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Related Concept Videos

Fibronectins Connect Cells with ECM01:25

Fibronectins Connect Cells with ECM

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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...
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Fibrous Proteins00:55

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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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Fibril-associated Collagen01:11

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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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The Extracellular Matrix01:29

The Extracellular Matrix

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Overview
In order to maintain tissue organization, many animal cells are surrounded by structural molecules that make up the extracellular matrix (ECM). Together, the molecules in the ECM maintain the structural integrity of tissue as well as the remarkable specific properties of certain tissues.
Composition of the Extracellular Matrix
The extracellular matrix (ECM) is commonly composed of ground substance, a gel-like fluid, fibrous components, and many structurally and functionally diverse...
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The Extracellular Matrix01:42

The Extracellular Matrix

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Extracellular Matrix01:26

Extracellular Matrix

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Unlike epithelial tissue, which is composed of cells closely packed with little or no extracellular space in between, connective tissue cells are dispersed in a matrix. This extracellular matrix (ECM) is composed of fibrous proteins like collagen, elastin, and fibronectin in a ground substance consisting of interstitial fluid, cell adhesion proteins, and proteoglycans. The proteoglycans form a gel-like material in the spaces between cells and provide hydration, buffering, binding, and force...
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ECM Protein Nanofibers and Nanostructures Engineered Using Surface-initiated Assembly
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Fibronectin, the extracellular glue.

Alicia J Zollinger1, Michael L Smith1

  • 1Department of Biomedical Engineering, Boston University, Boston, MA 02215, United States.

Matrix Biology : Journal of the International Society for Matrix Biology
|August 7, 2016
PubMed
Summary

Fibronectin, an extracellular matrix protein, binds many molecules and influences cell behavior. Its fiber conformation affects binding partner adhesion, crucial in tissue development and disease.

Keywords:
Cell adhesionExtracellular matrixFibronectin

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Tissue Engineering

Background:

  • Fibronectin is an extracellular matrix protein vital in tissue development, wound healing, and disease progression.
  • It plays a critical role in cell adhesion and signaling through interactions with various molecules.
  • Fibronectin fibers exhibit dynamic conformational changes influenced by binding partners and cellular forces.

Purpose of the Study:

  • To review the diverse binding partners of fibronectin.
  • To highlight how fibronectin's molecular conformation impacts the adhesiveness of its binding partners.
  • To explore the implications of these interactions in biological contexts.

Main Methods:

  • Literature review of studies on fibronectin binding and function.
  • Analysis of research on fibronectin's structural properties and conformational dynamics.
  • Synthesis of information on fibronectin's interactions with extracellular matrix proteins, growth factors, and synthetic ligands.

Main Results:

  • Fibronectin binds a wide array of molecules, including ECM components, signaling factors, and cell adhesion molecules.
  • The conformation of fibronectin fibers is labile and can be modulated by allosteric binding and mechanical forces.
  • Altered fibronectin conformation significantly impacts the adhesive properties of its bound partners.

Conclusions:

  • Fibronectin's unique binding capabilities and conformational plasticity are central to its biological functions.
  • Understanding these interactions is key to deciphering fibronectin's roles in normal and pathological tissue remodeling.
  • Further research into fibronectin conformation-dependent binding may yield therapeutic strategies.