| pubmed-article:7504626 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7504626 | lifeskim:mentions | umls-concept:C0028128 | lld:lifeskim |
| pubmed-article:7504626 | lifeskim:mentions | umls-concept:C0024432 | lld:lifeskim |
| pubmed-article:7504626 | lifeskim:mentions | umls-concept:C0378503 | lld:lifeskim |
| pubmed-article:7504626 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
| pubmed-article:7504626 | lifeskim:mentions | umls-concept:C1515877 | lld:lifeskim |
| pubmed-article:7504626 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:7504626 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:7504626 | pubmed:dateCreated | 1994-1-10 | lld:pubmed |
| pubmed-article:7504626 | pubmed:abstractText | Biosynthesis of nitric oxide (NO) from L-arginine modulates activity of iron-dependent enzymes, including mitochondrial acontiase, an [Fe-S] protein. We examined the effect of NO on the activity of iron regulatory factor (IRF), a cytoplasmic protein which modulates both ferritin mRNA translation and transferrin receptor mRNA stability by binding to specific mRNA sequences called iron responsive elements (IREs). Murine macrophages were activated with interferon-gamma and lipopolysaccharide to induce NO synthase activity and cultured in the presence or absence of NG-substituted analogues of L-arginine which served as selective inhibitors of NO synthesis. Measurement of the nitrite concentration in the culture medium was taken as an index of NO production. Mitochondria-free cytosols were then prepared and aconitase activity as well as IRE binding activity and induction of IRE binding activity were correlated and depended on NO synthesis after IFN-gamma and/or LPS stimulation. Authentic NO gas as well as the NO-generating compound 3-morpholinosydnonimine (SIN-1) also conversely modulated aconitase and IRE binding activities of purified recombinant IRF. These results provide evidence that endogenously produced NO may modulate the post-transcriptional regulation of genes involved in iron homeostasis and support the hypothesis that the [Fe-S] cluster of IRF mediates iron-dependent regulation. | lld:pubmed |
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| pubmed-article:7504626 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7504626 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7504626 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7504626 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7504626 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7504626 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:7504626 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:7504626 | pubmed:author | pubmed-author:WietzerbinJJ | lld:pubmed |
| pubmed-article:7504626 | pubmed:author | pubmed-author:KühnL CLC | lld:pubmed |
| pubmed-article:7504626 | pubmed:author | pubmed-author:DrapierJ CJC | lld:pubmed |
| pubmed-article:7504626 | pubmed:author | pubmed-author:KaldyPP | lld:pubmed |
