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Stretching fibronectin.

Harold P Erickson1

  • 1Department of Cell Biology, Box 3079, Duke University Medical Center, Durham, NC 27710, USA. h.erickson@cellbio.duke.edu

Journal of Muscle Research and Cell Motility
|June 6, 2003
PubMed
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Fibronectin matrix fibrils exhibit elasticity, stretching with cell movement and relaxing significantly when broken. Two proposed mechanisms explain this elasticity, focusing on molecular conformation and domain unfolding.

Area of Science:

  • Biochemistry and Molecular Biology
  • Cell Biology
  • Biophysics

Background:

  • Fibronectin (FN) matrix fibrils are crucial extracellular matrix components.
  • These fibrils display elastic properties, responding to cellular forces.
  • Observed relaxation to 1/3-1/4 of rest length upon breakage indicates significant elasticity.

Purpose of the Study:

  • To investigate the molecular mechanisms underlying fibronectin fibril elasticity.
  • To differentiate between proposed models for FN fibril mechanical behavior.
  • To discuss experimental evidence relevant to FN elasticity.

Main Methods:

  • Analysis of fibronectin (FN) matrix fibril behavior in cell culture.
  • Observation of fibril stretching in response to cell movements.

Related Experiment Videos

  • Examination of fibril relaxation dynamics after breakage.

    • Main Results:

    • Fibronectin fibrils stretch under cellular forces.
    • Broken fibrils relax to a fraction of their original length.
    • Two distinct molecular mechanisms are proposed for this elasticity.

    Conclusions:

    • The elasticity of fibronectin fibrils can be explained by two potential molecular mechanisms.
    • One model suggests FN molecules are looped and extend upon stretching.
    • The alternative model proposes FN molecules are pre-extended, with stretching involving domain unfolding.