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Effects of hyperoxia and iron on iron regulatory protein-1 activity and the ferritin synthesis in mouse peritoneal macrophages.

Abstract
Ferritin is an intracellular iron storage protein and its translation is inhibited by binding of iron regulatory proteins (IRPs) to the iron-responsive element (IRE) located in the 5' untranslated region of its mRNA. In this paper, we have investigated the effect of hyperoxia and iron on the binding activity of IRP-1 and the ferritin synthesis in mouse peritoneal macrophages. The binding activity of IRP-1 was increased and the ferritin synthesis was suppressed when the macrophages were cultured under hyperoxia, and the reverse occurred under hypoxia. Iron diminished the IRP-1-binding activity and the enhanced synthesis of ferritin. However, this effect was arrested under hyperoxia. Consistently, hypoxia-induced loss of binding activity of IRP-1 and the enhanced synthesis of ferritin were blocked in the presence of an iron chelator deferoxamine. These alterations of the binding activity of IRP-1 in response to oxygen and iron were not reproduced in the cell-free extract. The data suggest that in the macrophages oxygen and iron inversely act on the binding activity of IRP-1 and the ferritin synthesis, and that intracellular mechanism(s) to sense iron and/or oxygen is required for these actions.
AuthorsK Kuriyama-Matsumura, H Sato, M Suzuki, S Bannai
JournalBiochimica et biophysica acta (Biochim Biophys Acta) Vol. 1544 Issue 1-2 Pg. 370-7 (Jan 12 2001) ISSN: 0006-3002 [Print] Netherlands
PMID11341946 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Iron-Regulatory Proteins
  • Iron-Sulfur Proteins
  • RNA-Binding Proteins
  • Ferritins
  • Iron
  • Iron Regulatory Protein 1
Topics
  • Animals
  • Female
  • Ferritins (biosynthesis)
  • Hyperoxia (metabolism)
  • Iron (metabolism)
  • Iron Regulatory Protein 1
  • Iron-Regulatory Proteins
  • Iron-Sulfur Proteins (metabolism)
  • Macrophages, Peritoneal (metabolism)
  • Mice
  • Mice, Inbred C57BL
  • Oxidative Stress
  • RNA-Binding Proteins (metabolism)

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