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  • Homeostasis  (4)
  • American Association for the Advancement of Science (AAAS)  (4)
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  • American Association for the Advancement of Science (AAAS)  (4)
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  • 1
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    Regulation of mitochondrial iron accumulation by Yfh1p, a putative homolog of frataxin (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-06-13
    Description: The gene responsible for Friedreich's ataxia, a disease characterized by neurodegeneration and cardiomyopathy, has recently been cloned and its product designated frataxin. A gene in Saccharomyces cerevisiae was characterized whose predicted protein product has high sequence similarity to the human frataxin protein. The yeast gene (yeast frataxin homolog, YFH1) encodes a mitochondrial protein involved in iron homeostasis and respiratory function. Human frataxin also was shown to be a mitochondrial protein. Characterizing the mechanism by which YFH1 regulates iron homeostasis in yeast may help to define the pathologic process leading to cell damage in Friedreich's ataxia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Babcock, M -- de Silva, D -- Oaks, R -- Davis-Kaplan, S -- Jiralerspong, S -- Montermini, L -- Pandolfo, M -- Kaplan, J -- DK30534/DK/NIDDK NIH HHS/ -- DK49219/DK/NIDDK NIH HHS/ -- NS34192/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1997 Jun 13;276(5319):1709-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, School of Medicine, University of Utah, Salt Lake City, UT 84132, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9180083" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Transport ; Carrier Proteins/metabolism ; Cell Membrane/metabolism ; *Ceruloplasmin ; Cytosol/metabolism ; Friedreich Ataxia/metabolism ; Fungal Proteins/genetics/*metabolism ; Genes, Fungal ; Genetic Complementation Test ; Homeostasis ; Humans ; Iron/*metabolism ; *Iron-Binding Proteins ; Membrane Transport Proteins/metabolism ; Mitochondria/*metabolism ; Oxidative Stress ; Oxidoreductases/metabolism ; Phosphotransferases (Alcohol Group Acceptor)/metabolism ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/genetics/growth & development/*metabolism ; *Saccharomyces cerevisiae Proteins ; Transformation, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-10-30
    Description: Hepcidin is a peptide hormone secreted by the liver in response to iron loading and inflammation. Decreased hepcidin leads to tissue iron overload, whereas hepcidin overproduction leads to hypoferremia and the anemia of inflammation. Ferroportin is an iron exporter present on the surface of absorptive enterocytes, macrophages, hepatocytes, and placental cells. Here we report that hepcidin bound to ferroportin in tissue culture cells. After binding, ferroportin was internalized and degraded, leading to decreased export of cellular iron. The posttranslational regulation of ferroportin by hepcidin may thus complete a homeostatic loop: Iron regulates the secretion of hepcidin, which in turn controls the concentration of ferroportin on the cell surface.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nemeth, Elizabeta -- Tuttle, Marie S -- Powelson, Julie -- Vaughn, Michael B -- Donovan, Adriana -- Ward, Diane McVey -- Ganz, Tomas -- Kaplan, Jerry -- DK065029/DK/NIDDK NIH HHS/ -- DK30534/DK/NIDDK NIH HHS/ -- HL26922/HL/NHLBI NIH HHS/ -- T35HL007744/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2004 Dec 17;306(5704):2090-3. Epub 2004 Oct 28.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, David Geffen School of Medicine, University of California, Los Angeles, CA, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15514116" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antimicrobial Cationic Peptides/chemical ; synthesis/genetics/*metabolism/pharmacology ; Biological Transport ; Cation Transport Proteins/*metabolism ; Cell Line ; Cell Membrane/metabolism ; Cytosol/metabolism ; Ferritins/metabolism ; HeLa Cells ; Hepcidins ; Homeostasis ; Humans ; Iron/*metabolism ; Iron Regulatory Protein 2/metabolism ; Lysosomes/metabolism ; Mice ; Protein Binding ; RNA, Messenger/genetics/metabolism ; Receptor, Epidermal Growth Factor/metabolism ; Recombinant Fusion Proteins/metabolism ; Transfection ; Transferrin/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Localization of iron in Arabidopsis seed requires the vacuolar membrane transporter VIT1 (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-11-04
    Description: Iron deficiency is a major human nutritional problem wherever plant-based diets are common. Using synchrotron x-ray fluorescence microtomography to directly visualize iron in Arabidopsis seeds, we show that iron is localized primarily to the provascular strands of the embryo. This localization is completely abolished when the vacuolar iron uptake transporter VIT1 is disrupted. Vacuolar iron storage is also critical for seedling development because vit1-1 seedlings grow poorly when iron is limiting. We have uncovered a fundamental aspect of seed biology that will ultimately aid the development of nutrient-rich seed, benefiting both human health and agricultural productivity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, Sun A -- Punshon, Tracy -- Lanzirotti, Antonio -- Li, Liangtao -- Alonso, Jose M -- Ecker, Joseph R -- Kaplan, Jerry -- Guerinot, Mary Lou -- DK 30534/DK/NIDDK NIH HHS/ -- P42 ES07373/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 2006 Nov 24;314(5803):1295-8. Epub 2006 Nov 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Dartmouth College, Hanover, NH 03755, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17082420" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/genetics/growth & development/*metabolism ; Arabidopsis Proteins/genetics/*metabolism ; Cation Transport Proteins/genetics/*metabolism ; Cotyledon/chemistry ; Homeostasis ; Hypocotyl/chemistry ; Image Processing, Computer-Assisted ; Intracellular Membranes/metabolism ; Iron/analysis/*metabolism ; Manganese/analysis ; Mutation ; Plant Epidermis/chemistry ; Plants, Genetically Modified ; Recombinant Fusion Proteins/metabolism ; Seedlings/growth & development ; Seeds/chemistry/*metabolism ; Tomography, X-Ray Computed ; Vacuoles/chemistry/*metabolism ; Zinc/analysis
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    A heme export protein is required for red blood cell differentiation and iron homeostasis (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-02-09
    Description: Hemoproteins are critical for the function and integrity of aerobic cells. However, free heme is toxic. Therefore, cells must balance heme synthesis with its use. We previously demonstrated that the feline leukemia virus, subgroup C, receptor (FLVCR) exports cytoplasmic heme. Here, we show that FLVCR-null mice lack definitive erythropoiesis, have craniofacial and limb deformities resembling those of patients with Diamond-Blackfan anemia, and die in midgestation. Mice with FLVCR that is deleted neonatally develop a severe macrocytic anemia with proerythroblast maturation arrest, which suggests that erythroid precursors export excess heme to ensure survival. We further demonstrate that FLVCR mediates heme export from macrophages that ingest senescent red cells and regulates hepatic iron. Thus, the trafficking of heme, and not just elemental iron, facilitates erythropoiesis and systemic iron balance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Keel, Sioban B -- Doty, Raymond T -- Yang, Zhantao -- Quigley, John G -- Chen, Jing -- Knoblaugh, Sue -- Kingsley, Paul D -- De Domenico, Ivana -- Vaughn, Michael B -- Kaplan, Jerry -- Palis, James -- Abkowitz, Janis L -- New York, N.Y. -- Science. 2008 Feb 8;319(5864):825-8. doi: 10.1126/science.1151133.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Hematology, University of Washington, Seattle, WA 98195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18258918" target="_blank"〉PubMed〈/a〉
    Keywords: Anemia, Diamond-Blackfan/blood/pathology ; Animals ; Antimicrobial Cationic Peptides/metabolism ; Embryo Loss ; Embryonic Development ; Erythroblasts/cytology/metabolism ; *Erythropoiesis ; Heme/*metabolism ; Hepatocytes/metabolism ; Hepcidins ; Homeostasis ; Iron/*metabolism ; Macrophages/metabolism ; Membrane Transport Proteins/genetics/*metabolism ; Mice ; Receptors, Virus/genetics/*metabolism ; Red-Cell Aplasia, Pure/blood/pathology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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