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Related Concept Videos

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...
Structural Protein Function01:56

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to form...
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...
Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
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...
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...

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Updated: May 8, 2026

ECM Protein Nanofibers and Nanostructures Engineered Using Surface-initiated Assembly
16:33

ECM Protein Nanofibers and Nanostructures Engineered Using Surface-initiated Assembly

Published on: April 17, 2014

Multiscale relationships between fibronectin structure and functional properties.

M J Bradshaw1, M L Smith2

  • 1Department of Mechanical Engineering, Boston University, 44 Cummington St., ERB 502, Boston, MA 02215, USA.

Acta Biomaterialia
|August 28, 2013
PubMed
Summary
This summary is machine-generated.

Fibronectin (Fn) fibers in the extracellular matrix (ECM) control cell behavior. Mechanical forces alter Fn fiber architecture, influencing cell adhesion and signaling during development and disease.

Keywords:
Computational ModelingExtracellular matrixFibronectinMechanotransduction

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Area of Science:

  • Biomaterials Science
  • Cell Biology
  • Biophysics

Background:

  • Cell behavior is regulated by the extracellular matrix (ECM), with fibronectin (Fn) fibers playing a key role in dynamic biological processes like development and wound healing.
  • The fibrillar structure of Fn influences cell adhesion, growth factor signaling, matrix stiffness, and ligand binding, all of which are critical for in vivo cell functions.

Purpose of the Study:

  • To review and synthesize recent research linking the molecular properties of fibronectin (Fn) to the bulk characteristics of Fn matrix fibers.
  • To elucidate the mechanobiological functions of Fn by understanding its molecular arrangement and intermolecular interactions within assembled fibers.

Main Methods:

  • Review of studies investigating isolated Fn fibers to characterize material properties.
  • Integration of experimental data with computational models of Fn molecular behavior within fibers.

Main Results:

  • The multiscale architecture of Fn fibers dictates critical parameters such as ligand density, porosity for signaling molecules, and mechanical stiffness.
  • Mechanical strain applied to the ECM alters these architectural and material properties of Fn fibers.
  • Studies have begun to reveal the molecular arrangement and intermolecular forces within Fn fibers.

Conclusions:

  • Understanding the relationship between Fn molecular properties and bulk fiber characteristics is crucial for comprehending its mechanobiological roles.
  • Fn fibers are key regulators of cell behavior, with their properties dynamically modulated by mechanical forces in the ECM.