Expression of poly(ADP-ribose) glycohydrolase in wild-type and PARG-110 knock-out retina

Adv Exp Med Biol. 2014;801:463-9. doi: 10.1007/978-1-4614-3209-8_59.

Abstract

Poly(ADP-ribose) (PAR) turnover is required for many cellular processes, and highly relevant for cell death and survival. This post-translational protein modification is regulated by the synthesizing enzyme poly(ADP)ribose-polymerase (PARP) and the degrading enzyme poly(ADP-ribose) glycohydrolase (PARG). Previously, PARP activity was found to be involved in photoreceptor degeneration in the rd1 mouse and in rd1-like conditions PARP-1 was the main PARP family member contributing to photoreceptor cell death. Despite the manifest role of PARP and PAR accumulation in photoreceptor cell death, the influence of PAR degradation on photoreceptor viability was still unknown. Here, we investigated the role of PARG in photoreceptor degeneration using the PARG-110 knock out mouse and report for the first time on PARG expression in wild-type and knock-out retina.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Disease Models, Animal
  • Enzyme Inhibitors / pharmacology
  • Glycoside Hydrolases / antagonists & inhibitors
  • Glycoside Hydrolases / genetics*
  • Glycoside Hydrolases / metabolism
  • Mice
  • Mice, Knockout
  • Neuroprotective Agents / pharmacology
  • Photoreceptor Cells, Vertebrate / drug effects
  • Photoreceptor Cells, Vertebrate / pathology
  • Photoreceptor Cells, Vertebrate / physiology
  • Poly (ADP-Ribose) Polymerase-1
  • Poly(ADP-ribose) Polymerases / genetics*
  • Poly(ADP-ribose) Polymerases / metabolism
  • Retina / drug effects
  • Retina / pathology
  • Retina / physiology*
  • Retinal Degeneration / genetics
  • Retinal Degeneration / metabolism
  • Retinal Degeneration / physiopathology*

Substances

  • Enzyme Inhibitors
  • Neuroprotective Agents
  • Parp1 protein, mouse
  • Poly (ADP-Ribose) Polymerase-1
  • Poly(ADP-ribose) Polymerases
  • Glycoside Hydrolases
  • poly ADP-ribose glycohydrolase