Protein arginine (<i>N</i>)‐methyl transferase 7 (PRMT7) as a potential target for the sensitization of tumor cells to camptothecins

Vincent Verbiest, Danièle Montaudon, Michel Théodore Tautu, Joyce Moukarzel, J.P. Portail, Judith Markovits, Jacques Robert, François Ichas, Philippe Pourquier

FEBS Letters · 2008 · 50 citations · 26 references

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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.

References

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