Iron speciation in the cytosol: an overview

Hider, Robert C.; Kong, Xiaole

doi:10.1039/c2dt32149a

Cited by 145 publications

(112 citation statements)

References 100 publications

(124 reference statements)

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“…3A&B). This K M value for Fe lies within the measured chelatable Fe in the cellular labile iron pool (35). TMfrn1 readily transports Co, Cu, and Zn while Mn is a poorer substrate (Fig.…”

Section: Expressionmentioning

confidence: 71%

In vitro reconstitution, functional dissection, and mutational analysis of metal ion transport by mitoferrin-1

Christenson

Gallegos

Banerjee

2018

Journal of Biological Chemistry

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Mitoferrin-1 is a promiscuous transition metal transporterThe reactivity of iron is exploited across all kingdoms of life. The physiological roles that iron takes on are many-iron readily participates in redox reactions where it can donate or accept electrons, depending on its oxidation state. Iron plays essential roles in gas transport and sensing and can also act as a non-redox active metal ion cofactor in enzymes. Additionally, iron-containing cofactors can impart stability to folded proteins (1). Iron naturally occurs in the 2+ and the 3+ oxidation states but owing to the insolubility of Fe(III), the bioavailable form of iron is almost exclusively the 2+ form. The main route of cellular iron uptake is via the transferrin receptor pathway whereby transferrin-bound iron is targeted to endosomes and subsequently released from transferrin during endosomal acidification. Fe(II) is transported out of endosomes by divalent metal ion transporter (DMT1) and becomes available for incorporation into iron-containing proteins and cofactors (2).In eukaryotes, mitochondria are the hotspots for iron utilization-these organelles house heme assembly and the majority of Fe-S cluster biosynthesis apparatus (3,4). Mitochondria contain respiratory complexes which comprise many ironcontaining cofactors. Not surprisingly, http://www.jbc.org/cgi

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“…3A&B). This K M value for Fe lies within the measured chelatable Fe in the cellular labile iron pool (35). TMfrn1 readily transports Co, Cu, and Zn while Mn is a poorer substrate (Fig.…”

Section: Expressionmentioning

confidence: 71%

In vitro reconstitution, functional dissection, and mutational analysis of metal ion transport by mitoferrin-1

Christenson

Gallegos

Banerjee

2018

Journal of Biological Chemistry

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“…The main storage protein is ferritin, but other storage proteins exist such as hemosiderin [11,12]. Additionally, cells possess a pool of free iron known as the labile iron pool [13]. This pool is considered transient but necessary as the source of iron for newly synthesized proteins that require iron as a co-factor.…”

Section: +mentioning

confidence: 99%

Iron, Aging, and Neurodegeneration

Angelova

Brown

2015

Metals

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Abstract:Iron is a trace element of considerable interest to both chemistry and biology. In a biological context its chemistry is vital to the roles it performs. However, that same chemistry can contribute to a more deleterious role in a variety of diseases. The brain is a very sensitive organ due to the irreplaceable nature of neurons. In this regard regulation of brain iron chemistry is essential to maintaining neuronal viability. During the course of normal aging, the brain changes the way it deals with iron and this can contribute to its susceptibility to disease. Additionally, many of the known neurodegenerative diseases have been shown to be influenced by changes in brain iron. This review examines the role of iron in the brain and neurodegenerative diseases and the potential role of changes in brain iron caused by aging.

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“…[6] However deferiprone has two disadvantages, namely rapid metabolism [7] and initiation of reversible agranulocytosis in approximately 1% of patients receiving the drug. [8] Metabolism leads to glucuronidation of the 3-hydroxyl function, [7] thereby removing the chelating ability of the molecule.…”

Section: Introductionmentioning

confidence: 99%

Systematic comparison of the mono-, dimethyl- and trimethyl 3-hydroxy-4(1H)-pyridones – Attempted optimization of the orally active iron chelator, deferiprone

Xie

Kong

et al. 2016

European Journal of Medicinal Chemistry

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. Systematic comparison of the mono-, dimethyl-and trimethyl 3-hydroxy-4(1H)-pyridones -attempted optimization of the orally active iron chelator, deferiprone. EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY. https://doi.org/10.1016/j.ejmech.2016.03.014 Citing this paperPlease note that where the full-text provided on King's Research Portal is the Author Accepted Manuscript or Post-Print version this may differ from the final Published version. If citing, it is advised that you check and use the publisher's definitive version for pagination, volume/issue, and date of publication details. And where the final published version is provided on the Research Portal, if citing you are again advised to check the publisher's website for any subsequent corrections. General rightsCopyright and moral rights for the publications made accessible in the Research Portal are retained by the authors and/or other copyright owners and it is a condition of accessing publications that users recognize and abide by the legal requirements associated with these rights.•Users may download and print one copy of any publication from the Research Portal for the purpose of private study or research.•You may not further distribute the material or use it for any profit-making activity or commercial gain •You may freely distribute the URL identifying the publication in the Research Portal Take down policyIf you believe that this document breaches copyright please contact librarypure@kcl.ac.uk providing details, and we will remove access to the work immediately and investigate your claim. This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain.

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Iron speciation in the cytosol: an overview

Cited by 145 publications

References 100 publications

In vitro reconstitution, functional dissection, and mutational analysis of metal ion transport by mitoferrin-1

In vitro reconstitution, functional dissection, and mutational analysis of metal ion transport by mitoferrin-1

Iron, Aging, and Neurodegeneration

Systematic comparison of the mono-, dimethyl- and trimethyl 3-hydroxy-4(1H)-pyridones – Attempted optimization of the orally active iron chelator, deferiprone

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