Source:http://linkedlifedata.com/resource/pubmed/id/10833524
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
33
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| pubmed:dateCreated |
2000-9-21
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| pubmed:abstractText |
Transfectant HeLa cells were generated that expressed human ferritin H-chain wild type and an H-chain mutant with inactivated ferroxidase activity under the control of the tetracycline-responsive promoter (Tet-off). The clones accumulated exogenous ferritins up to levels 14-16-fold over background, half of which were as H-chain homopolymers. This had no evident effect in the mutant ferritin clone, whereas it induced an iron-deficient phenotype in the H-ferritin wild type clone, manifested by approximately 5-fold increase of IRPs activity, approximately 2.5-fold increase of transferrin receptor, approximately 1.8-fold increase in iron-transferrin iron uptake, and approximately 50% reduction of labile iron pool. Overexpression of the H-ferritin, but not of the mutant ferritin, strongly reduced cell growth and increased resistance to H(2)O(2) toxicity, effects that were reverted by prolonged incubation in iron-supplemented medium. The results show that in HeLa cells H-ferritin regulates the metabolic iron pool with a mechanism dependent on the functionality of the ferroxidase centers, and this affects, in opposite directions, cellular growth and resistance to oxidative damage. This, and the finding that also in vivo H-chain homopolymers are much less efficient than the H/L heteropolymers in taking up iron, indicate that functional activity of H-ferritin in HeLa cells is that predicted from the in vitro data.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Bacterial Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Apoferritins,
http://linkedlifedata.com/resource/pubmed/chemical/Ceruloplasmin,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Doxycycline,
http://linkedlifedata.com/resource/pubmed/chemical/Ferritins,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrogen Peroxide,
http://linkedlifedata.com/resource/pubmed/chemical/Iron,
http://linkedlifedata.com/resource/pubmed/chemical/Tetracycline
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| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
|
| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
18
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| pubmed:volume |
275
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
25122-9
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| pubmed:dateRevised |
2008-11-21
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| pubmed:meshHeading |
pubmed-meshheading:10833524-Anti-Bacterial Agents,
pubmed-meshheading:10833524-Apoferritins,
pubmed-meshheading:10833524-Cell Division,
pubmed-meshheading:10833524-Ceruloplasmin,
pubmed-meshheading:10833524-DNA, Complementary,
pubmed-meshheading:10833524-Doxycycline,
pubmed-meshheading:10833524-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:10833524-Ferritins,
pubmed-meshheading:10833524-HeLa Cells,
pubmed-meshheading:10833524-Humans,
pubmed-meshheading:10833524-Hydrogen Peroxide,
pubmed-meshheading:10833524-Immunoblotting,
pubmed-meshheading:10833524-Iron,
pubmed-meshheading:10833524-Mutagenesis,
pubmed-meshheading:10833524-Mutation,
pubmed-meshheading:10833524-Oxidative Stress,
pubmed-meshheading:10833524-Plasmids,
pubmed-meshheading:10833524-Precipitin Tests,
pubmed-meshheading:10833524-Promoter Regions, Genetic,
pubmed-meshheading:10833524-Tetracycline,
pubmed-meshheading:10833524-Time Factors,
pubmed-meshheading:10833524-Transfection
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| pubmed:year |
2000
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| pubmed:articleTitle |
Overexpression of wild type and mutated human ferritin H-chain in HeLa cells: in vivo role of ferritin ferroxidase activity.
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| pubmed:affiliation |
Dibit, Department of Biological and Technological Research, IRCCS H. San Raffaele, Milano, Italy.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|