TAILIEUCHUNG - Báo cáo khoa học: Iron regulatory protein-independent regulation of ferritin synthesis by nitrogen monoxide

The discovery of iron-responsive elements (IREs), along with the identifica-tion of iron regulatory proteins (IRP1, IRP2), has provided a molecular basis for our current understanding of the remarkable post-transcriptional regulation of intracellular iron homeostasis. In iron-depleted conditions, IRPs bind to IREs present in the 5¢-UTR of ferritin mRNA and the 3¢-UTR of transferrin receptor (TfR) mRNA. | ễFEBS Journal Iron regulatory protein-independent regulation of ferritin synthesis by nitrogen monoxide Marc Mikhael1 2 Sangwon F. Kim2 Matthias Schranzhofer3 Shan S. Lin1 4 Alex D. Sheftel1 2 Ernst W. Mullner3 and Prem Ponka1 2 1 Department of Physiology McGillUniversity Montreal Canada 2 Lady Davis Institute for MedicalResearch Jewish General Hospital Montreal Canada 3 Department of MedicalBiochemistry Division of Molecular Biology Max F. Perutz Laboratories MedicalUniversity of Vienna Austria 4 Division of ExperimentalMedicine McGillUniversity Montreal Canada Keywords ferritin iron iron regulatory proteins nitrogen monoxide NO Correspondence P. Ponka Lady Davis Institute McGill University 3755 Cote Ste-Catherine Road Montreal Quebec H3T 1E2 Canada Fax 1 514 340 7502 Tel 1 514 340 8260 E-mail Received 2 June 2006 revised 20 June 2006 accepted 22 June 2006 doi The discovery of iron-responsive elements IREs along with the identification of iron regulatory proteins IRP1 IRP2 has provided a molecular basis for our current understanding of the remarkable post-transcriptional regulation of intracellular iron homeostasis. In iron-depleted conditions IRPs bind to IREs present in the 5 -UTR of ferritin mRNA and the 3 -UTR of transferrin receptor TfR mRNA. Such binding blocks the translation of ferritin the iron storage protein and stabilizes TfR mRNA whereas the opposite scenario develops when iron in the intracellular transit pool is plentiful. Nitrogen monoxide commonly designated nitric oxide NO a gaseous molecule involved in numerous functions is known to affect cellular iron metabolism via the IRP IRE system. We previously demonstrated that the oxidized form of NO NO causes IRP2 degradation that is associated with an increase in ferritin synthesis Kim S Ponka P 2002 Proc Natl Acad Sci USA 99 12214-12219 . Here we report that sodium nitroprusside SNP an NO donor causes a dramatic and rapid increase in ferritin .

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