scholarly journals The role of iron regulatory proteins in the control of iron metabolism in mammals

2011 ◽  
Vol 1 ◽  
pp. 66-75 ◽  
Author(s):  
Agnieszka Styś ◽  
Rafał R. Starzyński ◽  
Paweł Lipiński
Keyword(s):  
Iron Metabolism ◽  
Regulatory Proteins ◽  
Iron Regulatory Proteins

Dysfunction of Iron Metabolism and Iron-Regulatory Proteins in the Rat Hippocampus After Heat Stroke

Shock ◽  
2019 ◽  
Vol 51 (6) ◽  
pp. 780-786 ◽  
Author(s):  
Jing Liu ◽  
Mingsheng Wan ◽  
Yun Zhang ◽  
Shu Zhang ◽  
Hongying Zhang ◽  
...  
Keyword(s):  
Iron Metabolism ◽  
Heat Stroke ◽  
Rat Hippocampus ◽  
Regulatory Proteins ◽  
Iron Regulatory Proteins

Iron Regulatory Proteins in Systemic Iron Metabolism and Erythropoiesis

Blood ◽  
2011 ◽  
Vol 118 (21) ◽  
pp. SCI-22-SCI-22
Author(s):  
Matthias W. Hentze
Keyword(s):  
Iron Metabolism ◽  
Iron Homeostasis ◽  
Mutant Mouse ◽  
Conflicts Of Interest ◽  
Regulatory Proteins ◽  
Iron Regulatory Proteins ◽  
Cellular Iron ◽  
Regulatory Systems ◽  
Biology I ◽  
Mouse Lines

Abstract Abstract SCI-22 Imbalances of iron homeostasis account for some of the most common human diseases. Pathologies can result from both iron deficiency or overload. The hepcidin/ferroportin and the IRE/IRP regulatory systems balance systemic and cellular iron metabolism, respectively, and understanding their points of intersection and crosstalk represents a major challenge in iron biology. I will discuss an emerging picture from studies with different mutant mouse lines according to which the “cellular” IRE/IRP system determines “set points” via its targets (including ferroportin and HIF2α). These are then subject to modulation via hepcidin in response to systemic cues. Disclosures: No relevant conflicts of interest to declare.

scholarly journals Iron-regulatory proteins: molecular biology and pathophysiological implications

2007 ◽  
Vol 9 (33) ◽  
pp. 1-13 ◽  
Author(s):  
Gaetano Cairo ◽  
Stefania Recalcati
Keyword(s):  
Cell Growth ◽  
Molecular Biology ◽  
Iron Metabolism ◽  
Iron Homeostasis ◽  
Regulatory Proteins ◽  
Cellular Functions ◽  
Major Health ◽  
Iron Regulatory Proteins ◽  
Human Disorders ◽  
Apoptosis And Inflammation

AbstractIron is required for key cellular functions, and there is a strong link between iron metabolism and important metabolic processes, such as cell growth, apoptosis and inflammation. Diseases that are directly or indirectly related to iron metabolism represent major health problems. Iron-regulatory proteins (IRPs) 1 and 2 are key controllers of vertebrate iron metabolism and post-transcriptionally regulate expression of the major iron homeostasis genes. Here we discuss how dysregulation of the IRP system can result from both iron-related and unrelated effectors and explain how this can have important pathological consequences in several human disorders.

Iron regulatory protein-1 and -2: transcriptome-wide definition of binding mRNAs and shaping of the cellular proteome by iron regulatory proteins

Blood ◽  
2011 ◽  
Vol 118 (22) ◽  
pp. e168-e179 ◽  
Author(s):  
Mayka Sanchez ◽  
Bruno Galy ◽  
Bjoern Schwanhaeusser ◽  
Jonathon Blake ◽  
Tomi Bähr-Ivacevic ◽  
...  
Keyword(s):  
Iron Metabolism ◽  
Rna Binding ◽  
Isotope Labeling ◽  
Rna Binding Proteins ◽  
Regulatory Protein ◽  
Regulatory Proteins ◽  
Iron Regulatory Proteins ◽  
Ribonucleoprotein Complexes ◽  
Cellular Iron ◽  
Irp1 And Irp2

Abstract Iron regulatory proteins (IRPs) 1 and 2 are RNA-binding proteins that control cellular iron metabolism by binding to conserved RNA motifs called iron-responsive elements (IREs). The currently known IRP-binding mRNAs encode proteins involved in iron uptake, storage, and release as well as heme synthesis. To systematically define the IRE/IRP regulatory network on a transcriptome-wide scale, IRP1/IRE and IRP2/IRE messenger ribonucleoprotein complexes were immunoselected, and the mRNA composition was determined using microarrays. We identify 35 novel mRNAs that bind both IRP1 and IRP2, and we also report for the first time cellular mRNAs with exclusive specificity for IRP1 or IRP2. To further explore cellular iron metabolism at a system-wide level, we undertook proteomic analysis by pulsed stable isotope labeling by amino acids in cell culture in an iron-modulated mouse hepatic cell line and in bone marrow-derived macrophages from IRP1- and IRP2-deficient mice. This work investigates cellular iron metabolism in unprecedented depth and defines a wide network of mRNAs and proteins with iron-dependent regulation, IRP-dependent regulation, or both.

Iron regulatory proteins and their role in controlling iron metabolism

Metallomics ◽  
2015 ◽  
Vol 7 (2) ◽  
pp. 232-243 ◽  
Author(s):  
Lukas C. Kühn
Keyword(s):  
Iron Metabolism ◽  
Iron Uptake ◽  
Iron Homeostasis ◽  
Regulatory Proteins ◽  
Feedback Mechanisms ◽  
Iron Regulatory Proteins ◽  
Body Iron ◽  
Transcriptional Feedback

Cellular and body iron homeostasis are regulated by iron-sensing and post-transcriptional feedback mechanisms, which control iron uptake, release, storage and heme biosythesis.

scholarly journals Oxalomalate, a competitive inhibitor of aconitase, modulates the RNA-binding activity of iron-regulatory proteins

2000 ◽  
Vol 348 (2) ◽  
pp. 315-320 ◽  
Author(s):  
Michela FESTA ◽  
Alfredo COLONNA ◽  
Concetta PIETROPAOLO ◽  
Alfredo RUFFO
Keyword(s):  
Iron Metabolism ◽  
Rna Binding ◽  
Competitive Inhibitor ◽  
Binding Activity ◽  
Regulatory Proteins ◽  
Mobility Shift ◽  
Prolonged Incubation ◽  
Iron Regulatory Proteins

We investigated the effect of oxalomalate (OMA, α-hydroxy-β-oxalosuccinic acid), a competitive inhibitor of aconitase, on the RNA-binding activity of the iron-regulatory proteins (IRP1 and IRP2) that control the post-transcriptional expression of various proteins involved in iron metabolism. The RNA-binding activity of IRP was evaluated by electrophoretic mobility-shift assay of cell lysates from 3T3-L1 mouse fibroblasts, SH-SY5Y human cells and mouse livers incubated in vitro with OMA, with and without 2-mercaptoethanol (2-ME). Analogous experiments were performed in vivo by prolonged incubation (72 h) of 3T3-L1 cells with OMA, and by injecting young mice with equimolar concentrations of oxaloacetate and glyoxylate, which are the precursors of OMA synthesis. OMA remarkably decreased the binding activity of IRP1 and, when present, of IRP2, in all samples analysed. In addition, the recovery of IRP1 by 2-ME in the presence of OMA was constantly lower versus control values. These findings suggest that the severe decrease in IRP1 RNA-binding activity depends on: (i) linking of OMA to the active site of aconitase, which prevents the switch to IRP1 and explains resistance to the reducing agents, and (ii) possible interaction of OMA with some functional amino acid residues in IRP that are responsible for binding to the specific mRNA sequences involved in the regulation of iron metabolism.

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