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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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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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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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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Evaluation of Keratinocyte Proliferation on Two- and Three-dimensional Type I Collagen Substrates
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Evaluation of Keratinocyte Proliferation on Two- and Three-dimensional Type I Collagen Substrates

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Collagen Fibril Assembly and Function.

David F Holmes1, Yinhui Lu1, Tobias Starborg1

  • 1Wellcome Trust Centre for Cell-Matrix Research, Faculty of Biology, Medicine and Health, Manchester Academic Health Science Centre, University of Manchester, Manchester, United Kingdom.

Current Topics in Developmental Biology
|June 2, 2018
PubMed
Summary
This summary is machine-generated.

Collagen fibrils form essential tissue frameworks in animals, assembling spontaneously or with cellular guidance. Understanding their intricate formation mechanisms is key to preventing tissue failure and fibrosis.

Keywords:
Connective tissueCorneaExtracellular matrixSerial block face-scanning electron microscopyTendon

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Area of Science:

  • Biomaterials Science
  • Cell Biology
  • Tissue Engineering

Background:

  • Collagen fibrils are the primary mechanical components of the extracellular matrix in diverse animal tissues.
  • They provide structural integrity and resist tension, forming complex, hierarchical fiber-composite systems tailored to specific mechanical demands.
  • These biological tissues exhibit remarkable self-maintenance and resistance to fatigue failure throughout an animal's lifespan.

Purpose of the Study:

  • To elucidate the intricate mechanisms governing the generation of collagen fibril networks.
  • To understand how cellular machinery regulates fibril nucleation, spatial orientation, and size during tissue development.
  • To highlight the link between collagen fibril architecture and tissue mechanical properties.

Main Methods:

  • Review of existing literature on collagen self-assembly.
  • Analysis of cellular regulation in developing tissues.
  • Investigation of the relationship between fibril network architecture and mechanical function.

Main Results:

  • Collagen fibrils can self-assemble from purified collagen molecules.
  • In developing tissues, cellular machinery actively regulates fibril formation, influencing nucleation, orientation, and size.
  • The mechanisms underlying the creation of specific collagen fibril architectures and their associated mechanical properties are increasingly understood.

Conclusions:

  • The self-organization of collagen fibrils, guided by cellular processes, is crucial for tissue stability and function.
  • Dysregulation of collagen fibril assembly can lead to mechanical failure and pathological conditions like fibrosis.
  • Further research into these mechanisms holds potential for therapeutic interventions in tissue repair and disease treatment.