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Related Concept Videos

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...
Structure and Function of Platelets01:18

Structure and Function of Platelets

The cell fragments known as platelets are disc-shaped, with an average diameter of about 3 μm and a thickness of roughly 1 μm. They play a crucial role in the body's vascular clotting system, which also involves plasma proteins, blood cells, and blood vessel tissues.
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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...
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...
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Cytoskeletal Linker Proteins - Plakins

Plakins are large proteins with binding domains for microtubules, microfilaments, intermediate filaments, and membrane-associated protein complexes at cell junctions. Plakin functions are evolutionarily conserved and are primarily involved in organizing the different components of the cytoskeleton by crosslinking them to each other and connecting them to the cell-matrix and cell adhesion complexes. They are also known to interact with signal transducers, serve as scaffolds for signaling...

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Related Experiment Video

Updated: Jul 11, 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

The factor VIII C1 domain contributes to platelet binding.

Ting-Chang Hsu1, Kathleen P Pratt, Arthur R Thompson

  • 1Puget Sound Blood Center, 921 Terry Ave, Seattle, WA 98104-1256, USA.

Blood
|October 6, 2007
PubMed
Summary

The C1 domain of activated factor VIII (FVIIIa) enhances binding to activated platelets, increasing affinity beyond the C2 domain alone. This finding clarifies FVIIIa

Area of Science:

  • Hematology
  • Biochemistry
  • Molecular Biology

Background:

  • Activated factor VIII (FVIIIa) is crucial for blood coagulation, forming a complex with factor IXa on negatively charged membranes like activated platelets.
  • Membrane attachment of FVIIIa is primarily attributed to its C2 domain, but the role of the adjacent C1 domain remains unclear.

Purpose of the Study:

  • To investigate the contribution of the FVIII C1 domain to the binding of FVIIIa to activated platelets.
  • To compare the binding characteristics of FVIII C1C2 and C2 domains to platelet surfaces.

Main Methods:

  • Flow cytometry was used to detect the binding of recombinant FVIII C1C2 and C2 proteins to platelets.
  • Proteins were labeled with fluorescein for highest binding and lowest background detection.

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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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Last Updated: Jul 11, 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

Investigating von Willebrand Factor Pathophysiology Using a Flow Chamber Model of von Willebrand Factor-platelet String Formation
08:30

Investigating von Willebrand Factor Pathophysiology Using a Flow Chamber Model of von Willebrand Factor-platelet String Formation

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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

  • Binding affinities and site numbers were estimated using fluorescent microbeads and competition assays with antibodies and FVIIIa.

    • Main Results:

    • Over 90% of activated platelets bound C1C2, compared to approximately 50% for C2.
    • C1C2 exhibited significantly more binding sites per platelet (approx. 7,000) than C2 (approx. 1,400).
    • C1C2 binding was partially inhibited by excess C2, suggesting a distinct binding contribution from the C1 domain.

    Conclusions:

    • The FVIII C1 domain significantly contributes to the binding affinity of FVIIIa to activated platelets.
    • This enhanced binding is independent of von Willebrand factor and distinct from C2-mediated interactions.
    • Understanding the C1 domain's role provides new insights into FVIIIa function in hemostasis.