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An Overlooked Hepcidin-Cadmium Connection
Dawid Płonka1, Marta D Wiśniewska1, Manuel D Peris-Díaz2
1Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5a, 02-106 Warsaw, Poland.
International Journal of Molecular Sciences
|December 23, 2022
Summary
Hepcidin, an iron hormone, binds strongly to zinc and cadmium ions. This suggests hepcidin
Area of Science:
- Biochemistry
- Metalloprotein Chemistry
Background:
- Hepcidin is a key iron-regulatory hormone, a 25-amino-acid peptide with four disulfide bonds.
- Hepcidin's known function involves marking ferroportin-1 for degradation to regulate iron.
- Reduced hepcidin may act as an octathiol ligand, similar to metallothioneins.
Purpose of the Study:
- To investigate the potential of hepcidin to bind zinc (Zn(II)) and cadmium (Cd(II)) ions.
- To compare hepcidin's metal-binding properties with a modified hepcidin model (5R-hepcidin).
- To assess hepcidin's ability to compete with metallothionein for cadmium ions.
Main Methods:
- Spectroscopic titrations (pH-metric) to determine metal ion binding affinities.
- Mass spectrometry to analyze metal-hepcidin interactions.
- Utilized both native hepcidin and a 5R-hepcidin model.
Main Results:
- Hepcidin forms mononuclear complexes with two Zn(II) or Cd(II) ions, saturating all eight Cys residues.
- High binding affinities were observed: 10^10.1 M^-1 for Zn(II) and 10^15.2 M^-1 / 10^14.1 M^-1 for Cd(II).
- Hepcidin competes with metallothionein-2 for Cd(II) ions.
Conclusions:
- Hepcidin exhibits strong binding affinity for Zn(II) and Cd(II) ions.
- These findings suggest hepcidin's potential role in intracellular zinc physiology and cadmium toxicity.
- Hepcidin's metal-binding capacity may extend beyond its established iron-regulatory function.
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