| pubmed-article:9314607 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9314607 | lifeskim:mentions | umls-concept:C0178539 | lld:lifeskim |
| pubmed-article:9314607 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:9314607 | lifeskim:mentions | umls-concept:C0017817 | lld:lifeskim |
| pubmed-article:9314607 | lifeskim:mentions | umls-concept:C0333668 | lld:lifeskim |
| pubmed-article:9314607 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:9314607 | pubmed:dateCreated | 1997-11-14 | lld:pubmed |
| pubmed-article:9314607 | pubmed:abstractText | This investigation tested the hypothesis that depletion of intracellular glutathione, in contrast to its oxidation could lead to non-native oxidation of protein thiols, thereby trapping proteins in an unstable conformation. Chinese hamster cells were exposed to the alpha, beta-unsaturated dicarboxylic acid diethylmaleate in order to produce rapid glutathione (GSH) depletion without oxidation. Measurement of the fluorescence of oxidized 2',7'-dichlorofluorescein diacetate indicated that reactive oxygen species accumulated in GSH depleted cells. Glutathione depletion was found to alter protein thiol/disulfide exchange ratios such that 17 to 23 nmol of protein SH/mg protein underwent oxidation. Differential scanning calorimetry (DSC) of glutathione depleted cells yielded a profile of specific heat capacity versus temperature that was characteristic of cells containing destabilized and denatured protein. In addition, cells depleted of glutathione exhibited a two-fold increase in NP-40 insoluble protein. These results indicate that depletion of intracellular glutathione caused oxidation of protein thiols, protein denaturation and aggregation and provide a mechanism to explain how GSH depletion can initiate stress responses. | lld:pubmed |
| pubmed-article:9314607 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9314607 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9314607 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9314607 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9314607 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9314607 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9314607 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9314607 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9314607 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9314607 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9314607 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:9314607 | pubmed:issn | 1355-8145 | lld:pubmed |
| pubmed-article:9314607 | pubmed:author | pubmed-author:FreemanM LML | lld:pubmed |
| pubmed-article:9314607 | pubmed:author | pubmed-author:MeredithM JMJ | lld:pubmed |
| pubmed-article:9314607 | pubmed:author | pubmed-author:LepockJJ | lld:pubmed |
| pubmed-article:9314607 | pubmed:author | pubmed-author:SenisterraG... | lld:pubmed |
| pubmed-article:9314607 | pubmed:author | pubmed-author:HuntleyS ASA | lld:pubmed |
| pubmed-article:9314607 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9314607 | pubmed:volume | 2 | lld:pubmed |
| pubmed-article:9314607 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9314607 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9314607 | pubmed:pagination | 191-8 | lld:pubmed |
| pubmed-article:9314607 | pubmed:dateRevised | 2008-11-20 | lld:pubmed |
| pubmed-article:9314607 | pubmed:meshHeading | pubmed-meshheading:9314607-... | lld:pubmed |
| pubmed-article:9314607 | pubmed:meshHeading | pubmed-meshheading:9314607-... | lld:pubmed |
| pubmed-article:9314607 | pubmed:meshHeading | pubmed-meshheading:9314607-... | lld:pubmed |
| pubmed-article:9314607 | pubmed:meshHeading | pubmed-meshheading:9314607-... | lld:pubmed |
| pubmed-article:9314607 | pubmed:meshHeading | pubmed-meshheading:9314607-... | lld:pubmed |
| pubmed-article:9314607 | pubmed:meshHeading | pubmed-meshheading:9314607-... | lld:pubmed |
| pubmed-article:9314607 | pubmed:meshHeading | pubmed-meshheading:9314607-... | lld:pubmed |
| pubmed-article:9314607 | pubmed:meshHeading | pubmed-meshheading:9314607-... | lld:pubmed |
| pubmed-article:9314607 | pubmed:meshHeading | pubmed-meshheading:9314607-... | lld:pubmed |
| pubmed-article:9314607 | pubmed:meshHeading | pubmed-meshheading:9314607-... | lld:pubmed |
| pubmed-article:9314607 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9314607 | pubmed:articleTitle | Destabilization and denaturation of cellular protein by glutathione depletion. | lld:pubmed |
| pubmed-article:9314607 | pubmed:affiliation | Vanderbilt Center for Radiation Oncology, Vanderbilt University School of Medicine, Nashville, TN 37232, USA. Freemaml@ctrvax.vanderbilt.edu | lld:pubmed |
| pubmed-article:9314607 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9314607 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9314607 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9314607 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9314607 | lld:pubmed |
