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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.
Formation of Intermediate Filaments00:57

Formation of Intermediate Filaments

Intermediate filaments are cytoskeletal proteins with higher tensile strength and flexibility than microfilaments and microtubules. Unlike the other two cytoskeletal proteins, intermediate filament formation lacks the enzymatic activity to hydrolyze nucleotides like ATP and GTP to generate energy for polymerization. Therefore, the formation of intermediate filaments is multistep self-assembly. The involvement of any accessory proteins in intermediate filament formation has not yet been reported.
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...
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...
Fibronectins Connect Cells with ECM01:25

Fibronectins Connect Cells with ECM

Fibronectin is an adhesive glycoprotein present in the extracellular matrix of embryogenic and adult tissue. These molecules primarily aid in regulating cell motility and attachment. A fibronectin molecule is composed of two identical polypeptide chains attached to each other by a pair of disulfide bonds at the C-terminal.
Both proteoglycans and collagen are attached to fibronectin proteins, which, in turn, are attached to integrin proteins. These integrin proteins interact with transmembrane...
Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...

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Related Experiment Video

Updated: Jun 27, 2026

Engineering Fibrin-based Tissue Constructs from Myofibroblasts and Application of Constraints and Strain to Induce Cell and Collagen Reorganization
12:13

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Ultrathin self-assembled fibrin sheets.

E Tim O'Brien1, Michael R Falvo, Daniel Millard

  • 1Department of Physics and Astronomy, University of North Carolina, Chapel Hill, NC 27599-3255, USA. etobrien@email.unc.edu

Proceedings of the National Academy of Sciences of the United States of America
|December 5, 2008
PubMed
Summary

Fibrin can form thin, 2D sheets, not just fibers. These novel fibrin sheets may play an unexpected role in blood clot formation and adhesion.

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Area of Science:

  • Biochemistry and Biophysics
  • Materials Science
  • Hematology

Background:

  • Fibrin is the primary structural component of blood clots and thrombi, forming a fibrous network.
  • Previous research has focused on fibrin fiber polymerization, overlooking other potential structures.

Purpose of the Study:

  • To investigate the spontaneous polymerization of fibrin into alternative structures.
  • To characterize the physical and mechanical properties of these novel fibrin structures.
  • To explore the potential role of these structures in fibrin clot formation.

Main Methods:

  • Polymerization of fibrinogen and thrombin in physiologic buffers under controlled low concentrations.
  • Utilized micro-patterned surfaces and a combined fluorescence/atomic force microscope system for detection and characterization.
  • Employed video microscopy and various electron microscopy techniques (fluorescence, transmission, scanning) to observe assembly and structural transitions.

Main Results:

  • Demonstrated spontaneous polymerization of fibrin into extensive, molecularly thin, 2D sheets across three species.
  • Characterized sheets as approximately 5 nm thick, flat, elastic, and mechanically continuous.
  • Observed rapid sheet assembly and structural transitions into fibers, including folding, rolling, and hole formation.

Conclusions:

  • Fibrin 2D sheets represent a previously unrecognized structural form of fibrin polymerization.
  • These sheets exhibit unique assembly dynamics and mechanical properties, potentially influencing clot structure and function.
  • A new model of fibrin fiber formation involving sheet intermediates is proposed, challenging existing polymerization theories.