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Related Concept Videos

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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.
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Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
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The Extracellular Matrix01:29

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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.
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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. 
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Matrix metalloproteases (MMPs) are enzymes involved in the hydrolysis of proteins and glycoproteins of the extracellular matrix. MMPs are essential for the migration and proliferation of cells through the dense matrix network, throughout embryonic development, and throughout morphogenesis. The first MMP activity discovered was a collagenase in a tadpole's tail undergoing metamorphosis. The active collagen deposition and modifications lead to the morphogenesis of tadpoles into the adult...
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The extracellular matrix or ECM holds cells together to form a tissue and allows the cells within the tissue to communicate. ECM comprises proteins such as fibronectin, collagen, laminin, etc. The most abundant protein in this space is collagen. Collagen fibers are interwoven with carbohydrate-containing protein molecules called proteoglycans. ECM allows cell migration and provides a structural scaffold at cell adhesion that anchors the cell when the extracellular matrix proteins interact with...
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Dipeptidyl Peptidase-4-Mediated Fibronectin Processing Evokes a Profibrotic Extracellular Matrix.

Karina A Zeyer1, Olivier Bornert1, Valentin Nelea2

  • 1Department of Dermatology, Medical Faculty, Medical Center - University of Freiburg, Freiburg, Germany.

The Journal of Investigative Dermatology
|April 3, 2024
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Summary

Altered fibronectin deposition drives fibrosis. Dipeptidyl peptidase-4 inhibitors normalized fibronectin and extracellular matrix (ECM) organization, revealing a new therapeutic target for fibrotic diseases.

Keywords:
CollagenCollagen VIIDystrophic epidermolysis bullosaFibrillinProteolysis

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Area of Science:

  • Extracellular Matrix Biology
  • Fibrosis Pathogenesis
  • Dermatology

Background:

  • Fibronectin is crucial for organizing the extracellular matrix (ECM), including collagen and fibrillin.
  • Altered fibronectin deposition is an early event in fibrotic diseases, leading to disorganized ECM.
  • Recessive dystrophic epidermolysis bullosa serves as a model for severe dermal fibrosis.

Purpose of the Study:

  • To investigate the role of fibronectin's ECM-organizational capacity in fibrosis development.
  • To explore the link between dipeptidyl peptidase-4 (DPP-4) and fibronectin deposition in fibrosis.
  • To identify potential therapeutic strategies targeting DPP-4 for fibrotic conditions.

Main Methods:

  • Culturing fibroblasts from recessive dystrophic epidermolysis bullosa patients in 2D and 3D.
  • Analyzing fibronectin, fibrillin, and collagen I deposition.
  • Utilizing proteomics, DPP-4 inhibitors, and mutagenesis studies.

Main Results:

  • Fibroblasts from patients showed dysregulated fibronectin deposition.
  • Increased profibrotic DPP-4-positive fibroblasts correlated with altered fibronectin deposition.
  • DPP-4 inhibition normalized fibronectin, fibrillin, and collagen I deposition.
  • DPP-4 modulates ECM deposition via proteolysis of the fibronectin N-terminus.

Conclusions:

  • DPP-4 plays a key role in fibrotic ECM dysregulation.
  • Targeting DPP-4 can restore normal ECM assembly and offers a potential therapeutic approach for fibrosis.
  • This study elucidates the mechanism of DPP-4 in fibronectin-guided ECM assembly in health and disease.