| Characterization of nuclear ferritin and mechanism of translocation. | |
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MedLine Citation:
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PMID: 15675895 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Ferritin, normally considered a cytoplasmic iron-storage protein, is also found in cell nuclei. It is an established fact that H-ferritin is the major form of nuclear ferritin, but little is known about the roles of ferritin in nuclei or about the mechanisms that control its appearance within the nuclear volume. In the present study, we show that, for human SW1088 astrocytoma cells, the nuclear and cytoplasmic forms of H-ferritin are products of the same mRNA. Histochemical and biochemical evidence is presented showing that ferritin is distributed non-randomly within the nuclear volume and that it preferentially associates with heterochromatin. Both cytoplasmic and nuclear populations of H-ferritin contain mixtures of non- and O-glycosylated forms, but the nuclear population is enriched in O-glycosylated forms. Cells treated with alloxan, a potent inhibitor of O-glycosylation, contained significantly less nuclear ferritin compared with cells grown in control media. Alloxan inhibited the reappearance of H-ferritin in nuclei of cells released from conditions of iron depletion, but did not prevent its disappearance from nuclei of cells undergoing iron depletion. These results suggest that O-glycosylation accompanies the transfer of ferritin from the cytoplasm to the nucleus, but does not influence the reverse process. The picture that emerges is one in which ferritin translocation between the cytoplasm and the nucleus is post-translationally regulated and responds to environmental and nutritional cues. |
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Authors:
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Nodar Surguladze; Stephanie Patton; Anna Cozzi; Michael G Fried; James R Connor |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: The Biochemical journal Volume: 388 ISSN: 1470-8728 ISO Abbreviation: Biochem. J. Publication Date: 2005 Jun |
Date Detail:
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Created Date: 2005-06-06 Completed Date: 2005-12-13 Revised Date: 2011-09-26 |
Medline Journal Info:
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Nlm Unique ID: 2984726R Medline TA: Biochem J Country: England |
Other Details:
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Languages: eng Pagination: 731-40 Citation Subset: IM |
Affiliation:
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Department of Neurosurgery, The Pennsylvania State University College of Medicine, 500 University Drive, Hershey, PA 17033, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Active Transport, Cell Nucleus Alloxan / pharmacology Apoferritins Cell Line, Tumor Cell Nucleus / metabolism* Cytoplasm / metabolism Deoxyribonucleases / metabolism Ferritins / biosynthesis, chemistry, genetics, metabolism* Glycosylation / drug effects Humans Iron / chemistry, metabolism Protein Biosynthesis Protein Subunits RNA Interference RNA, Messenger / genetics, metabolism |
| Grant Support | |
ID/Acronym/Agency:
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DK54289/DK/NIDDK NIH HHS; R01 GM070662-01/GM/NIGMS NIH HHS; R01 GM070662-02/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Protein Subunits; 0/RNA, Messenger; 50-71-5/Alloxan; 7439-89-6/Iron; 9007-73-2/Ferritins; 9013-31-4/Apoferritins; EC 3.1.-/Deoxyribonucleases |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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