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Related Concept Videos

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...

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Related Experiment Video

Updated: Jul 5, 2026

Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides
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Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides

Published on: January 31, 2014

Advances in collagen cross-link analysis.

David R Eyre1, Mary Ann Weis, Jiann-Jiu Wu

  • 1Orthopaedic Research Labs, Department of Orthopaedics & Sports Medicine, University of Washington, 1959 NE Pacific Street, Seattle, WA 98195-6500, USA. deyre@u.washington.edu

Methods (San Diego, Calif.)
|April 30, 2008
PubMed
Summary

This study combines mass spectrometry and antibodies to analyze collagen cross-linking domains in bone and cartilage. These methods reveal how post-translational modifications impact collagen structure and function.

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Last Updated: Jul 5, 2026

Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides
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Preparation of 3D Collagen Gels and Microchannels for the Study of 3D Interactions In Vivo
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Preparation of 3D Collagen Gels and Microchannels for the Study of 3D Interactions In Vivo

Published on: May 9, 2016

Area of Science:

  • Biochemistry
  • Structural Biology
  • Mass Spectrometry

Background:

  • Collagen is a crucial structural protein in connective tissues like bone and cartilage.
  • Understanding collagen cross-linking is vital for comprehending tissue integrity and disease.
  • Post-translational modifications significantly influence collagen structure and function.

Purpose of the Study:

  • To demonstrate the combined use of ion-trap mass spectrometry and peptide-specific antibodies for analyzing collagen cross-linking domains.
  • To investigate the role of post-translational modifications in collagen cross-linking.
  • To explore how intermolecular binding partners affect cross-link type and placement.

Main Methods:

  • Utilized ion-trap mass spectrometry for structural analysis.
  • Employed peptide-specific antibodies for targeted isolation of collagen cross-linking domains.
  • Applied these techniques to various collagen types, with a focus on bone and cartilage.

Main Results:

  • Successfully isolated and structurally characterized collagen cross-linking domains.
  • Provided examples of results from diverse collagenous tissues.
  • Highlighted the influence of post-translational modifications, such as lysine hydroxylation and glycosylation, on cross-linking.

Conclusions:

  • The combined approach offers powerful insights into collagen cross-linking.
  • Post-translational modifications are key regulators of collagen cross-link type and placement.
  • This methodology advances the understanding of collagen's role in tissue biomechanics and pathology.