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Related Concept Videos

Complement System01:27

Complement System

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The complement system is a group of approximately 20 plasma proteins that strengthen the body's defenses against infections through opsonization, inflammation, and cell lysis. Opsonization involves coating pathogens with complement proteins, making them more recognizable and facilitating phagocyte engulfment. Certain complement proteins induce inflammation that attracts immune cells to the site of infection. Cell lysis involves the destruction of pathogens through the formation of a...
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Anticoagulant Drugs: Low-Molecular-Weight Heparins01:30

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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...
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Clot Retraction and Fibrinolysis01:16

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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.
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Extrinsic and Intrinsic Pathways of Hemostasis01:20

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Blood clotting or coagulation involves extrinsic and intrinsic pathways, which ultimately merge into the common pathway, forming a fibrin clot.
The Extrinsic Pathway
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Disorders of Hemostasis01:24

Disorders of Hemostasis

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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.
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Coagulation01:09

Coagulation

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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: Mar 16, 2026

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

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Thrombomodulin enhances complement regulation through strong affinity interactions with factor H and C3b-Factor H

M Heurich1, R J S Preston2, V B O'Donnell1

  • 1Division of Infection & Immunity and Systems Immunity Research Institute, School of Medicine, Cardiff University, Heath Park, Cardiff CF14 4XN, United Kingdom.

Thrombosis Research
|August 12, 2016
PubMed
Summary

Thrombomodulin (TM) binds complement proteins Factor H (FH) and C3b, inhibiting complement activation. This study quanties TM

Keywords:
ComplementHemolytic assaySurface plasmon resonanceThrombomodulin

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Area of Science:

  • Biochemistry
  • Immunology
  • Molecular Biology

Background:

  • Coagulation and complement systems are activated concurrently at tissue injury sites, generating thrombin and C3b.
  • Thrombomodulin (TM) regulates thrombin and enhances complement factor H (FH) activity, promoting C3b degradation.
  • Understanding TM's interaction with complement proteins is crucial for its regulatory role in inflammation and thrombosis.

Purpose of the Study:

  • To determine the biophysical interaction affinities of recombinant TM analogs with thrombin, FH, and C3b.
  • To analyze the ability of TM analogs to regulate serum complement activity.
  • To investigate the mechanisms by which TM influences complement activation.

Main Methods:

  • Surface plasmon resonance (SPR) was employed to measure binding affinities of TM analogs to FH, C3b, and thrombin.
  • Complement hemolytic activity assays were performed to assess the regulatory capacity of TM analogs in serum.
  • Standardized assays were used to ensure reproducibility and comparability of results.

Main Results:

  • TM analogs demonstrated nanomolar affinity for FH and C3b-FH complex, and micromolar affinity for C3b.
  • Binding affinity of TM analogs for thrombin was significantly higher than for FH.
  • At physiological concentrations, TM inhibited serum complement hemolytic activity through both FH-dependent and independent pathways.

Conclusions:

  • TM exhibits significant binding affinity for complement proteins FH and the C3b-FH complex.
  • Soluble TM effectively inhibits complement activation in serum at physiologically relevant concentrations.
  • TM's dual role in regulating both coagulation and complement systems highlights its therapeutic potential.