Into the matrix: regulation of the iron regulatory hormone hepcidin by matriptase-2

Nutr Rev. 2009 May;67(5):284-8. doi: 10.1111/j.1753-4887.2009.00200.x.

Abstract

Matriptase-2 is a recently identified membrane-bound, cell-surface serine protease expressed primarily in liver. Mutations in matriptase-2 in mice and humans cause iron-deficiency anemia that responds poorly to iron therapy. The poor response results from an inability to decrease hepcidin production during iron deficiency. Cell culture studies reveal that matriptase-2 inhibits hepcidin induction by cleaving membrane hemojuvelin, a potent activator of hepcidin transcription. As a novel suppressor of hepcidin expression, matriptase-2 emerges as a possible candidate for therapeutic interventions aimed at treating disorders of iron metabolism.

Publication types

  • Review

MeSH terms

  • Anemia, Iron-Deficiency / drug therapy
  • Anemia, Iron-Deficiency / genetics*
  • Antimicrobial Cationic Peptides / antagonists & inhibitors*
  • Antimicrobial Cationic Peptides / metabolism*
  • Hepcidins
  • Humans
  • Iron / metabolism*
  • Iron / therapeutic use
  • Membrane Proteins / physiology*
  • Mutation
  • Serine Endopeptidases / physiology*
  • Signal Transduction
  • Treatment Failure

Substances

  • Antimicrobial Cationic Peptides
  • HAMP protein, human
  • Hamp protein, mouse
  • Hepcidins
  • Membrane Proteins
  • Iron
  • Serine Endopeptidases
  • matriptase 2