| pubmed-article:20600834 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20600834 | lifeskim:mentions | umls-concept:C0007600 | lld:lifeskim |
| pubmed-article:20600834 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:20600834 | lifeskim:mentions | umls-concept:C0006826 | lld:lifeskim |
| pubmed-article:20600834 | lifeskim:mentions | umls-concept:C2347026 | lld:lifeskim |
| pubmed-article:20600834 | lifeskim:mentions | umls-concept:C0370003 | lld:lifeskim |
| pubmed-article:20600834 | lifeskim:mentions | umls-concept:C0079419 | lld:lifeskim |
| pubmed-article:20600834 | lifeskim:mentions | umls-concept:C0312586 | lld:lifeskim |
| pubmed-article:20600834 | lifeskim:mentions | umls-concept:C0205369 | lld:lifeskim |
| pubmed-article:20600834 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:20600834 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:20600834 | pubmed:dateCreated | 2010-7-27 | lld:pubmed |
| pubmed-article:20600834 | pubmed:abstractText | Previously, we reported that human p53 is functionally inactivated by S-glutathionylation at Cys-141 during oxidative and DNA-damaging treatments. Here, we describe the presence of thiolated p53 and the dynamic nature of this modification in human tissues using unique and specific polyclonal antibodies raised against a 12-residue p53 peptide bearing a mixed disulfide at Cys-141. The affinity- purified antibodies (glut-p53) were sequence-specific in that they recognized the antigenic peptide but not the unthiolated peptide or a scrambled glutathionylated peptide in ELISAs. On immunoblots, the purified antibodies did not react with native p53 or recombinant p53 (rp53), but readily detected the glutathionylated or cysteinylated or ethanethiol-treated rp53 only under nonreducing conditions. Untreated HCT116 cells showed low levels of glut-p53, which increased markedly after H(2)O(2), diamide, cisplatin, and doxorubicin treatments. Glut-p53 levels decreased sharply after cells were passed into oxidant-free medium, suggesting efficient dethiolation. The mutant p53 present in HT29 and T47D human cancer cells was also recognized. In vitro, the glut-p53 was rapidly degraded by rabbit reticulocyte lysates. Human prostate and prostate cancer tissues showed an abundant presence of glut-p53 in luminal epithelium, a site well known to generate ROS. Melanoma and colon cancer samples were also positive for glut-p53. The availability of the thiolation-specific antibodies should enhance our knowledge of p53 regulation in redox-perturbed states found in various diseases including cancer. | lld:pubmed |
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| pubmed-article:20600834 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20600834 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20600834 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20600834 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:20600834 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20600834 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:20600834 | pubmed:issn | 1873-4596 | lld:pubmed |
| pubmed-article:20600834 | pubmed:author | pubmed-author:SrivenugopalK... | lld:pubmed |
| pubmed-article:20600834 | pubmed:author | pubmed-author:BhatG... | lld:pubmed |
| pubmed-article:20600834 | pubmed:author | pubmed-author:YusufMohd AMA | lld:pubmed |
| pubmed-article:20600834 | pubmed:author | pubmed-author:ChuangTrinett... | lld:pubmed |
| pubmed-article:20600834 | pubmed:copyrightInfo | Copyright 2010 Elsevier Inc. All rights reserved. | lld:pubmed |
| pubmed-article:20600834 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20600834 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:20600834 | pubmed:volume | 49 | lld:pubmed |
| pubmed-article:20600834 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20600834 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20600834 | pubmed:pagination | 908-17 | lld:pubmed |
| pubmed-article:20600834 | pubmed:dateRevised | 2011-9-13 | lld:pubmed |
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