| pubmed-article:10880356 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10880356 | lifeskim:mentions | umls-concept:C0035647 | lld:lifeskim |
| pubmed-article:10880356 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:10880356 | lifeskim:mentions | umls-concept:C0185125 | lld:lifeskim |
| pubmed-article:10880356 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:10880356 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
| pubmed-article:10880356 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:10880356 | lifeskim:mentions | umls-concept:C1521840 | lld:lifeskim |
| pubmed-article:10880356 | pubmed:issue | Pt 2 | lld:pubmed |
| pubmed-article:10880356 | pubmed:dateCreated | 2001-1-26 | lld:pubmed |
| pubmed-article:10880356 | pubmed:abstractText | Site-specific S-glutathionylation is emerging as a novel mechanism by which S-nitrosoglutathione (GSNO) may modify functionally important protein thiols. Here, we show that GSNO-Sepharose mimicks site-specific S-glutathionylation of the transcription factors c-Jun and p50 by free GSNO in vitro. Both c-Jun and p50 were found to bind to immobilized GSNO through the formation of a mixed disulphide, involving a conserved cysteine residue located in the DNA-binding domains of these transcription factors. Furthermore, we show that c-Jun, p50, glycogen phosphorylase b, glyceraldehyde-3-phosphate dehydrogenase, creatine kinase, glutaredoxin and caspase-3 can be precipitated from a mixture of purified thiol-containing proteins by the formation of a mixed-disulphide bond with GSNO-Sepharose. With few exceptions, protein binding to this matrix correlated well with the susceptibility of the investigated proteins to undergo GSNO- but not diamide-induced mixed-disulphide formation in vitro. Finally, it is shown that covalent GSNO-Sepharose chromatography of HeLa cell nuclear extracts results in the enrichment of proteins which incorporate glutathione in response to GSNO treatment. As suggested by DNA-binding assays, this group of nuclear proteins include the transcription factors activator protein-1, nuclear factor-kappaB and cAMP-response-element-binding protein. In conclusion, we introduce GSNO-Sepharose as a probe for site-specific S-glutathionylation and as a novel and potentially useful tool to isolate and identify proteins which are candidate targets for GSNO-induced mixed-disulphide formation. | lld:pubmed |
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| pubmed-article:10880356 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10880356 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10880356 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10880356 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10880356 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10880356 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:10880356 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:10880356 | pubmed:author | pubmed-author:KlattPP | lld:pubmed |
| pubmed-article:10880356 | pubmed:author | pubmed-author:LamasSS | lld:pubmed |
| pubmed-article:10880356 | pubmed:author | pubmed-author:Pérez-SalaDD | lld:pubmed |
| pubmed-article:10880356 | pubmed:author | pubmed-author:Pineda... | lld:pubmed |
| pubmed-article:10880356 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10880356 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:10880356 | pubmed:volume | 349 | lld:pubmed |
| pubmed-article:10880356 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10880356 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10880356 | pubmed:pagination | 567-78 | lld:pubmed |
| pubmed-article:10880356 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:10880356 | pubmed:meshHeading | pubmed-meshheading:10880356... | lld:pubmed |
| pubmed-article:10880356 | pubmed:meshHeading | pubmed-meshheading:10880356... | lld:pubmed |
| pubmed-article:10880356 | pubmed:meshHeading | pubmed-meshheading:10880356... | lld:pubmed |
| pubmed-article:10880356 | pubmed:meshHeading | pubmed-meshheading:10880356... | lld:pubmed |
| pubmed-article:10880356 | pubmed:meshHeading | pubmed-meshheading:10880356... | lld:pubmed |
