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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Landry, Aaron P. Cheng, Zishuo Ding, Huangen |
| Description | Country affiliation: United States Author Affiliation: Landry AP ( Department of Biological Sciences, Louisiana State University, Baton Rouge, LA 70803, USA.); Cheng Z ( Department of Biological Sciences, Louisiana State University, Baton Rouge, LA 70803, USA.); Ding H ( Department of Biological Sciences, Louisiana State University, Baton Rouge, LA 70803, USA. Electronic address: hding@lsu.edu.) |
| Abstract | The human mitochondrial outer membrane protein mitoNEET is a newly discovered target of the type 2 diabetes drug pioglitazone. Structurally, mitoNEET is a homodimer with each monomer containing an N-terminal transmembrane helix tethered to the mitochondrial outer membrane and a C-terminal cytosolic domain hosting a redox-active [2Fe-2S] cluster. Genetic studies have shown that mitoNEET has a central role in regulating energy metabolism in mitochondria. However, the specific function of mitoNEET remains largely elusive. Here we find that the mitoNEET [2Fe-2S] clusters can be efficiently reduced by Escherichia coli thioredoxin reductase and glutathione reductase in an NADPH-dependent reaction. Purified human glutathione reductase has the same activity as E. coli thioredoxin reductase and glutathione reductase to reduce the mitoNEET [2Fe-2S] clusters. However, rat thioredoxin reductase, a human thioredoxin reductase homolog that contains selenocysteine in the catalytic center, has very little or no activity to reduce the mitoNEET [2Fe-2S] clusters. N-ethylmaleimide, a potent thiol modifier, completely inhibits human glutathione reductase from reducing the mitoNEET [2Fe-2S] clusters, indicating that the redox-active disulfide in the catalytic center of human glutathione reductase may be directly involved in reducing the mitoNEET [2Fe-2S] clusters. Additional studies reveal that the reduced mitoNEET [2Fe-2S] clusters in mouse heart cell extracts can be reversibly oxidized by hydrogen peroxide without disruption of the clusters, suggesting that the mitoNEET [2Fe-2S] clusters may undergo redox transition to regulate energy metabolism in mitochondria in response to oxidative signals. |
| File Format | HTM / HTML |
| ISSN | 08915849 |
| e-ISSN | 18734596 |
| DOI | 10.1016/j.freeradbiomed.2015.01.017 |
| Journal | Free Radical Biology and Medicine |
| Volume Number | 81 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2015-04-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Discipline Free radicals biology Glutathione Reductase Metabolism Mitochondria, Heart Mitochondrial Membranes Mitochondrial Proteins Animals Escherichia Coli Genetics Escherichia Coli Proteins Chemistry Ethylmaleimide Pharmacology Gene Expression Hydrogen Peroxide Iron-sulfur Proteins Mice Drug Effects Myocardium Oxidation-reduction Recombinant Proteins Thiazolidinediones Thioredoxin-disulfide Reductase Research Support, N.i.h., Extramural Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Physiology (medical) Biochemistry |
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