Activation and inactivation of the iron hormone hepcidin: Biochemical characterization of prohepcidin cleavage and sequential degradation to N-terminally truncated hepcidin isoforms.

@article{Schranz2009ActivationAI,
  title={Activation and inactivation of the iron hormone hepcidin: Biochemical characterization of prohepcidin cleavage and sequential degradation to N-terminally truncated hepcidin isoforms.},
  author={Melanie Schranz and Rania Bakry and Marc Creus and G{\"u}nther Bonn and Wolfgang Vogel and Heinz Zoller},
  journal={Blood cells, molecules & diseases},
  year={2009},
  volume={43 2},
  pages={169-79}
}
The hormone hepcidin is produced mainly in the liver in response to iron loading and inflammation and secreted into the circulation as a 25-amino acid peptide. The 84-amino acid prohormone undergoes limited proteolytic cleavage at a conserved proprotein convertase (PC) recognition site. In addition to the 25-amino acid hepcidin, N-terminally truncated isoforms of lower biological activity are found in plasma and urine. Here we show that a redundant system of proprotein convertases cleaves… CONTINUE READING
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