pubmed-article:18817763 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:18817763 | lifeskim:mentions | umls-concept:C0206745 | lld:lifeskim |
pubmed-article:18817763 | lifeskim:mentions | umls-concept:C0019904 | lld:lifeskim |
pubmed-article:18817763 | lifeskim:mentions | umls-concept:C0006104 | lld:lifeskim |
pubmed-article:18817763 | lifeskim:mentions | umls-concept:C1171362 | lld:lifeskim |
pubmed-article:18817763 | lifeskim:mentions | umls-concept:C0441889 | lld:lifeskim |
pubmed-article:18817763 | lifeskim:mentions | umls-concept:C1539081 | lld:lifeskim |
pubmed-article:18817763 | lifeskim:mentions | umls-concept:C1705525 | lld:lifeskim |
pubmed-article:18817763 | lifeskim:mentions | umls-concept:C1417708 | lld:lifeskim |
pubmed-article:18817763 | lifeskim:mentions | umls-concept:C1423613 | lld:lifeskim |
pubmed-article:18817763 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
pubmed-article:18817763 | lifeskim:mentions | umls-concept:C0429403 | lld:lifeskim |
pubmed-article:18817763 | pubmed:dateCreated | 2008-11-5 | lld:pubmed |
pubmed-article:18817763 | pubmed:abstractText | The role of nuclear factor kappa B (NF-kappaB) in oxidative stress, and most recently in pro- and anti-apoptotic-related mechanistic pathways, has well been established. Because of the dual nature of NF-kappaB, the wide range of genes it regulates and the plethora of stimuli that activate it, various studies addressing the functional role of NF-kappaB proteins have resulted in a number of differing findings. The present study examined the effect of a stimulus-free environment on the frontal cortex of mice brain with the p50 subunit of NF-kappaB knocked out p50 (-/-). Homozygous p50 mice knockout (KO) and wild type (WT) were used, and at 7-9 weeks they were sacrificed and various brain regions dissected. We analyzed the levels of oxidation in the frontal cortex of both the p50 (-/-) and WT mice. There was a significant reduction in the levels of protein-bound 4-hydroxynonenal (HNE) [a lipid peroxidation product], 3-nitrotyrosine (3NT), and protein carbonyls in the p50 (-/-) mice when compared to the WT. A proteomic profile analysis identified ATP synthase gamma chain, ubiquinol-cyt-C reductase, heat shock protein 10 (Hsp10), fructose bisphosphate aldolase C, and NADH-ubiquinone oxidoreductase as proteins whose expressions were significantly increased in the p50 (-/-) mice compared to the WT. With the reduction in the levels of oxidative stress and the increase in expression of key proteins in the p50 (-/-) brain, this study suggests that the p50 subunit can potentially be targeted for the development of therapeutic interventions in disorders in which oxidative stress plays a key role. | lld:pubmed |
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pubmed-article:18817763 | pubmed:language | eng | lld:pubmed |
pubmed-article:18817763 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18817763 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:18817763 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18817763 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:18817763 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18817763 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:18817763 | pubmed:month | Nov | lld:pubmed |