Labile iron pool as a parameter to monitor iron overload and oxidative stress status in β‐thalassemic erythrocytes

Chutvanichkul, Boonyanuch; Vattanaviboon, Paiboon; Mas-Oodi, Sumana; U-Pratya, Yaowalak; Wanachiwanawin, Wanchai

doi:10.1002/cyto.b.21633

Cited by 29 publications

(14 citation statements)

References 16 publications

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“…2A). The decreased iron resistance is most likely related to the increased levels of chelatable iron, as the amount of “free” chelatable iron has been reported to trigger the production of toxic hydroxyl radicals 90,91. Notably, the depletion of Nfs1 or GSH caused a significantly higher increase in iron uptake and cellular iron accumulation compared to the inactivation of MrsA (Fig.…”

Section: Resultsmentioning

confidence: 91%

Iron-sensing is governed by mitochondrial, not by cytosolic iron–sulfur cluster biogenesis inAspergillus fumigatus

et al. 2018

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Section: Resultsmentioning

confidence: 91%

Iron-sensing is governed by mitochondrial, not by cytosolic iron–sulfur cluster biogenesis inAspergillus fumigatus

et al. 2018

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“…Hydrogen peroxide can donate 2e − to the ferrylheme radical cation to produce ferriheme and water in a peroxidase-like reaction (Alayash et al, 2001). Second, ferrylheme radical cation can abstract a hydrogen atom from unsaturated lipids to produce lipid peroxides (Chutvanichkul et al, 2018) and Fe(4+)=O. In a second reaction, Fe(4+)=O abstracts an electron from a second lipid or other reducing substance to generate methemoglobin and a second radical (Nagababu and Rifkind, 2000;Potor et al, 2013).…”

Section: Hemoglobin Redox Cyclingmentioning

confidence: 99%

“…hemoglobin degradation. At any given time there is an amount of iron available in the cytosol to be used elsewhere; this ill-defined feature is the Labile Iron Pool (LIP) and acts as a steady-state repository for iron as it is shuffled between demands (Chutvanichkul et al, 2018;Philpott et al, 2020). The composition of the LIP is not clearly defined, no specific set of molecules have been found associated with intracellular iron.…”

Section: Mechanism Of Ferroptosismentioning

confidence: 99%

The Chemical Basis of Intracerebral Hemorrhage and Cell Toxicity With Contributions From Eryptosis and Ferroptosis

Derry

Gnanansekaran

et al. 2020

Front. Cell. Neurosci.

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Intracerebral hemorrhage (ICH) is a particularly devastating event both because of the direct injury from space-occupying blood to the sequelae of the brain exposed to free blood components from which it is normally protected. Not surprisingly, the usual metabolic and energy pathways are overwhelmed in this situation. In this review article, we detail the complexity of red blood cell degradation, the contribution of eryptosis leading to hemoglobin breakdown into its constituents, the participants in that process, and the points at which injury can be propagated such as elaboration of toxic radicals through the metabolism of the breakdown products. Two prominent products of this breakdown sequence, hemin, and iron, induce a variety of pathologies including free radical damage and DNA breakage, which appear to include events independent from typical oxidative DNA injury. As a result of this confluence of damaging elements, multiple pathways of injury, cell death, and survival are likely engaged including ferroptosis (which may be the same as oxytosis but viewed from a different perspective) and senescence, suggesting that targeting any single cause will likely not be a sufficient strategy to maximally improve outcome. Combination therapies in addition to safe methods to reduce blood burden should be pursued.

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“…For instance, Fe-S clusters have been assigned both a structural and redox role in DNA repair proteins and other enzymes [6][7][8]. In addition to protein-embedded iron, a limited quantity of free iron is also available in cells, in what is called the free-iron pool (FIP) [9][10][11]. FIP is constituted by iron in both II and III oxidation states and the metal is usually complexed with different, and not very well characterized, ligands and chelatants [12].…”

Section: Introductionmentioning

confidence: 99%

The Iron Maiden. Cytosolic Aconitase/IRP1 Conformational Transition in the Regulation of Ferritin Translation and Iron Hemostasis

et al. 2021

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Maintaining iron homeostasis is fundamental for almost all living beings, and its deregulation correlates with severe and debilitating pathologies. The process is made more complicated by the omnipresence of iron and by its role as a fundamental component of a number of crucial metallo proteins. The response to modifications in the amount of the free-iron pool is performed via the inhibition of ferritin translation by sequestering consensus messenger RNA (mRNA) sequences. In turn, this is regulated by the iron-sensitive conformational equilibrium between cytosolic aconitase and IRP1, mediated by the presence of an iron–sulfur cluster. In this contribution, we analyze by full-atom molecular dynamics simulation, the factors leading to both the interaction with mRNA and the conformational transition. Furthermore, the role of the iron–sulfur cluster in driving the conformational transition is assessed by obtaining the related free energy profile via enhanced sampling molecular dynamics simulations.

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Labile iron pool as a parameter to monitor iron overload and oxidative stress status in β‐thalassemic erythrocytes

Abstract: The LIP assay is suggested as an alternative test to monitor the magnitude of iron overload and its consequent oxidative stress in β-thalassemia. LIP level may also be used as a marker for therapeutic response to iron chelation treatment. © 2018 International Clinical Cytometry Society.

Cited by 29 publications

References 16 publications

Iron-sensing is governed by mitochondrial, not by cytosolic iron–sulfur cluster biogenesis inAspergillus fumigatus

Iron-sensing is governed by mitochondrial, not by cytosolic iron–sulfur cluster biogenesis inAspergillus fumigatus

The Chemical Basis of Intracerebral Hemorrhage and Cell Toxicity With Contributions From Eryptosis and Ferroptosis

The Iron Maiden. Cytosolic Aconitase/IRP1 Conformational Transition in the Regulation of Ferritin Translation and Iron Hemostasis

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