non-radioactive and quantitative assay system for PARG activity based on dot-blot assay using anti-poly(ADP-ribose) and nitrocellulose membrane. The maximum velocity Vmax and the Michaelis constant Km of PARG reaction according to this method are 4.46 microM and 128.33 micromol/min/mg, respectively
the protozoan enzyme represents a good model for human PARG and is therefore likely to prove useful in guiding structure-based discovery of new classes of PARG inhibitors
DNA damage repair enzymes, including the enzyme poly(ADP-ribose) glycohydrolase (PARG), are promising targets in the development of therapeutic agents for a wide range of cancers and potentially other diseases
enzyme activity modulates the inflammatory response and tissue events associated with spinal cord trauma and participates in target organ damage under these conditions
treatment of wild-type mice with pharmacological inhibitors GPI 16552 or GPI 18214 shows a protective effect in dinitrobenzene sulfonic acid-induced colitis. Mice lacking the functional 110 kDa isoform of enzyme are resistant to colon injury by dinitrobenzene sulfonic acid. Mucosa of mutant mice colon tissue shows reduction of myeloperoxidase activity and attenuated staining for intercellular adhesion molecule 1 and vascular cell adhesion molecule 1. Overproduction of proinflammatory factors tumor necrosis factor alpha and interleukin 1beta and activation of cell death signaling pathway are inhibited in these mice
since combination of poly(ADP-ribose) polymerase-1 and poly(ADP-ribose) glycohydrolase inhibition in chemotherapy does not produce increased HeLa cell death, strategies that target poly(ADP-ribose) metabolism for the improved treatment of cancer may be required to target poly(ADP-ribose) polymerase-1 and poly(ADP-ribose) glycohydrolase individually in order to optimize cancer cell death