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

2001 ◽  
Vol 1544 (1-2) ◽  
pp. 370-377 ◽  
Author(s):  
Kazumi Kuriyama-Matsumura ◽  
Hideyo Sato ◽  
Mika Suzuki ◽  
Shiro Bannai
Keyword(s):  
Regulatory Protein ◽  
Peritoneal Macrophages ◽  
Iron Regulatory Protein ◽  
Ferritin Synthesis ◽  
Mouse Peritoneal Macrophages ◽  
Ferritin Synthesis In ◽  
Iron Regulatory Protein 1

scholarly journals Iron Regulatory Protein-1 Protects against Mitoferrin-1-deficient Porphyria

2014 ◽  
Vol 289 (11) ◽  
pp. 7835-7843 ◽  
Author(s):  
Jacky Chung ◽  
Sheila A. Anderson ◽  
Babette Gwynn ◽  
Kathryn M. Deck ◽  
Michael J. Chen ◽  
...  
Keyword(s):  
Regulatory Protein ◽  
Iron Regulatory Protein ◽  
Iron Regulatory Protein 1

scholarly journals Glycogen branching enzyme controls cellular iron homeostasis via Iron Regulatory Protein 1 and mitoNEET

2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Nhan Huynh ◽  
Qiuxiang Ou ◽  
Pendleton Cox ◽  
Roland Lill ◽  
Kirst King-Jones
Keyword(s):  
Iron Homeostasis ◽  
Nuclear Translocation ◽  
Regulatory Protein ◽  
Glycogen Metabolism ◽  
Glycogen Storage Disease Type ◽  
Iron Regulatory Protein ◽  
Messenger Rnas ◽  
Branching Enzyme ◽  
Cellular Iron ◽  
Iron Regulatory Protein 1

AbstractIron Regulatory Protein 1 (IRP1) is a bifunctional cytosolic iron sensor. When iron levels are normal, IRP1 harbours an iron-sulphur cluster (holo-IRP1), an enzyme with aconitase activity. When iron levels fall, IRP1 loses the cluster (apo-IRP1) and binds to iron-responsive elements (IREs) in messenger RNAs (mRNAs) encoding proteins involved in cellular iron uptake, distribution, and storage. Here we show that mutations in the Drosophila 1,4-Alpha-Glucan Branching Enzyme (AGBE) gene cause porphyria. AGBE was hitherto only linked to glycogen metabolism and a fatal human disorder known as glycogen storage disease type IV. AGBE binds specifically to holo-IRP1 and to mitoNEET, a protein capable of repairing IRP1 iron-sulphur clusters. This interaction ensures nuclear translocation of holo-IRP1 and downregulation of iron-dependent processes, demonstrating that holo-IRP1 functions not just as an aconitase, but throttles target gene expression in anticipation of declining iron requirements.

HBx modulates iron regulatory protein 1-mediated iron metabolism via reactive oxygen species

2008 ◽  
Vol 133 (2) ◽  
pp. 167-177 ◽  
Author(s):  
Jin-Mo Gu ◽  
Seung Oe Lim ◽  
Sae Jin Oh ◽  
So-Mi Yoon ◽  
Je Kyung Seong ◽  
...  
Keyword(s):  
Reactive Oxygen Species ◽  
Iron Metabolism ◽  
Regulatory Protein ◽  
Reactive Oxygen ◽  
Iron Regulatory Protein ◽  
Oxygen Species ◽  
Iron Regulatory Protein 1
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