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Related Concept Videos

Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin networks...
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.
Cell-matrix's Response to Mechanical Forces01:13

Cell-matrix's Response to Mechanical Forces

In animal cells, the extracellular matrix allows cells within tissues to withstand external stresses and transmits signals from the outside of the cell to the inside. The extracellular matrix is extensive, and its composition varies between different types of tissues. For example, the reticular fibers and ground substance make up the ECM in loose connective tissue, while collagen and bone minerals make up the ECM of bone tissue. 
Anchoring junctions mechanically attach a cell to the...
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...
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...
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...

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Related Experiment Video

Updated: Jul 14, 2026

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

Published on: October 28, 2013

Strain-Driven Topological Reorganization in Soft Fibrin Nanofibrous Networks Enabling Tissue-Like Alignment.

Mao Mao1,2, Rongzhi Liu1,2, Zhishuo Ren1,2

  • 1State Key Laboratory For Manufacturing Systems Engineering, Xi'an Jiaotong University, Xi'an, People's Republic of China.

Advanced Materials (Deerfield Beach, Fla.)
|July 13, 2026
PubMed
Summary

Researchers developed a new method to align nanofibers in soft tissues by stretching them during gel formation. This technique improves cell organization and tissue function for applications in tissue engineering.

Keywords:
alignmentcardiac tissue engineeringfibrous hydrogelstrain

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Last Updated: Jul 14, 2026

Engineering Fibrin-based Tissue Constructs from Myofibroblasts and Application of Constraints and Strain to Induce Cell and Collagen Reorganization
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Published on: October 28, 2013

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Microengineering 3D Collagen Hydrogels with Long-Range Fiber Alignment
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Microengineering 3D Collagen Hydrogels with Long-Range Fiber Alignment

Published on: September 7, 2022

Area of Science:

  • Biomaterials Science
  • Tissue Engineering
  • Soft Matter Physics

Background:

  • Creating aligned nanofibrous matrices in soft, cell-laden materials is difficult.
  • Existing alignment methods often use external templates or non-physiological fields.
  • Controlling anisotropy in fibrin matrices is crucial for tissue engineering applications.

Purpose of the Study:

  • To develop a gelation-coupled, strain-induced alignment strategy for fibrin matrices.
  • To investigate the mechanism of strain-induced fibril reorientation and pore elongation.
  • To evaluate the impact of aligned matrices on cardiomyocyte function.

Main Methods:

  • Applied uniaxial deformation during the fibrillogenesis window of partially crosslinked fibrin.
  • Utilized structural and rheological analyses to characterize matrix properties.
  • Developed a simplified pore-straightening model to explain alignment behavior.

Main Results:

  • Achieved stable anisotropy in fibrin matrices through gelation-stage mechanical reorganization.
  • Observed rapid fibril reorientation and pore elongation along the strain direction, saturating near 1.6× elongation.
  • Demonstrated improved cardiomyocyte structural organization, anisotropic contraction, and electrical responsiveness in aligned matrices.

Conclusions:

  • Strain-guided mechanical reorganization during gelation is an effective strategy for programming anisotropy in fibrin.
  • This biologically compatible method enables the creation of directionally functional fibrin-based tissues.
  • Further functional enhancement is possible with integrated deformable piezoelectric scaffolds.