Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
20
|
| pubmed:dateCreated |
1992-8-14
|
| 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.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jul
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
267
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
14436-42
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:1321148-Animals,
pubmed-meshheading:1321148-Binding, Competitive,
pubmed-meshheading:1321148-Cell Nucleus,
pubmed-meshheading:1321148-Gene Expression,
pubmed-meshheading:1321148-Gene Expression Regulation, Viral,
pubmed-meshheading:1321148-Genes, Viral,
pubmed-meshheading:1321148-Glycoside Hydrolases,
pubmed-meshheading:1321148-Hydrolyzable Tannins,
pubmed-meshheading:1321148-Kinetics,
pubmed-meshheading:1321148-Mammary Neoplasms, Experimental,
pubmed-meshheading:1321148-Mammary Tumor Virus, Mouse,
pubmed-meshheading:1321148-Mice,
pubmed-meshheading:1321148-Mice, Inbred C3H,
pubmed-meshheading:1321148-Molecular Structure,
pubmed-meshheading:1321148-Structure-Activity Relationship,
pubmed-meshheading:1321148-Tannins,
pubmed-meshheading:1321148-Transcription, Genetic,
pubmed-meshheading:1321148-Tumor Cells, Cultured
|
| pubmed:year |
1992
|
| pubmed:articleTitle |
Mouse mammary tumor virus gene expression is suppressed by oligomeric ellagitannins, novel inhibitors of poly(ADP-ribose) glycohydrolase.
|
| pubmed:affiliation |
Department of Pharmacology, Faculty of Medical Sciences, Taipei Medical College, Taiwan, Republic of China.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|