| pubmed-article:19887391 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19887391 | lifeskim:mentions | umls-concept:C0034721 | lld:lifeskim |
| pubmed-article:19887391 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
| pubmed-article:19887391 | lifeskim:mentions | umls-concept:C0299583 | lld:lifeskim |
| pubmed-article:19887391 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:19887391 | lifeskim:mentions | umls-concept:C0243192 | lld:lifeskim |
| pubmed-article:19887391 | lifeskim:mentions | umls-concept:C1121571 | lld:lifeskim |
| pubmed-article:19887391 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
| pubmed-article:19887391 | lifeskim:mentions | umls-concept:C1709059 | lld:lifeskim |
| pubmed-article:19887391 | lifeskim:mentions | umls-concept:C1612060 | lld:lifeskim |
| pubmed-article:19887391 | lifeskim:mentions | umls-concept:C0965514 | lld:lifeskim |
| pubmed-article:19887391 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:19887391 | pubmed:dateCreated | 2010-1-19 | lld:pubmed |
| pubmed-article:19887391 | pubmed:abstractText | The adipose tissue hormone leptin and homocysteine (Hcy)-thiolactone are linked to the pathogenesis of atherosclerosis through their interactions with the anti-atherogenic enzyme paraoxonase 1 that has the ability to hydrolyze Hcy-thiolactone and minimizes protein N-homocysteinylation. Here we examined the relationships between hyperleptinemia, Hcy-thiolactonase, and protein N-homocysteinylation in rats. Hyperleptinemia was induced in adult rats by administration of leptin for 7 days (0.25 mg/kg twice daily s.c). We found that serum Hcy-thiolactonase was lower in hyperleptinemic than in control animals (-41.0%, P<0.001). Leptin administration increased the level of N-linked Hcy in plasma proteins (+92.9%, P<0.01), but had no effect on plasma total Hcy. These effects were not reproduced by pair-feeding. We also found that the synthetic liver X receptor (LXR) agonist, T0901317 (1 mg/kg per day) normalized Hcy-thiolactonase and protein N-homocysteinylation levels in leptin-treated rats. However, leptin-induced increase in plasma isoprostane levels (a marker of oxidative stress) was not normalized by T0901317. The NADPH oxidase inhibitor apocynin prevented leptin-induced increase in isoprostane levels but did not normalize Hcy-thiolactonase and protein N-homocysteinylation levels. These results suggest that the decreased capacity to metabolize Hcy-thiolactone and concomitant increase in protein N-homocysteinylation contribute to pro-atherogenic effect of chronic hyperleptinemia, independently of oxidative stress. LXR agonists normalize Hcy-thiolactonase levels and decrease protein N-homocysteinylation, especially under conditions associated with excess leptin such as metabolic syndrome. | lld:pubmed |
| pubmed-article:19887391 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19887391 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19887391 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19887391 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19887391 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19887391 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19887391 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19887391 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19887391 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19887391 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19887391 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19887391 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19887391 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19887391 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19887391 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19887391 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19887391 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19887391 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:19887391 | pubmed:issn | 1479-6805 | lld:pubmed |
| pubmed-article:19887391 | pubmed:author | pubmed-author:WójcickaGrazy... | lld:pubmed |
| pubmed-article:19887391 | pubmed:author | pubmed-author:JakubowskiHie... | lld:pubmed |
| pubmed-article:19887391 | pubmed:author | pubmed-author:BeltowskiJerz... | lld:pubmed |
| pubmed-article:19887391 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19887391 | pubmed:volume | 204 | lld:pubmed |
| pubmed-article:19887391 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19887391 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19887391 | pubmed:pagination | 191-8 | lld:pubmed |
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| pubmed-article:19887391 | pubmed:meshHeading | pubmed-meshheading:19887391... | lld:pubmed |
| pubmed-article:19887391 | pubmed:meshHeading | pubmed-meshheading:19887391... | lld:pubmed |
| pubmed-article:19887391 | pubmed:meshHeading | pubmed-meshheading:19887391... | lld:pubmed |
| pubmed-article:19887391 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:19887391 | pubmed:articleTitle | Modulation of paraoxonase 1 and protein N-homocysteinylation by leptin and the synthetic liver X receptor agonist T0901317 in the rat. | lld:pubmed |
| pubmed-article:19887391 | pubmed:affiliation | Department of Pathophysiology, Medical University, 20-090 Lublin, Poland. jerzy.beltowski@am.lublin.pl | lld:pubmed |
| pubmed-article:19887391 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19887391 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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