The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Depletion of the 110-Kilodalton Isoform of Poly(ADP-Ribose) Glycohydrolase Increases Sensitivity to Genotoxic and Endotoxic Stress in Mice
Open accessAbstract
Poly(ADP-ribosylation) is rapidly stimulated in cells following DNA damage. This posttranslational modification is regulated by the synthesizing enzyme poly(ADP-ribose) polymerase 1 (PARP-1) and the degrading enzyme poly(ADP-ribose) glycohydrolase (PARG). Although the role of PARP-1 in response to DNA damage has been studied extensively, the function of PARG and the impact of poly(ADP-ribose) homeostasis in various cellular processes are largely unknown. Here we show that by gene targeting in embryonic stem cells and mice, we specifically deleted the 110-kDa PARG protein (PARG(110)) normally found in the nucleus and that depletion of PARG(110) severely compromised the automodification of PARP-1 in vivo. PARG(110)-deficient mice were viable and fertile, but these mice were hypersensitive to alkylating agents and ionizing radiation. In addition, these mice were susceptible to streptozotocin-induced diabetes and endotoxic shock. These data indicate that PARG(110) plays an important role in DNA damage responses and in pathological processes.
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Citations
Cites
The immunopathogenesis of sepsis
Cohen, J. (2002) · Nature · doi:10.1038/nature01326 · Cited by 2,742
Cited by
Poly(ADP-ribose): novel functions for an old molecule
Schreiber, V., Dantzer, F., Ame, J.-C., & de Murcia, G. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1963 · Cited by 1,915
The multifaceted roles of PARP1 in DNA repair and chromatin remodelling
Ray Chaudhuri, A., & Nussenzweig, A. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.53 · Cited by 1,786
The PARP Side of the Nucleus: Molecular Actions, Physiological Outcomes, and Clinical Targets
Krishnakumar, R., & Kraus, W. L. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.06.017 · Cited by 836
Poly(ADP-ribosyl)ation by PARP-1: `PAR-laying' NAD+ into a nuclear signal
Kim, M. Y., Zhang, T., & Kraus, W. L. (2005) · Genes & Development · doi:10.1101/gad.1331805 · Cited by 802
Hassa, P. (2008) · Frontiers in Bioscience · doi:10.2741/2909 · Cited by 584
Metadata
- Authors
- Cortes, U., Tong, W.-M., Coyle, D. L., Meyer-Ficca, M. L., Meyer, R. G., Petrilli, V., Herceg, Z., Jacobson, E. L., Jacobson, M. K., & Wang, Z.-Q.
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2004-08-01
- Volume
- 24
- Issue
- 16
- Pages
- 7163-7178
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- OpenAlex
- W2144711308
- Cited by
- 175
- References
- 1
- FWCI
- 6.17
- Type
- journal article
- Language
- en
- Open access
- green
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- The paper
- Cortes, U., Tong, W.-M., Coyle, D. L., Meyer-Ficca, M. L., Meyer, R. G., Petrilli, V., Herceg, Z., Jacobson, E. L., Jacobson, M. K., & Wang, Z.-Q. (2004). Depletion of the 110-Kilodalton Isoform of Poly(ADP-Ribose) Glycohydrolase Increases Sensitivity to Genotoxic and Endotoxic Stress in Mice. Molecular and Cellular Biology. https://doi.org/10.1128/mcb.24.16.7163-7178.2004
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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