| pubmed-article:1321148 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1321148 | lifeskim:mentions | umls-concept:C0024662 | lld:lifeskim |
| pubmed-article:1321148 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:1321148 | lifeskim:mentions | umls-concept:C0071349 | lld:lifeskim |
| pubmed-article:1321148 | lifeskim:mentions | umls-concept:C1418269 | lld:lifeskim |
| pubmed-article:1321148 | lifeskim:mentions | umls-concept:C0243077 | lld:lifeskim |
| pubmed-article:1321148 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:1321148 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:1321148 | lifeskim:mentions | umls-concept:C1449693 | lld:lifeskim |
| pubmed-article:1321148 | pubmed:issue | 20 | lld:pubmed |
| pubmed-article:1321148 | pubmed:dateCreated | 1992-8-14 | lld:pubmed |
| pubmed-article:1321148 | pubmed:abstractText | Oligomeric ellagitannins (nobotanins B, E, and K) were found to be potent inhibitors of poly(ADP-ribose) glycohydrolase purified from mouse mammary tumor 34I cells. Kinetic analysis revealed that the inhibition of nobotanin B (dimer) was competitive with respect to the substrate poly(ADP-ribose), whereas nobotanin E (trimer) and nobotanin K (tetramer) exhibited mixed-type inhibition. These results suggest that the dimeric structure of ellagitannin may have a functional domain that competes with poly(ADP-ribose) on the poly(ADP-ribose) glycohydrolase molecule. To determine the inhibitory effects of oligomeric ellagitannins on poly(ADP-ribose) glycohydrolase in vivo, we examined their effects on de-poly(ADP-ribosyl)ation of some chromosomal proteins in intact 34I cells that was induced by glucocorticoid treatment. Nobotanin B caused concentration-dependent inhibition of glucocorticoid-induced de-poly(ADP-ribosyl)ation of HMG 14 and 17 and histone H1 in intact 34I cells. Interestingly, this inhibition was associated with suppression of the glucocorticoid-sensitive mouse mammary tumor virus (MMTV) mRNA synthesis. In contrast, nobotanin E and K had little inhibitory effect on either de-poly(ADP-ribosyl)ation of these proteins or induction of MMTV transcription after glucocorticoid treatment. Nobotanin B but not E and K was taken into 34I cells. These results may suggest that the suppression of glucocorticoid-sensitive MMTV transcription results from in vivo inhibition of poly(ADP-ribose) glycohydrolase by nobotanin B. These results also indicate the importance of de-poly(ADP-ribosyl)ation of HMG 14 and 17 and histone H1 in regulation of transcription of the glucocorticoid-sensitive MMTV gene. | lld:pubmed |
| pubmed-article:1321148 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1321148 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1321148 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1321148 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1321148 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1321148 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1321148 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1321148 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1321148 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:1321148 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:1321148 | pubmed:author | pubmed-author:AbeHH | lld:pubmed |
| pubmed-article:1321148 | pubmed:author | pubmed-author:OkudaTT | lld:pubmed |
| pubmed-article:1321148 | pubmed:author | pubmed-author:AokiTT | lld:pubmed |
| pubmed-article:1321148 | pubmed:author | pubmed-author:MarutaHH | lld:pubmed |
| pubmed-article:1321148 | pubmed:author | pubmed-author:HatanoTT | lld:pubmed |
| pubmed-article:1321148 | pubmed:author | pubmed-author:TanumaSS | lld:pubmed |
| pubmed-article:1321148 | pubmed:author | pubmed-author:SakagamiHH | lld:pubmed |
| pubmed-article:1321148 | pubmed:author | pubmed-author:SARIAA | lld:pubmed |
| pubmed-article:1321148 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1321148 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:1321148 | pubmed:volume | 267 | lld:pubmed |
| pubmed-article:1321148 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1321148 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1321148 | pubmed:pagination | 14436-42 | lld:pubmed |
| pubmed-article:1321148 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:1321148 | pubmed:meshHeading | pubmed-meshheading:1321148-... | lld:pubmed |
| pubmed-article:1321148 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1321148 | pubmed:articleTitle | Mouse mammary tumor virus gene expression is suppressed by oligomeric ellagitannins, novel inhibitors of poly(ADP-ribose) glycohydrolase. | lld:pubmed |
| pubmed-article:1321148 | pubmed:affiliation | Department of Pharmacology, Faculty of Medical Sciences, Taipei Medical College, Taiwan, Republic of China. | lld:pubmed |
| pubmed-article:1321148 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1321148 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:1321148 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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