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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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Structural Protein Function01:56

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Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
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Following injury, the integrity of the injured tissues must be reestablished. For example, in skin tissue, wound repair involves coordination among resident skin cells, blood mononuclear cells, extracellular matrix, growth factors, and cytokines to complete the healing cascade.
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Related Experiment Video

Updated: May 3, 2026

Evaluation of Keratinocyte Proliferation on Two- and Three-dimensional Type I Collagen Substrates
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Novel functions for type II procollagen.

Linda J Sandell1

  • 1Department of Orthopaedic Surgery and Department of Cell Biology and Physiology, Musculoskeletal Research Center, Washington University School of Medicine , St. Louis, MO , USA.

Connective Tissue Research
|January 21, 2014
PubMed
Summary
This summary is machine-generated.

Cartilage contains a novel anti-angiogenic molecule, the NH2-propeptide of type IIB collagen. This peptide protects cartilage by eliminating endothelial cells, osteoclasts, and tumor cells.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Oncology

Background:

  • Cartilage is an avascular tissue, naturally resistant to tumor invasion.
  • Research since the 1970s has identified anti-angiogenic molecules in cartilage.
  • Degradative enzymes can release active anti-angiogenic fragments from cartilage proteins.

Purpose of the Study:

  • To highlight a newly identified anti-angiogenic and anti-tumor compound from cartilage.
  • To investigate the protective mechanisms of this compound within cartilage.

Main Methods:

  • Review of existing literature on cartilage anti-angiogenic properties.
  • Identification and characterization of the NH2-propeptide of type IIB collagen.
  • Analysis of the propeptide's biological activity against endothelial cells, osteoclasts, and tumor cells.

Main Results:

  • The NH2-propeptide of type IIB collagen is a potent anti-angiogenic and anti-tumor moiety.
  • This propeptide is released during collagen synthesis.
  • It independently kills endothelial cells, osteoclasts, and tumor cells, protecting cartilage.

Conclusions:

  • The NH2-propeptide of type IIB collagen represents a significant discovery in cartilage biology and cancer research.
  • This molecule has potential therapeutic applications for cartilage protection and anti-tumor strategies.
  • Understanding these endogenous protective mechanisms could lead to novel treatments.