Protein arginine (N)-methyl transferase 7 (PRMT7) as a potential target for the sensitization of tumor cells to camptothecins |
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Authors: | Verbiest Vincent Montaudon Danièle Tautu Michel T Moukarzel Joyce Portail Jean-Pierre Markovits Judith Robert Jacques Ichas François Pourquier Philippe |
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Affiliation: | INSERM U916, VINCO, Institut Bergonié and Université Victor Segalen Bordeaux 2, 33076 Bordeaux, France. |
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Abstract: | PRMT7 belongs to the protein arginine methyl-transferases family. We show that downregulation of PRMT7alpha and beta isoforms in DC-3F hamster cells was associated with increased sensitivity to the Top1 inhibitor camptothecin (CPT). This effect was not due to a change in Top1 contents or catalytic activity, or to a difference in the reversal of DNA breaks. Overexpression of PRMT7alpha and beta in DC-3F cells had no effect on CPT sensitivity, whereas it conferred a resistance to DC-3F/9-OH-E cells for which both isoforms are reduced by two- to three-fold as compared to DC-3F parental cells. Finally, downregulation of the human PRMT7 could also sensitize HeLa cells to CPT, suggesting that it could be used as a target to potentiate CPT derivatives. |
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Keywords: | Protein arginine-methyl transferase (PRMT) Topoisomerase I Camptothecin Apoptosis Drug response Resistance |
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