Document Detail

Characterization of nuclear ferritin and mechanism of translocation.
MedLine Citation:
PMID:  15675895     Owner:  NLM     Status:  MEDLINE    
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.
Nodar Surguladze; Stephanie Patton; Anna Cozzi; Michael G Fried; James R Connor
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Biochemical journal     Volume:  388     ISSN:  1470-8728     ISO Abbreviation:  Biochem. J.     Publication Date:  2005 Jun 
Date Detail:
Created Date:  2005-06-06     Completed Date:  2005-12-13     Revised Date:  2014-09-16    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  England    
Other Details:
Languages:  eng     Pagination:  731-40     Citation Subset:  IM    
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MeSH Terms
Active Transport, Cell Nucleus
Alloxan / pharmacology
Cell Line, Tumor
Cell Nucleus / metabolism*
Cytoplasm / metabolism
Deoxyribonucleases / metabolism
Ferritins / biosynthesis,  chemistry,  genetics,  metabolism*
Glycosylation / drug effects
Iron / chemistry,  metabolism
Protein Biosynthesis
Protein Subunits
RNA Interference
RNA, Messenger / genetics,  metabolism
Grant Support
Reg. No./Substance:
0/Protein Subunits; 0/RNA, Messenger; 6SW5YHA5NG/Alloxan; 9007-73-2/Ferritins; 9013-31-4/Apoferritins; E1UOL152H7/Iron; EC 3.1.-/Deoxyribonucleases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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