posted on 2016-09-30, 00:00authored byDominic
I. James, Kate M. Smith, Allan M. Jordan, Emma E. Fairweather, Louise
A. Griffiths, Nicola S. Hamilton, James R. Hitchin, Colin P. Hutton, Stuart Jones, Paul Kelly, Alison E. McGonagle, Helen Small, Alexandra I. J. Stowell, Julie Tucker, Ian D. Waddell, Bohdan Waszkowycz, Donald J. Ogilvie
The
enzyme poly(ADP-ribose) glycohydrolase (PARG) performs a critical
role in the repair of DNA single strand breaks (SSBs). However, a
detailed understanding of its mechanism of action has been hampered
by a lack of credible, cell-active chemical probes. Herein, we demonstrate
inhibition of PARG with a small molecule, leading to poly(ADP-ribose)
(PAR) chain persistence in intact cells. Moreover, we describe two
advanced, and chemically distinct, cell-active tool compounds with
convincing on-target pharmacology and selectivity. Using one of these
tool compounds, we demonstrate pharmacology consistent with PARG inhibition.
Further, while the roles of PARG and poly(ADP-ribose) polymerase (PARP)
are closely intertwined, we demonstrate that the pharmacology of a
PARG inhibitor differs from that observed with the more thoroughly
studied PARP inhibitor olaparib. We believe that these tools will
facilitate a wider understanding of this important component of DNA
repair and may enable the development of novel therapeutic agents
exploiting the critical dependence of tumors on the DNA damage response
(DDR).