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Related Concept Videos

Fibril-associated Collagen01:11

Fibril-associated Collagen

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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.
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Three main types of fibers are secreted by fibroblasts: collagen fibers, elastic fibers, and reticular fibers. Collagen fiber is made from fibrous protein subunits linked together to form a long, straight fiber. Collagen fibers, while flexible, have great tensile strength, resist stretching, and give ligaments and tendons their characteristic resilience and strength. These fibers hold connective tissues together, even during the body's movement.
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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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Related Experiment Video

Updated: Sep 28, 2025

Scanning Electron Microscopy of Macerated Tissue to Visualize the Extracellular Matrix
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Collagen type XIX regulates cardiac extracellular matrix structure and ventricular function.

Ghazal Sadri1, Annalara G Fischer1, Kenneth R Brittian1

  • 1Diabetes and Obesity Center, University of Louisville School of Medicine, Louisville, KY, USA.

Matrix Biology : Journal of the International Society for Matrix Biology
|March 29, 2022
PubMed
Summary

Collagen type XIX (Col19a1), a fibril-associated collagen with interrupted triple helices (FACIT), is crucial for cardiac structure and function. Its absence in mice impairs systolic function and alters extracellular matrix organization.

Keywords:
Cardiac fibroblastsCardiac functionCardiomyocyte hypertrophyCollagen type XIXExtracellular matrix structure

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Area of Science:

  • Cardiovascular Biology
  • Extracellular Matrix Research
  • Collagen Biology

Background:

  • The cardiac extracellular matrix (ECM) is vital for heart function and repair.
  • While fibrillar collagens are well-studied, non-fibrillar collagens, like fibril-associated collagens with interrupted triple helices (FACITs), are less understood.
  • Collagen type XIX (Col19a1) expression in the heart, particularly during ischemia, suggests a significant role in cardiac ECM.

Purpose of the Study:

  • To identify the cellular source of collagen XIX in the adult murine heart.
  • To investigate the role of collagen XIX in cardiac extracellular matrix structure and ventricular function.

Main Methods:

  • Immunodetection of collagen XIX in fractionated cardiovascular cell lineages.
  • Echocardiography and histology in Col19a1 null (Col19a1N/N) mice.
  • Analysis of enzyme expression (PLOD1, LOX) in Col19a1N/N cardiac fibroblasts.
  • Second harmonic generation imaging and transmission electron microscopy of ECM and decellularized hearts.
  • Assessment of focal adhesion kinase (FAK) phosphorylation.

Main Results:

  • Fibroblasts and smooth muscle cells are the primary producers of collagen XIX in the heart.
  • Col19a1N/N mice exhibited reduced systolic function, thinned ventricular walls, and increased cardiomyocyte size.
  • Col19a1N/N cardiac fibroblasts showed increased expression of PLOD1 and LOX.
  • ECM from Col19a1N/N fibroblasts and decellularized Col19a1N/N hearts displayed disorganized fibrillar collagen structure.
  • Col19a1N/N mice had enhanced FAK phosphorylation, indicating FAK pathway de-repression.

Conclusions:

  • Collagen XIX plays a previously unrecognized role in regulating mammalian heart structure and function.
  • Collagen XIX may modulate cardiac ECM fibrillar collagen organization.
  • Collagen XIX influences ECM superstructure by regulating fibroblast expression of collagen synthesis and stabilization enzymes.