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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.
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...
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...
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...
Fibril-associated Collagen01:11

Fibril-associated Collagen

Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
Fibrous Proteins00:55

Fibrous Proteins

Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...

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Related Experiment Video

Updated: Jul 4, 2026

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy
06:27

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy

Published on: November 30, 2018

Polyphosphate enhances fibrin clot structure.

Stephanie A Smith1, James H Morrissey

  • 1Departments of Internal Medicine and Biochemistry, College of Medicine, University of Illinois at Urbana-Champaign, USA.

Blood
|June 12, 2008
PubMed
Summary
This summary is machine-generated.

Polyphosphate enhances fibrin clot structure, increasing turbidity and fiber thickness. This inorganic polymer also prolongs clot lysis times, suggesting a role in hemostasis and potential applications in surgical sealants.

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Leveraging Turbidity and Thromboelastography for Complementary Clot Characterization
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Leveraging Turbidity and Thromboelastography for Complementary Clot Characterization

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Last Updated: Jul 4, 2026

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy
06:27

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy

Published on: November 30, 2018

Leveraging Turbidity and Thromboelastography for Complementary Clot Characterization
06:28

Leveraging Turbidity and Thromboelastography for Complementary Clot Characterization

Published on: June 4, 2020

Area of Science:

  • Biochemistry
  • Hematology
  • Materials Science

Background:

  • Polyphosphate, a linear inorganic phosphate polymer, resides in platelet dense granules and is released upon activation.
  • Previous research identified polyphosphate as a potent hemostatic regulator, activating the contact pathway and accelerating factor V activation upstream of thrombin.

Purpose of the Study:

  • To investigate the effect of polyphosphate on fibrin clot structure and properties.
  • To determine the role of calcium and factor XIIIa in polyphosphate-mediated fibrin clot enhancement.
  • To assess the impact of polyphosphate on fibrin clot resistance to fibrinolysis.

Main Methods:

  • Formation of fibrin clots in the presence and absence of polyphosphate.
  • Measurement of clot turbidity and mass-length ratios.
  • Scanning electron microscopy (SEM) of fibrin fibers.
  • Assessment of clot lysis using plasmin and tissue plasminogen activators.

Main Results:

  • Polyphosphate significantly enhanced fibrin clot structure, leading to up to 3-fold higher turbidity and increased mass-length ratios.
  • SEM revealed thicker fibrin fibers in clots formed with polyphosphate.
  • The pro-structure effects of polyphosphate were calcium-dependent but independent of factor XIIIa activity.
  • Fibrin clots containing polyphosphate exhibited prolonged lysis times when exposed to plasmin or tPA.

Conclusions:

  • Polyphosphate modulates fibrin clot structure, promoting thicker fibers and increased turbidity.
  • Polyphosphate enhances fibrin clot resistance to fibrinolysis, potentially via its effects on clot structure.
  • The release of polyphosphate from platelets or pathogens may be crucial for regulating fibrin structure and stability.
  • Polyphosphate holds promise for improving the structural integrity of surgical fibrin sealants.