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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.
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: Feb 24, 2026

Engineering Fibrin-based Tissue Constructs from Myofibroblasts and Application of Constraints and Strain to Induce Cell and Collagen Reorganization
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Visualizing In Vitro Type I Collagen Fibrillogenesis by Transmission Electron Microscopy.

J Robin Harris1,2

  • 1Institute of Zoology, University of Mainz, Mainz, Germany. rharris@uni-mainz.de.

Methods in Molecular Biology (Clifton, N.J.)
|August 25, 2017
PubMed
Summary
This summary is machine-generated.

This study presents methods for in vitro collagen type I fibril formation. Researchers can control fibrillogenesis conditions and monitor collagen fibril development using transmission electron microscopy.

Keywords:
ATPCollagen type ID-Banded fibrilElectron microscopyFibrillogenesisHeterotrimerNegative stainingPolyphosphateSegment long spacing (SLS) crystalliteSulfonated diazo dyeTactoid

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Area of Science:

  • Biochemistry
  • Biomaterials Science
  • Microscopy

Background:

  • Collagen type I is a crucial structural protein.
  • Understanding collagen fibrillogenesis is vital for tissue engineering and biomaterials.
  • Controlling in vitro collagen fibril formation presents challenges.

Purpose of the Study:

  • To present techniques and protocols for in vitro collagen type I fibril formation.
  • To demonstrate the biochemical variation of fibrillogenesis conditions.
  • To establish transmission electron microscopy (TEM) as a monitoring tool.

Main Methods:

  • Development of in vitro fibrillogenesis protocols for collagen type I.
  • Systematic variation of biochemical conditions during fibrillogenesis.
  • Monitoring of fibril formation using transmission electron microscopy (TEM) of negatively stained specimens.

Main Results:

  • Successful in vitro formation of collagen type I fibrils under varied conditions.
  • TEM imaging provides clear visualization of fibril products.
  • Demonstration of extensive biochemical and structural possibilities.

Conclusions:

  • The presented protocols enable controlled in vitro collagen type I fibril formation.
  • TEM is an effective method for monitoring collagen fibrillogenesis.
  • The integrated approach offers significant flexibility for biomaterial design.