Iron at the center of ferritin, metal/oxygen homeostasis and novel dietary strategies

X. Liu, K. Hintze, B. Lonnerdal, Elizabeth C. Theil

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


Bioiron central to respiration, photosynthesis and DNA synthesis and complicated by radical chemistry with oxygen depends on ferritin, the super family of protein nanocages (maxi-ferritins in humans, animals, plants and bacteria, and mini-ferritins, also called DPS proteins, in bacteria) for iron and oxygen control. Regulation of ferritin synthesis, best studied in animals, uses DNA transcription and mRNA translation check points. Ferritin is a member of both the "oxidant stress response" gene family that includes thioredoxin reductase and quinine reductase, and a member of the iron responsive gene family that includes ferroportin and mt-aconitase ferritin DNA regulation responds preferentially to oxidant response inducers and ferritin mRNA to iron inducers; heme confers regulator synergy. Ferritin proteins manage iron and oxygen, with ferroxidase sites and iron + oxygen substrates to form mineral of both Fe and O atoms; maxi-ferritins contribute more to cellular iron metabolism and mini-ferritins to stress responses. Iron recovery from ferritin is controlled by gated protein pores, possibly contributing to iron absorption from ferritin, a significant dietary iron source. Ferritin gene regulation is a model for integrating DNA/ mRNA controls, while ferritin protein function is central to molecular nutrition cellular metabolism at the crossroads of iron and oxygen in biology.

Original languageEnglish (US)
Pages (from-to)167-171
Number of pages5
JournalBiological Research
Issue number1
StatePublished - 2006

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)


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