Protein arginine (N)-methyl transferase 7 (PRMT7) as a potential target for the sensitization of tumor cells to camptothecins

Vincent Verbiest, Danièle Montaudon, Michel T. Tautu, Joyce Moukarzel, Jean-Pierre Portail, Judith Markovits, Jacques Robert, François Ichas, Philippe Pourquier
FEBS Letters. 2008-03-31; 582(10): 1483-1489
DOI: 10.1016/j.febslet.2008.03.031

PubMed
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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.

 

Auteurs Bordeaux Neurocampus