Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Extrinsic and Intrinsic Pathways of Hemostasis01:20

Extrinsic and Intrinsic Pathways of Hemostasis

10.9K
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...
10.9K
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

2.8K
Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
2.8K
Electron Transport Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

6.7K
During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
6.7K
Anticoagulant Drugs: Vitamin K Antagonists and Direct Oral Anticoagulants01:18

Anticoagulant Drugs: Vitamin K Antagonists and Direct Oral Anticoagulants

2.7K
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...
2.7K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.1K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
2.1K
Anticoagulant Drugs: Low-Molecular-Weight Heparins01:30

Anticoagulant Drugs: Low-Molecular-Weight Heparins

2.6K
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...
2.6K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Microgravity-induced transcriptional reprogramming in embryonic chicken limb bud-derived chondrogenic cultures.

Frontiers in cell and developmental biology·2026
Same author

Severe vitamin K deficiency-associated coagulopathy triggered by Clostridioides difficile infection and antibiotic-associated dysbiosis: A case report and literature review.

Infection·2026
Same author

The Hypofibrinolysis State Associated with the Dysfibrinogenemia Dusart is Mainly Related to the Altered Fibrin Clot Structure.

Hamostaseologie·2026
Same author

Venous Blood Cell Ratios as Predictors of Reperfusion Outcomes in Ischemic Stroke: A Systematic Review and Meta-analysis.

Neurology and therapy·2026
Same author

Exploring the Link Between PACAP Signalling and Hyaluronic Acid Production in Melanoma Progression.

International journal of molecular sciences·2025
Same author

[Results of the evaluation of cognitive functions in acute haemorrhagic stroke].

Neuropsychopharmacologia Hungarica : a Magyar Pszichofarmakologiai Egyesulet lapja = official journal of the Hungarian Association of Psychopharmacology·2025

Related Experiment Video

Updated: May 4, 2026

Analyzing the Interaction of Fluorescent-Labeled Proteins with Artificial Phospholipid Microvesicles using Quantitative Flow Cytometry
08:26

Analyzing the Interaction of Fluorescent-Labeled Proteins with Artificial Phospholipid Microvesicles using Quantitative Flow Cytometry

Published on: April 6, 2022

1.9K

Interaction of factor XIII subunits.

Eva Katona1, Krisztina Pénzes, Andrea Csapó

  • 1Clinical Research Center, University of Debrecen, Medical and Health Science Center, Debrecen, Hungary; and.

Blood
|January 11, 2014
PubMed
Summary

Coagulation factor XIII (FXIII) interaction reveals that FXIII-A2 is mostly bound to FXIII-B in plasma but largely free in other bodily fluids. Free FXIII-A2 is active and can cross-link fibrin.

More Related Videos

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

19.9K
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

11.7K

Related Experiment Videos

Last Updated: May 4, 2026

Analyzing the Interaction of Fluorescent-Labeled Proteins with Artificial Phospholipid Microvesicles using Quantitative Flow Cytometry
08:26

Analyzing the Interaction of Fluorescent-Labeled Proteins with Artificial Phospholipid Microvesicles using Quantitative Flow Cytometry

Published on: April 6, 2022

1.9K
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

19.9K
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

11.7K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Hematology

Background:

  • Coagulation factor XIII (FXIII) is a heterotetramer composed of catalytic FXIII-A2 and protective FXIII-B2 subunits.
  • FXIII-B subunits, with 10 sushi domains, extend the circulation time of FXIII-A2 and prevent premature activation.
  • Understanding the subunit interaction is crucial for FXIII function in hemostasis.

Purpose of the Study:

  • To investigate the biochemical interaction between FXIII-A2 and FXIII-B subunits.
  • To quantify the free FXIII-A2 in different biological fluids.
  • To identify the binding site of FXIII-B involved in subunit interaction.

Main Methods:

  • Surface plasmon resonance (SPR) to determine the equilibrium dissociation constant (Kd).
  • Enzyme-linked immunosorbent assay (ELISA)-type binding assays.
  • Plasma immunodepletion to isolate free FXIII-A2.
  • Epitope mapping using monoclonal antibodies and recombinant FXIII-B domains.

Main Results:

  • The equilibrium dissociation constant (Kd) for FXIII subunit interaction is in the range of 10(-10) M.
  • Approximately 1% of FXIII-A2 is free in plasma, confirmed by immunodepletion experiments.
  • In cerebrospinal fluid and tears, over 80% of FXIII-A2 exists in a free form.
  • An antibody inhibiting FXIII subunit interaction binds to the first and second sushi domains of FXIII-B, with the epitope at positions 96-103.

Conclusions:

  • FXIII-A2 is predominantly complexed with FXIII-B in plasma but largely exists as free, active FXIII-A2 in lower concentration fluids like CSF and tears.
  • Free FXIII-A2 retains its functional activity, capable of fibrin cross-linking upon activation.
  • The N-terminal sushi domains of FXIII-B are critical for binding FXIII-A2.