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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

Summary

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.

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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.
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.

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