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Coated vesicles from chicken liver bind ferritin.

A Passaniti1, T F Roth

  • 1Department of Biological Sciences, University of Maryland Baltimore County, Catonsville 21228.

Journal of Cell Science
|February 1, 1989
PubMed
Summary
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Highly purified coated vesicles (CV) from chicken liver contain the iron-storage protein ferritin. This ferritin is associated with the clathrin lattice, suggesting a novel cellular role for this complex.

Area of Science:

  • Cell Biology
  • Biochemistry
  • Protein Interactions

Background:

  • Ferritin is the primary intracellular iron-storage protein.
  • Coated vesicles (CV) are involved in intracellular trafficking.
  • The relationship between ferritin and CV has not been previously established.

Purpose of the Study:

  • To investigate the potential association of ferritin with purified coated vesicles.
  • To characterize the nature of this association in chicken liver cells.

Main Methods:

  • Purification of coated vesicles using controlled-pore glass-bead chromatography.
  • Immunological detection of ferritin using a specific monoclonal anti-ferritin antibody.
  • Electron microscopy to visualize ferritin association with CV.

Related Experiment Videos

  • Biochemical treatments (urea, Triton X-100) to assess the stability of the association.

    • Main Results:

    • Highly purified chicken liver coated vesicles were found to contain ferritin.
    • Ferritin particles were observed to be associated with CV by electron microscopy.
    • The ferritin-CV association was stable to detergent but dissociable under conditions that also disrupt the clathrin lattice.

    Conclusions:

    • Purified chicken liver coated vesicles contain ferritin associated with the clathrin lattice.
    • This finding suggests a potential functional role for the ferritin-clathrin complex within the cell.