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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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Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...
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Related Experiment Video

Updated: Nov 28, 2025

Quantifying Fibrillar Collagen Organization with Curvelet Transform-Based Tools
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Quantifying Fibrillar Collagen Organization with Curvelet Transform-Based Tools

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Quantifying Fibrillar Collagen Organization with Curvelet Transform-Based Tools.

Yuming Liu1, Kevin W Eliceiri2

  • 1Laboratory for Optical and Computational Instrumentation, Center for Quantitative Cell Imaging, University of Wisconsin-Madison.

Journal of Visualized Experiments : Jove
|November 30, 2020
PubMed
Summary
This summary is machine-generated.

A new collagen fiber quantification tool uses curvelet transform (CT) for accurate analysis of extracellular matrix (ECM) in disease research. This user-friendly platform offers detailed fiber measurements, improving biological and biomedical applications.

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Area of Science:

  • Biomedical Engineering
  • Computational Biology
  • Materials Science

Background:

  • Fibrillar collagens are key extracellular matrix (ECM) components implicated in disease progression, particularly cancers.
  • Existing collagen fiber quantification tools have limitations in accuracy, manual intervention, and localized feature analysis.
  • Changes in collagen topology are associated with various diseases, necessitating precise quantification methods.

Purpose of the Study:

  • To introduce a novel, user-driven collagen fiber quantitation platform based on curvelet transform (CT).
  • To overcome limitations of existing tools by providing accurate, localized, and comprehensive collagen fiber analysis.
  • To enable efficient quantification of collagen fiber organization for diverse biological and biomedical applications.

Main Methods:

  • Utilized curvelet transform (CT) for optimal multiscale image representation to denoise images and enhance fiber edges.
  • Developed two integrated software packages, CT-FIRE and CurveAlign, for quantifying fiber organization.
  • Enabled measurement of individual fiber properties (length, angle, width, straightness) and bulk properties (density, alignment).

Main Results:

  • The CT-based framework accurately quantifies collagen fiber organization on global, region of interest (ROI), or individual fiber levels.
  • The platform measures up to thirty distinct fiber features, including relative angles to segmented boundaries.
  • The system handles large datasets and requires no prior programming or image processing experience.

Conclusions:

  • The developed collagen quantification platform offers a comprehensive and efficient solution for analyzing extracellular matrix fiber organization.
  • This user-friendly tool enhances the study of collagen's role in disease pathogenesis and progression.
  • The platform facilitates advanced biological and biomedical research through precise and accessible collagen fiber analysis.