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

Clot Retraction and Fibrinolysis01:16

Clot Retraction and Fibrinolysis

After a fibrin clot is formed, the next step is clot retraction, a vital process facilitated by platelet contractile proteins, such as actin and myosin. These proteins pull the fibrin strands closer together and condense the clot. This action reduces the size of the clot, creating a smaller, denser structure that effectively seals off the damaged vessel. Clot retraction consolidates the clot and helps with wound healing by bringing the edges of the damaged blood vessel closer together.
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...
Formation of the Platelet Plug01:22

Formation of the Platelet Plug

The platelet phase, the second stage of hemostasis, commences around 15-20 seconds after an injury. It follows and overlaps with the vascular phase, during which blood vessels constrict to minimize blood loss.
As the injured blood vessel contracts, endothelial cells undergo contraction, revealing collagen fibers in the basement membrane and underlying connective tissue. Furthermore, the plasma membrane of endothelial cells becomes adhesive, preparing the site for platelet adhesion. Platelets...
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...
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

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...
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...

You might also read

Related Articles

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

Sort by
Same author

How much Copper Do Calves Need? Retention and Hepatic Storage in Artificially Reared Milk-Fed Holstein-Friesian Calves.

Biological trace element research·2026
Same author

Prothrombinase processivity is conferred by substrate allostery.

The EMBO journal·2026
Same author

Engineering a membrane-independent human prothrombinase through parsimonious mutation of factor Xa.

Journal of thrombosis and haemostasis : JTH·2025
Same author

A 3.3-Ă… cryo-EM structure of an engineered high-affinity human prothrombinase complex.

Blood·2025
Same author

The rumen microbiota and metabolism of dairy cows are affected by the dietary rate of inclusion of <i>Yucca schidigera</i> extract.

Microbiology spectrum·2025
Same author

The preclinical profile of SerpinPC: a potential new treatment for hemophilia.

Blood advances·2025
Same journal

Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

Molecular Basis of Disease Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

General Subjects Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

Erratum to 'on the role of exchangeable hydrogen bonds for the kinetics of P680<sup>+·</sup> Q<sub>A</sub> <sup>-·</sup> formation and P680<sup>+·</sup> Pheo<sup>-·</sup> recombination in photosystem II' [Biochim. Biophys. Acta 1276 (1996) 35-44].

Biochimica et biophysica acta·2019
Same journal

Oligomeric state of the light-harvesting complexes B800-850 and B875 from purple bacterium Rubrivivax gelatinosus in detergent solution.

Biochimica et biophysica acta·2019
Same journal

Regulation of pigment content and enzyme activity in the cyanobacterium Nostoc sp. Mac grown in continuous light, a light-dark photoperiod, or darkness.

Biochimica et biophysica acta·2019
See all related articles

Related Experiment Video

Updated: May 30, 2026

The Nijmegen Hemostasis Assay: Simultaneous Fluorogenic Measurement of Thrombin and Plasmin Generation in a Single Well
08:01

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

Published on: February 27, 2026

Thrombin plasticity.

James A Huntington1

  • 1Department of Haematology, University of Cambridge, Cambridge Institute for Medical Research, Wellcome Trust/MRC Building, Cambridge, UK. jah52@cam.ac.uk

Biochimica Et Biophysica Acta
|July 26, 2011
PubMed
Summary
This summary is machine-generated.

Thrombin, a key protease in blood clotting, exhibits inherent flexibility influencing its activity and specificity. This plasticity offers a new framework for understanding enzyme regulation in hemostasis.

More Related Videos

Tracking Fibrinolysis of Chandler Loop-Formed Whole Blood Clots Under Shear Flow in An In-Vitro Thrombolysis Model
06:16

Tracking Fibrinolysis of Chandler Loop-Formed Whole Blood Clots Under Shear Flow in An In-Vitro Thrombolysis Model

Published on: April 19, 2024

RNA-seq Analysis of Transcriptomes in Thrombin-treated and Control Human Pulmonary Microvascular Endothelial Cells
18:30

RNA-seq Analysis of Transcriptomes in Thrombin-treated and Control Human Pulmonary Microvascular Endothelial Cells

Published on: February 13, 2013

Related Experiment Videos

Last Updated: May 30, 2026

The Nijmegen Hemostasis Assay: Simultaneous Fluorogenic Measurement of Thrombin and Plasmin Generation in a Single Well
08:01

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

Published on: February 27, 2026

Tracking Fibrinolysis of Chandler Loop-Formed Whole Blood Clots Under Shear Flow in An In-Vitro Thrombolysis Model
06:16

Tracking Fibrinolysis of Chandler Loop-Formed Whole Blood Clots Under Shear Flow in An In-Vitro Thrombolysis Model

Published on: April 19, 2024

RNA-seq Analysis of Transcriptomes in Thrombin-treated and Control Human Pulmonary Microvascular Endothelial Cells
18:30

RNA-seq Analysis of Transcriptomes in Thrombin-treated and Control Human Pulmonary Microvascular Endothelial Cells

Published on: February 13, 2013

Area of Science:

  • Biochemistry
  • Hematology
  • Enzymology

Background:

  • Thrombin is the terminal protease in the blood coagulation cascade.
  • It plays crucial roles in both pro-coagulant and anti-coagulant functions.
  • Understanding thrombin's regulation is vital for maintaining hemostatic balance.

Purpose of the Study:

  • To review the role of conformational changes in thrombin specificity.
  • To discuss the impact of inherent flexibility on thrombin activity.
  • To present a new conceptual framework for enzyme regulation.

Main Methods:

  • Review of existing literature on thrombin structure and function.
  • Analysis of studies on enzyme allostery and conformational transitions.
  • Discussion of thrombin's flexibility in the context of zymogen-to-protease transition.

Main Results:

  • Thrombin exists in multiple conformations, affecting its activity and specificity.
  • Recent findings highlight inherent flexibility in unliganded thrombin.
  • This flexibility influences enzyme activity and substrate recognition.

Conclusions:

  • Thrombin's inherent flexibility, termed 'plasticity,' is central to its function.
  • This concept provides a novel framework for understanding enzyme activity regulation.
  • Further research into thrombin plasticity can advance knowledge of hemostasis and enzyme function.