Human iron transporters

Garrick, Michael D.

doi:10.1007/s12263-010-0184-8

Cited by 49 publications

(33 citation statements)

References 57 publications

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“…It is a component of heme and iron-sulphur centers in many key redox enzymes, and is an essential component of oxygen storage and transporting proteins such as haemoglobin and myoglobin (Andrews, 1999). It is also an integral part of several classes of enzymes involved in the synthesis of steroid hormones, detoxifi cation of foreign substances in the liver, synthesis of neurotransmitters and DNA synthesis and breakdown (Garrick, 2011). In all species, the concentration of iron in biological fl uids is tightly regulated to provide iron as needed and to avoid toxicity, because iron excess can lead to the generation of reactive oxygen species (ROS) by catalyzing the Fenton reaction and highly generates reactive hydroxyl radicals, which can damage the lipid membranes, proteins and nucleic acids (Eaton and Qian, 2002;Gao et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

Protective effects of lycopene on oxidative stress, proliferation and autophagy in iron supplementation rats

et al. 2013

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Lycopene is common in diet and known for its antioxidant activities. However, the impact of lycopene on iron metabolism is poorly investigated. In this study, we hypothesize that lycopene can prevent iron-mediated oxidative stress, proliferation and autophagy in liver and use a rat model of nutritional iron supplementation to confi rm its intervention in these defence mechanisms. We found that iron supplementation induced cell proliferation predominantly in non parenchymal cells compared with hepatocytes, but not apoptosis. In addition, iron was accumulated within the hepatic lysosomes where it triggered autophagy as evidenced by the formation of autophagic vesicles detected by LC3-B staining. Iron supplementation also induced morphologic alterations of the mitochondrial membranes probably due to increased lipid peroxidation as indicated by elevated iron and malondialdehyde concentrations in serum and tissues. Lycopene reduced iron-catalyzed lipid peroxidation by decreasing the malondialdehyde level in the liver and colon and enhancing the total superoxide dismutase activities in serum and tissues. The result suggest that lycopene prevents iron-induced oxidative stress, proliferation and autophagy at both biochemical and histological levels due to its potent free radical scavenging and antioxidant properties.

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Section: Introductionmentioning

confidence: 99%

Protective effects of lycopene on oxidative stress, proliferation and autophagy in iron supplementation rats

et al. 2013

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“…Cells may also uptake nontransferrin-bound iron probably through surface DMT1 or other not yet fully characterized transporters. 5 To avoid the detrimental Fenton reaction and ROS generation, excess iron is rapidly sequestered and safely stored by cytosolic ferritin, a shell protein formed by assembled L (FtL) and H (FtH) ferritin subunits. 6 Alternatively, excess iron is exported by ferroportin (Fpn).…”

Section: Introductionmentioning

confidence: 99%

Iron increases the susceptibility of multiple myeloma cells to bortezomib

et al. 2012

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ABSTRACTbeen reported following proteasome inhibition in cells treated with H 2 O 2 and nitric oxide generators. 13,14 Ferritin might undergo proteasomal degradation to recycle stored iron in cells pre-loaded with ferric ammonium citrate (FAC) 15 in conditions of decreased cell iron content 16,17 or in the presence of oxidative stress stimuli. 18 Here we report the analysis of iron metabolism and the effects of iron manipulation in MM cell lines and primary cells of patients treated with bortezomib. We observed that the basal iron storage capacity of MM cell lines directly correlates with bortezomib resistance and that bortezomib sensitizes MM cells to iron toxicity. Manipulation of iron homeostasis might be a tool to increase the susceptibility of MM cells to the effect of bortezomib and to overcome bortezomib resistance. Design and Methods Cell culture and cellular extractsCell culture media and reagents were from Invitrogen (Karlsruhe, Germany) and from Sigma-Aldrich (St. Louis, MO, USA). Bortezomib was purchased from LC Laboratories (Wobun, MA, USA). Patient-derived plasma cells were purified from bone marrow aspirates by density gradient centrifugation and then by CD138 immunomagnetic positive selection (Miltenyi Biotec, Bergisch Gladbach, Germany). Samples from Patient 2 were collected both at diagnosis (sample a) and relapse (sample b). Informed consent was obtained in accordance with the Declaration of Helsinki and the approval for use of primary samples was obtained from the Institutional Review Board of the San Raffaele Scientific Institute. MM cell lines and primary cells were cultured in RPMI medium supplemented with 10% fetal bovine serum (FBS), 100 units/mL penicillin, 100 mg/mL streptomycin and 2 mM L-glutamine.Cellular extracts were prepared as described in the Online Supplementary Appendix. Iron manipulationsIron removal was obtained by addition of deferoxamine (DFO; Biofutura Pharma, Milan, Italy). Ferric ammonium citrate (FAC), holo-transferrin (FeTf) (Sigma-Aldrich) and N-acetyl Cysteine (NAC) (Sigma-Aldrich) were used for iron loading experiments. FAC and 55 FeAC were prepared by mixing FeCl 3 -HCl (Merk Millipore, Billerica, MA, USA) or 55 FeCl 3 -HCl (PerkinElmer, Monza, Italy) with citric acid at 1:2 ratios and then by adjusting pH to 7.4 with NH 4 OH.To estimate ferritin content in patients' cells, cellular extracts were incubated in vitro with a molar excess of 55 FeAC plus ascorbic acid. Then extracts were loaded without heating on sodium dodecylsulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and exposed to autoradiography. Cell viabilityCell viability was determined by measuring the reduction of 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) (Sigma-Aldrich). Briefly, cells were seeded in 96-well plates and assay performed on at least three wells for every condition. MTT was then added for 3 h at a final concentration of 0.25 mg/mL. Plates were centrifuged at 3200g for 5 min and the soluble fraction decanted. Crystal pellets were suspended in DMSO a...

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“…El transporte de metales se acopla con el transporte de protones. Los tejidos en los que se sintetiza esta proteína son el intestino, la médula ósea, la placenta, el hígado, los pulmones, los riñones y el músculo esquelético (11,14,18,27,28).…”

Section: El Transportador 1 De Metales Divalentes (Dmt1)unclassified

“…El DMT1-No IRE por su parte, se encarga de expulsar el hierro de los endosomas durante el ciclo de la transferrina (11,27,29), lo cual se abordará posteriormente.…”

Section: El Transportador 1 De Metales Divalentes (Dmt1)unclassified

Proteínas relacionadas con el metabolismo del hierro corporal

Corrales-Agudelo¹,

Sosa

Herrera

2017

Perspect Nutr Humana

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Como citar este artículo: Corrales-Agudelo V, Parra-Sosa BE, Burgos-Herrera LC. Proteínas relacionadas con el metabolismo del hierro corporal. Perspect Nutr Humana. 2016;18:95-116. DOI:10.17533/udea.penh.v18n1a08 Proteínas relacionadas con el metabolismo del hierro corporal ResumenAntecedentes: el hierro es uno de los minerales más estudiados; existe amplia información en cuanto a su metabolismo, función, interacciones y regulación; sin embargo, los estudios y análisis realizados se basan en proteínas específicas y pocos integran, en un solo texto, las características de estas moléculas relacionadas con el metabolismo del hierro corporal. Objetivo: profundizar en los aspectos moleculares, metabólicos y de modulación de las proteínas que participan en la homeostasis del hierro y en sus interacciones. Materiales y métodos: se hizo una búsqueda sistemática de información en bases de datos científicas de artículos sobre el tema, publicados entre 2006 y 2016. Resultados: la homeostasis del hierro corporal, es un proceso complejo y altamente regulado por diferentes moléculas que participan de manera integrada en su metabolismo; en los últimos años han surgido nuevas proteínas, algunas de ellas participan en el transporte de otros nutrientes y se les ha encontrado relación con el control humoral y celular del hierro; además, involucran la participación de varios órganos, tejidos y sistemas. Esta revisión incluye proteínas encargadas de facilitar el aprovechamiento biológico del nutriente, así como aquellas que protegen a las células de toxicidad por exceso de este mineral.Palabras clave: hierro, proteínas de unión al hierro, expresión génica, oxidación-reducción, homeostasis, deficiencia de hierro. Proteínas del metabolismo del hierro 96Vol. 18, N° 1, enero-junio de 2016Proteins associated with the metabolism of total body iron Abstract Background: Iron is an essential nutrient well studied for its role in human health, and much evidence exists regarding its metabolism, functions, interactions, and regulations. However, studies and analyses that have been done are often based on specific proteins and few integrate into a single text the characteristics of multiple proteins related to total body iron metabolism. Objective: Explore in-depth the molecular, metabolic, and modulation aspects of proteins that participate in iron homeostasis and related interactions. Materials and methods: A literature review was completed using scientific databases in conjunction with a search for related scientific articles published between 2006 and 2016. Results: Homeostasis of total body iron stores is a complex process that is highly regulated by various molecules that participate in an integrated manner in iron metabolism. In recent years, new proteins have been discovered regarding the humoral and cellular control of iron, some of which are also involved in the transport of other nutrients. Additionally, these proteins involve participation from various organs, tissues, and systems. This review includes proteins responsible for ...

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Human iron transporters

Cited by 49 publications

References 57 publications

Protective effects of lycopene on oxidative stress, proliferation and autophagy in iron supplementation rats

Protective effects of lycopene on oxidative stress, proliferation and autophagy in iron supplementation rats

Iron increases the susceptibility of multiple myeloma cells to bortezomib

Proteínas relacionadas con el metabolismo del hierro corporal

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