scholarly journals Resistance to the Antitumor Agent Gallium Nitrate in Human Leukemic Cells Is Associated with Decreased Gallium/Iron Uptake, Increased Activity of Iron Regulatory Protein-1, and Decreased Ferritin Production

1997 ◽  
Vol 272 (18) ◽  
pp. 12151-12157 ◽  
Author(s):  
Christopher R. Chitambar ◽  
Janine P. Wereley
2015 ◽  
Vol 116 (9) ◽  
pp. 1919-1931 ◽  
Author(s):  
Chun-Ming Cheng ◽  
Dan Wang ◽  
Xian Cao ◽  
Qian-Qian Luo ◽  
Ya-Peng Lu ◽  
...  

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

2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Nhan Huynh ◽  
Qiuxiang Ou ◽  
Pendleton Cox ◽  
Roland Lill ◽  
Kirst King-Jones

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.


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