Regulation of ferritin synthesis in macrophages by oxygen and a sulfhydryl-reactive agent.
Ferritin synthesis is known to be regulated translationally by specific mRNA-protein interactions between an iron-responsive element (IRE) localized in the 5' untranslated region of ferritin mRNA and IRE-binding protein (IRE-BP). Binding of IRE-BP to IRE depresses its translation. In the present study, we demonstrated that ferritin synthesis in macrophages is strongly induced under hypoxic conditions by diethylmaleate, a sulfhydryl-reactive agent. The induction by diethylmaleate decreased as the oxygen tension rose. O2- is involved in this oxygen effect, because the induction was prevented when O2(-)-generating agents were present. Actinomycin D did not inhibit the ferritin synthesis induced by diethylmaleate under hypoxi. These results suggest that O2- is involved in post-transcriptional regulation of ferritin synthesis.
Sato
H
H
Department of Biological Chemistry, University of Tsukuba, Ibaraki, Japan.
Yamaguchi
M
M
Bannai
S
S
D000818:Animals; D003609:Dactinomycin / Q000494:pharmacology; D005260:Female; D005293:Ferritins / Q000096:biosynthesis*; D006861:Hydrogen Peroxide / Q000378:metabolism; D007501:Iron / Q000378:metabolism; D017737:Macrophages, Peritoneal / Q000378:metabolism*; D051379:Mice; D008810:Mice, Inbred C57BL; D010100:Oxygen / Q000502:physiology*; D013438:Sulfhydryl Compounds / Q000502:physiology*; D013481:Superoxides / Q000378:metabolism
D013438:Sulfhydryl Compounds; D013481:Superoxides; D003609:Dactinomycin; D005293:Ferritins; D006861:Hydrogen Peroxide; D007501:Iron; D010100:Oxygen