| pubmed-article:16890185 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16890185 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:16890185 | lifeskim:mentions | umls-concept:C0003402 | lld:lifeskim |
| pubmed-article:16890185 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:16890185 | lifeskim:mentions | umls-concept:C0149925 | lld:lifeskim |
| pubmed-article:16890185 | lifeskim:mentions | umls-concept:C0162638 | lld:lifeskim |
| pubmed-article:16890185 | lifeskim:mentions | umls-concept:C2825097 | lld:lifeskim |
| pubmed-article:16890185 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:16890185 | pubmed:dateCreated | 2006-8-14 | lld:pubmed |
| pubmed-article:16890185 | pubmed:abstractText | It has been suggested that the alpha-class glutathione S-transferases (GSTs) protect various cell types from oxidative stress and lipid peroxidation (LPO). In order to examine the protective role of alpha-class GST isozyme hGSTA1-1 against doxorubicin (DOX)-induced lipid peroxidation, cytotoxicity, and apoptosis, human small cell lung cancer (SCLC) H69 cells were stably transfected with hGSTA1. Immunological and biochemical characterization of hGSTA1-transfected cells revealed the expression of functionally active hGSTA1-1 localized near the cellular plasma membranes. hGSTA1-transfected cells acquired significantly increased resistance to the DOX-induced cytotoxicity by suppressing lipid peroxidation levels in these cells. Overexpression of hGSTA1-1 in cells inhibited DOX-mediated depletion of GSH and higher GSH levels were found in DOX-treated hGSTA1-transfected cells as compared with empty vector-transfected controls. hGSTA1-1 overexpression also provided protection to cells from DOX-induced apoptosis by inhibiting phosphorylation of c-Jun-N-terminal kinases (JNK), caspase-3 activation, and by preserving the levels of anti-apoptotic protein Bcl-2. These results are consistent with the idea that the alpha-class GSTs provide protection against oxidative stress by attenuating lipid peroxidation and these enzymes can modulate signaling for apoptosis. | lld:pubmed |
| pubmed-article:16890185 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16890185 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16890185 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16890185 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16890185 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16890185 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16890185 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16890185 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16890185 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16890185 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16890185 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16890185 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16890185 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:16890185 | pubmed:issn | 0003-9861 | lld:pubmed |
| pubmed-article:16890185 | pubmed:author | pubmed-author:LoyMM | lld:pubmed |
| pubmed-article:16890185 | pubmed:author | pubmed-author:AwasthiSanjay... | lld:pubmed |
| pubmed-article:16890185 | pubmed:author | pubmed-author:AwasthiYogesh... | lld:pubmed |
| pubmed-article:16890185 | pubmed:author | pubmed-author:SharmaRajendr... | lld:pubmed |
| pubmed-article:16890185 | pubmed:author | pubmed-author:SharmaAbhaA | lld:pubmed |
| pubmed-article:16890185 | pubmed:author | pubmed-author:PatrickBradB | lld:pubmed |
| pubmed-article:16890185 | pubmed:author | pubmed-author:JeyabalPrince... | lld:pubmed |
| pubmed-article:16890185 | pubmed:author | pubmed-author:ReddyPrasada... | lld:pubmed |
| pubmed-article:16890185 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16890185 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:16890185 | pubmed:volume | 452 | lld:pubmed |
| pubmed-article:16890185 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16890185 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16890185 | pubmed:pagination | 165-73 | lld:pubmed |
| pubmed-article:16890185 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:16890185 | pubmed:meshHeading | pubmed-meshheading:16890185... | lld:pubmed |
| pubmed-article:16890185 | pubmed:meshHeading | pubmed-meshheading:16890185... | lld:pubmed |
| pubmed-article:16890185 | pubmed:meshHeading | pubmed-meshheading:16890185... | lld:pubmed |
| pubmed-article:16890185 | pubmed:meshHeading | pubmed-meshheading:16890185... | lld:pubmed |
| pubmed-article:16890185 | pubmed:meshHeading | pubmed-meshheading:16890185... | lld:pubmed |
| pubmed-article:16890185 | pubmed:meshHeading | pubmed-meshheading:16890185... | lld:pubmed |
| pubmed-article:16890185 | pubmed:meshHeading | pubmed-meshheading:16890185... | lld:pubmed |
| pubmed-article:16890185 | pubmed:meshHeading | pubmed-meshheading:16890185... | lld:pubmed |
| pubmed-article:16890185 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16890185 | pubmed:articleTitle | Glutathione S-transferases as antioxidant enzymes: small cell lung cancer (H69) cells transfected with hGSTA1 resist doxorubicin-induced apoptosis. | lld:pubmed |
| pubmed-article:16890185 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX, USA. | lld:pubmed |
| pubmed-article:16890185 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16890185 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16890185 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16890185 | lld:pubmed |
