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Related Concept Videos

Role of Matrix Metalloproteases in Degradation of ECM01:23

Role of Matrix Metalloproteases in Degradation of ECM

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 body.
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Related Experiment Video

Updated: Jun 16, 2026

An Ex Vivo Tissue Culture Model of Cartilage Remodeling in Bovine Knee Explants
07:10

An Ex Vivo Tissue Culture Model of Cartilage Remodeling in Bovine Knee Explants

Published on: November 3, 2019

Collagen degradation assays.

Anthony P Hollander1

  • 1Department of Cellular and Molecular Medicine, University of Bristol, Bristol, UK.

Methods in Molecular Biology (Clifton, N.J.)
|February 6, 2010
PubMed
Summary
This summary is machine-generated.

Assessing collagen degradation is complex due to its biochemistry. A new method uses antibodies targeting hidden epitopes exposed after collagen cleavage, enabling accurate collagen degradation assays.

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Organotypic Collagen I Assay: A Malleable Platform to Assess Cell Behaviour in a 3-Dimensional Context
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Organotypic Collagen I Assay: A Malleable Platform to Assess Cell Behaviour in a 3-Dimensional Context

Published on: October 13, 2011

Related Experiment Videos

Last Updated: Jun 16, 2026

An Ex Vivo Tissue Culture Model of Cartilage Remodeling in Bovine Knee Explants
07:10

An Ex Vivo Tissue Culture Model of Cartilage Remodeling in Bovine Knee Explants

Published on: November 3, 2019

Organotypic Collagen I Assay: A Malleable Platform to Assess Cell Behaviour in a 3-Dimensional Context
10:45

Organotypic Collagen I Assay: A Malleable Platform to Assess Cell Behaviour in a 3-Dimensional Context

Published on: October 13, 2011

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Immunology

Background:

  • Collagen's complex biochemistry complicates degradation assays.
  • Hidden epitopes are masked in intact collagen helices.
  • These epitopes become accessible upon collagen cleavage and denaturation.

Purpose of the Study:

  • To describe a novel method for assaying collagen degradation.
  • To utilize antibodies targeting specific collagen epitopes.
  • To combine antibody use with proteolytic extraction for enhanced accuracy.

Main Methods:

  • Raising antibodies against hidden epitopes of collagen.
  • Employing selective proteolytic extraction techniques.
  • Developing an assay based on antibody binding to exposed epitopes.

Main Results:

  • The described method allows for the assay of collagen degradation.
  • Antibody binding to exposed epitopes provides a quantifiable measure.
  • Selective extraction enhances the specificity of the assay.

Conclusions:

  • A novel and effective method for collagen degradation assaying is presented.
  • This approach leverages specific antibody recognition of exposed epitopes.
  • The technique offers a valuable tool for studying collagen breakdown.