Publications
1998
Duranton B., Keith G., Goss, Bergmann C., Schleiffer R., Raul F.
Concomitant changes in polyamine pools and DNA methylation during growth inhibition of human colonic cancer cells Article de journal
Dans: Exp Cell Res, vol. 243, non 2, p. 319-25, 1998, (0014-4827 Journal Article).
Résumé | BibTeX | Étiquettes: *Cell, *DNA, &, Adenosylmethionine, Amidines/pharmacology, Caco-2, Cells, Decarboxylase/antagonists, Differentiation/drug, Division/drug, effects, Eflornithine/pharmacology, enzyme, Gov't, Human, Indans/pharmacology, inhibitors/metabolism, Inhibitors/pharmacology, Methylation, Non-U.S., Ornithine, Polyamines/*metabolism, Support
@article{,
title = {Concomitant changes in polyamine pools and DNA methylation during growth inhibition of human colonic cancer cells},
author = { B. Duranton and G. Keith and Goss and C. Bergmann and R. Schleiffer and F. Raul},
year = {1998},
date = {1998-01-01},
journal = {Exp Cell Res},
volume = {243},
number = {2},
pages = {319-25},
abstract = {The effects of CGP 48664 and DFMO, selective inhibitors of the key enzymes of polyamine biosynthesis, namely, of S-adenosylmethionine decarboxylase (AdoMetDC) and ornithine decarboxylase (ODC), were investigated on growth, polyamine metabolism, and DNA methylation in the Caco-2 cell line. Both inhibitors caused growth inhibition and affected similarly the initial expression of the differentiation marker sucrase. In the presence of the AdoMetDC inhibitor, ODC activity and the intracellular pool of putrescine were enhanced, whereas the spermidine and spermine pools were decreased. In the presence of the ODC inhibitor, the AdoMetDC activity was enhanced and the intracellular pools of putrescine and spermidine were decreased. With both compounds, the degree of global DNA methylation was increased. Spermine and spermidine (but not putrescine) selectively inhibited cytosine-DNA methyltransferase activity. Our observations suggest that spermidine (and to a lesser extent spermine) controls DNA methylation and may represent a crucial step in the regulation of Caco-2 cell growth and differentiation.},
note = {0014-4827
Journal Article},
keywords = {*Cell, *DNA, &, Adenosylmethionine, Amidines/pharmacology, Caco-2, Cells, Decarboxylase/antagonists, Differentiation/drug, Division/drug, effects, Eflornithine/pharmacology, enzyme, Gov't, Human, Indans/pharmacology, inhibitors/metabolism, Inhibitors/pharmacology, Methylation, Non-U.S., Ornithine, Polyamines/*metabolism, Support},
pubstate = {published},
tppubtype = {article}
}
The effects of CGP 48664 and DFMO, selective inhibitors of the key enzymes of polyamine biosynthesis, namely, of S-adenosylmethionine decarboxylase (AdoMetDC) and ornithine decarboxylase (ODC), were investigated on growth, polyamine metabolism, and DNA methylation in the Caco-2 cell line. Both inhibitors caused growth inhibition and affected similarly the initial expression of the differentiation marker sucrase. In the presence of the AdoMetDC inhibitor, ODC activity and the intracellular pool of putrescine were enhanced, whereas the spermidine and spermine pools were decreased. In the presence of the ODC inhibitor, the AdoMetDC activity was enhanced and the intracellular pools of putrescine and spermidine were decreased. With both compounds, the degree of global DNA methylation was increased. Spermine and spermidine (but not putrescine) selectively inhibited cytosine-DNA methyltransferase activity. Our observations suggest that spermidine (and to a lesser extent spermine) controls DNA methylation and may represent a crucial step in the regulation of Caco-2 cell growth and differentiation.