissue cells outside the blood vessels—this interaction with TF triggers biochemical reactions involving specific clotting factors. The key player here is Factor VII, which forms a...
Venous Thrombosis III: Interprofessional Care01:29

Venous Thrombosis III: Interprofessional Care

Venous thrombosis requires effective prevention and treatment strategies to improve patient outcomes and reduce potential complications.Prevention StrategiesHealthcare providers must prioritize preventing venous thromboembolism (VTE) for all adult patients upon admission. Interventions depend on bleeding and thrombosis risk, medical history, current medications, diagnoses, planned procedures, and patient preferences. Patients on bed rest should change positions every two hours and, if not...
Disorders of Hemostasis01:24

Disorders of Hemostasis

Hemostasis, the process that stops bleeding after a blood vessel injury, is crucial for maintaining the integrity of the circulatory system. However, disorders of hemostasis can disrupt this delicate balance, leading to either excessive clotting or bleeding. These disorders can be broadly classified into thromboembolic disorders and bleeding disorders.
Thromboembolic Disorders
Two factors primarily cause thromboembolic conditions.
Coagulation01:09

Coagulation

The coagulation phase is a critical part of the body's process to prevent blood loss following injury to blood vessels. It involves chemical reactions that form a clot to seal the injured area. The clotting process begins shortly after injury, within 15-20 seconds for severe damage and 1-2 minutes for minor injuries.
During the coagulation phase, clotting factors, or procoagulants, play a vital role in initiating and progressing the coagulation cascade. This cascade is a series of reactions...

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Related Experiment Video

Updated: Jun 19, 2026

Measurement of Factor V Activity in Human Plasma Using a Microplate Coagulation Assay
13:08

Measurement of Factor V Activity in Human Plasma Using a Microplate Coagulation Assay

Published on: September 9, 2012

Coagulation factor XIII variants with altered thrombin activation rates.

Mette Dahl Andersen1, Marianne Kjalke, Susanne Bang

  • 1Biopharmaceutical Research Unit, Novo Nordisk A/S, Novo Nordisk Park, DK-2760 Måløv, Denmark.

Biological Chemistry
|October 7, 2009
PubMed
Summary

Coagulation factor XIII (FXIII) variants can be engineered for enhanced clot stability. Modifying the FXIII-A activation peptide, particularly with an optimal thrombin cleavage site, significantly boosts clot resistance to breakdown.

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Last Updated: Jun 19, 2026

Measurement of Factor V Activity in Human Plasma Using a Microplate Coagulation Assay
13:08

Measurement of Factor V Activity in Human Plasma Using a Microplate Coagulation Assay

Published on: September 9, 2012

The Nijmegen Hemostasis Assay: Simultaneous Fluorogenic Measurement of Thrombin and Plasmin Generation in a Single Well
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The Nijmegen Hemostasis Assay: Simultaneous Fluorogenic Measurement of Thrombin and Plasmin Generation in a Single Well

Published on: February 27, 2026

Helical Organization of Blood Coagulation Factor VIII on Lipid Nanotubes
12:24

Helical Organization of Blood Coagulation Factor VIII on Lipid Nanotubes

Published on: June 3, 2014

Area of Science:

  • Biochemistry
  • Hematology
  • Molecular Biology

Background:

  • Coagulation factor XIII (FXIII) stabilizes fibrin clots by catalyzing crosslinking.
  • The V34L polymorphism in FXIII-A affects activation kinetics and clot properties.
  • Understanding FXIII-A activation is crucial for hemostasis research.

Purpose of the Study:

  • To investigate the impact of engineered FXIII-A activation peptides on clot formation and stability.
  • To explore the potential of modifying FXIII-A activation rates for improved hemostatic function.

Main Methods:

  • Generation of FXIII-A variants with modified activation peptides.
  • Assays to measure FXIII-A activation rates by thrombin.
  • Analysis of fibrin network formation and resistance to fibrinolysis.

Main Results:

  • The V34L polymorphism enhances FXIII-A activation and promotes tighter clots at lower fibrinogen levels.
  • An engineered FXIII-A variant (V34L+V35T) with an optimal thrombin cleavage site showed a 7.6-fold increased activation rate.
  • This engineered variant formed fibrin networks more resistant to fibrinolysis compared to wild-type FXIII-A.
  • Introducing fibrinopeptide A fragments severely impaired FXIII-A activation.

Conclusions:

  • FXIII-A activation peptide engineering can significantly modulate clot properties.
  • Optimized thrombin cleavage sites enhance FXIII-A activation and fibrin clot resistance to fibrinolysis.
  • These findings offer insights into potential therapeutic strategies for bleeding disorders.