| pubmed-article:18841468 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18841468 | lifeskim:mentions | umls-concept:C0013018 | lld:lifeskim |
| pubmed-article:18841468 | lifeskim:mentions | umls-concept:C0034721 | lld:lifeskim |
| pubmed-article:18841468 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
| pubmed-article:18841468 | lifeskim:mentions | umls-concept:C0031847 | lld:lifeskim |
| pubmed-article:18841468 | lifeskim:mentions | umls-concept:C0007776 | lld:lifeskim |
| pubmed-article:18841468 | lifeskim:mentions | umls-concept:C0022655 | lld:lifeskim |
| pubmed-article:18841468 | lifeskim:mentions | umls-concept:C0001613 | lld:lifeskim |
| pubmed-article:18841468 | lifeskim:mentions | umls-concept:C0039067 | lld:lifeskim |
| pubmed-article:18841468 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:18841468 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:18841468 | pubmed:dateCreated | 2009-3-20 | lld:pubmed |
| pubmed-article:18841468 | pubmed:abstractText | The NO donor 3-Morpholinosydnonimine (SIN-1) releases NO in the presence of molecular oxygen. In this study, we evaluated the effect of SIN-1 on mitochondria of rat cortical synaptosomes. We demonstrated in vitro that the amount of ONOO(-) generated and H(2)O(2) formation directly correlated with SIN-1 concentration. The mean oxygen consumption by synaptosomal mitochondria was approximately 3.8 nmol of O(2) min(-1) mg(-1) protein, which decreased significantly in the presence of SIN-1 1 mM to 2.5 nmol O(2) min(-1) mg(-1). This decrease was not modified by catalase or Trolox, demonstrating that ONOO(-) was responsible for the effect. The same concentration of SIN-1 caused a significant decrease of ATP production by synaptosomal mitochondria and depolarized the mitochondrial membrane. Moreover, ROS production increased progressively and was completely inhibited by pre-incubation of synaptosomes with Trolox. Finally, phosphatidylserine was externalized and, at the same time, intrasynaptosomal lactate dehydrogenase decreased confirming both, the external membrane breakdown after the addition of SIN-1 and the damage to the synaptosomes. | lld:pubmed |
| pubmed-article:18841468 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18841468 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18841468 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18841468 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18841468 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18841468 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18841468 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18841468 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18841468 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18841468 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18841468 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18841468 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18841468 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18841468 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18841468 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18841468 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18841468 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18841468 | pubmed:month | May | lld:pubmed |
| pubmed-article:18841468 | pubmed:issn | 1573-6903 | lld:pubmed |
| pubmed-article:18841468 | pubmed:author | pubmed-author:PessinaG PGP | lld:pubmed |
| pubmed-article:18841468 | pubmed:author | pubmed-author:PalmiMM | lld:pubmed |
| pubmed-article:18841468 | pubmed:author | pubmed-author:Blanco... | lld:pubmed |
| pubmed-article:18841468 | pubmed:author | pubmed-author:ValotiMM | lld:pubmed |
| pubmed-article:18841468 | pubmed:author | pubmed-author:BuonocoreGG | lld:pubmed |
| pubmed-article:18841468 | pubmed:author | pubmed-author:AldinucciCC | lld:pubmed |
| pubmed-article:18841468 | pubmed:author | pubmed-author:MaiorcaS MSM | lld:pubmed |
| pubmed-article:18841468 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18841468 | pubmed:volume | 34 | lld:pubmed |
| pubmed-article:18841468 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18841468 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18841468 | pubmed:pagination | 931-41 | lld:pubmed |
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| pubmed-article:18841468 | pubmed:meshHeading | pubmed-meshheading:18841468... | lld:pubmed |
| pubmed-article:18841468 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:18841468 | pubmed:articleTitle | Physiopathological effects of the NO donor 3-morpholinosydnonimine on rat cortical synaptosomes. | lld:pubmed |
| pubmed-article:18841468 | pubmed:affiliation | Department of Physiology, University of Siena, Siena, Italy. | lld:pubmed |
| pubmed-article:18841468 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18841468 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:18841468 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
