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Parp1  -  poly (ADP-ribose) polymerase 1

Rattus norvegicus

Synonyms: ADP-ribosyltransferase diphtheria toxin-like 1, ADPRT 1, ARTD1, Adprt, NAD(+) ADP-ribosyltransferase 1, ...
 
 
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Disease relevance of Parp1

  • These results indicated that PARP-1 plays a principal role in inducing mitochondrial impairment that ultimately leads to apoptosis of neurons after cerebral ischemia [1].
  • These findings suggest that although blockade of PARP activity fully attenuates NMDA-induced PAR formation and loss of retinal ATP content, and improves the survival of select populations of ganglion cells, this approach does not provide full neuroprotection [2].
  • These results suggest that pyruvate may significantly improve the outcome after severe hypoglycemia by circumventing a sustained impairment in neuronal glucose utilization resulting from PARP-1 activation [3].
  • BACKGROUND: Poly (ADP-ribose) polymerase (PARP), a nuclear enzyme activated by strand breaks in DNA, plays an important role in the development of ischemia/reperfusion (I/R) injury [4].
  • To further study the mechanism of peroxynitrite toxicity to neurons we investigated the role of caspases and poly (ADP-ribose) polymerase (PARP) in this model system [5].
 

Psychiatry related information on Parp1

  • CONCLUSIONS: These data demonstrate that BCNCI in a rat model causes increased PARP activation, resulting in severe erectile dysfunction [6].
  • In this study the effect of Abeta 25-35 (25 microM) and non-Abeta component of Alzheimer's disease amyloid (NAC, 10 microM) on mChR-dependent signaling to PARP-1 was determined [7].
 

High impact information on Parp1

  • We found that the CA1 tissue from hippocampus possesses an ADPRT activity that is dramatically stimulated by NO and attenuated by two different inhibitors of mono-ADPRT activity, phylloquinone and nicotinamide [8].
  • Postsynaptic injection of nicotinamide failed to attenuate LTP, suggesting that the critical site of ADPRT activity resides at a nonpostsynaptic locus [8].
  • Hepatocyte apoptosis, caspase activation, and poly (ADP-ribose) polymerase (PARP) cleavage, which are normally observed in response to both bile acids, were largely prevented after preincubation of hepatocytes with betaine [9].
  • Caspase inhibition accelerates the loss of mitochondrial potential and shifts the mode of cell death to necrosis; inhibition of PARP with 3AB attenuates this effect of caspase inhibition [10].
  • DNA strand breaks and associated activation of poly-ADP-ribose polymerase (PARP) and NAD depletion occur rapidly after exposure to homocysteine and precede mitochondrial dysfunction, oxidative stress, and caspase activation [10].
 

Chemical compound and disease context of Parp1

 

Biological context of Parp1

  • Recent reports have linked neuronal cell death by necrosis to poly(ADP-ribose) polymerase-1 (PARP-1) hyperactivation [2].
  • The tripeptide protease inhibitor z-Val-Ala-Asp (zVAD) prevented PARP and lamin cleavage, DNA fragmentation, morphological changes, and cell detachment in irradiated EC [14].
  • Poly(ADP-ribose) polymerase 1 (PARP-1) is the predominant NAD-dependent modifying enzyme in DNA repair, transcription, and apoptosis; its involvement in development has not been defined [15].
  • In later gestation and postnatally, PARP-1 staining was primarily cytoplasmic and progressively restricted to a subset of cells, mainly bronchial epithelial and smooth muscle cells [15].
  • In conclusion, levels of oxidative DNA damage and the DNA repair enzyme PARP-1 are increased in vessels after balloon injury [16].
 

Anatomical context of Parp1

 

Associations of Parp1 with chemical compounds

  • Blockade of PARP activity attenuates poly(ADP-ribosyl)ation but offers only partial neuroprotection against NMDA-induced cell death in the rat retina [2].
  • Inhibition of PARP-1 activity by 5-iodo-6-amino-1,2-benzopyrone in fetal rat lung explant culture did not affect SP-A and -B mRNA, but significantly increased SP-C mRNA [15].
  • In the present article, by the use of DNA and protein cross-linking reactions, by cis-diamminedichloroplatinum II (cDDP) and sodium tetrathionate (NaTT) respectively, we present more evidences about the association of PARP-1, PARP-2, and PARPs related proteins with the NM [17].
  • Western blot analysis of proteins was performed by probing immunoblots with antibodies against p53, bax and PARP (poly ADP-ribose polymerase) [18].
  • We describe the involvement of poly(ADP-ribose)polymerase 1 and 2 (PARP-1 and -2) and poly(ADP-ribose)glycohydrolase (PARG) in the response of rat germinal cells to the action of the NO donors, 3-morpholino-sydnonimine (SIN-1) and spermine nonoate (SNO) [19].
 

Regulatory relationships of Parp1

  • Caspase inhibition switches the mode of cell death induced by cyanide by enhancing reactive oxygen species generation and PARP-1 activation [20].
 

Other interactions of Parp1

  • Caspase-9 and -3 were activated, causing cleavage of PARP, a hallmark of apoptosis and internucleosomal DNA fragmentation [21].
  • Western blot analysis showed no change either on poly-ADP ribose polymerase (PARP) or p53 transcription factor in CCI and sham rats [22].
  • Activation of intracellular caspases, manifest by proteolytic poly (ADP-ribose) polymerase (PARP) and lamin B cleavage, was maximal at 15 h after IR, concident with other indices of EC apoptosis, including oligonucleosomal DNA degradation, TUNEL immunostaining, and morphologic changes [14].
  • Furthermore, inhibition of poly(ADP-ribosylation) prevented intranuclear localization of apoptosis-inducing factor and protected neurons from excitotoxic injury; and PARP-1 null fibroblasts were protected from oxidative stress-induced cell death [23].
  • Furthermore, a large decrease of apoptotic bodies was associated with a significant drop of caspase and PARP-1 cleavages, suggesting that the protective effect of DP closely correlates with limitation of apoptosis expansion [24].
 

Analytical, diagnostic and therapeutic context of Parp1

  • HI induced a marked increase in activated caspase-9, caspase-3 and PARP cleavage at 12 h to 7 days after HI in brain areas displaying TUNEL (+) cells [25].
  • Immunohistochemistry for PARP-1 in Embryonic Day 18 rat lung showed predominantly nuclear staining in most cells [15].
  • Furthermore, PARP inhibitors significantly decrease the ischemia-reperfusion-induced increase of lipid peroxidation, protein oxidation, single-strand DNA breaks, and the inactivation of respiratory complexes, which indicate a decreased mitochondrial ROS production in the reperfusion period [26].
  • Purified germinal cell populations and rats of different age were used for activity-, immuno-, and Northern blot experiments, to determine at which level poly(ADPR)polymerase (PARP) is regulated at various stages of spermatogenesis [27].
  • The DNA synthesis was due to de novo synthesis and not to DNA repair as a consequence of the initiation of apoptosis, determined by flow cytometry, and lack of proteolytic activation of PARP by caspase 3 [28].

References

  1. Mitochondrial impairment induced by poly(ADP-ribose) polymerase-1 activation in cortical neurons after oxygen and glucose deprivation. Tanaka, S., Takehashi, M., Iida, S., Kitajima, T., Kamanaka, Y., Stedeford, T., Banasik, M., Ueda, K. J. Neurochem. (2005) [Pubmed]
  2. Blockade of PARP activity attenuates poly(ADP-ribosyl)ation but offers only partial neuroprotection against NMDA-induced cell death in the rat retina. Goebel, D.J., Winkler, B.S. J. Neurochem. (2006) [Pubmed]
  3. Pyruvate administered after severe hypoglycemia reduces neuronal death and cognitive impairment. Suh, S.W., Aoyama, K., Matsumori, Y., Liu, J., Swanson, R.A. Diabetes (2005) [Pubmed]
  4. 5-Aminoisoquinolinone reduces renal injury and dysfunction caused by experimental ischemia/reperfusion. Chatterjee, P.K., Chatterjee, B.E., Pedersen, H., Sivarajah, A., McDonald, M.C., Mota-Filipe, H., Brown, P.A., Stewart, K.N., Cuzzocrea, S., Threadgill, M.D., Thiemermann, C. Kidney Int. (2004) [Pubmed]
  5. Caspase-1 and poly (ADP-ribose) polymerase inhibitors may protect against peroxynitrite-induced neurotoxicity independent of their enzyme inhibitor activity. Zhang, Y., Rosenberg, P.A. Eur. J. Neurosci. (2004) [Pubmed]
  6. Poly(Adenosine diphosphate-ribose) polymerase inhibition preserves erectile function in rats after cavernous nerve injury. Kendirci, M., Zsengellér, Z., Bivalacqua, T.J., Gur, S., Usta, M.F., Chen, M., Szabó, C., Hellstrom, W.J. J. Urol. (2005) [Pubmed]
  7. Alzheimer's disease related peptides affected cholinergic receptor mediated poly(ADP-ribose) polymerase activity in the hippocampus. Adamczyk, A., Jeśko, H., Strosznajder, R.P. Folia neuropathologica / Association of Polish Neuropathologists and Medical Research Centre, Polish Academy of Sciences. (2005) [Pubmed]
  8. An ADP-ribosyltransferase as a potential target for nitric oxide action in hippocampal long-term potentiation. Schuman, E.M., Meffert, M.K., Schulman, H., Madison, D.V. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  9. Prevention of bile acid-induced apoptosis by betaine in rat liver. Graf, D., Kurz, A.K., Reinehr, R., Fischer, R., Kircheis, G., Häussinger, D. Hepatology (2002) [Pubmed]
  10. Homocysteine elicits a DNA damage response in neurons that promotes apoptosis and hypersensitivity to excitotoxicity. Kruman, I.I., Culmsee, C., Chan, S.L., Kruman, Y., Guo, Z., Penix, L., Mattson, M.P. J. Neurosci. (2000) [Pubmed]
  11. Inhibitors of poly(ADP-ribose) polymerase-1 suppress transcriptional activation in lymphocytes and ameliorate autoimmune encephalomyelitis in rats. Chiarugi, A. Br. J. Pharmacol. (2002) [Pubmed]
  12. Beneficial effects of PJ34 and INO-1001, two novel water-soluble poly(ADP-ribose) polymerase inhibitors, on the consequences of traumatic brain injury in rat. Besson, V.C., Zsengellér, Z., Plotkine, M., Szabó, C., Marchand-Verrecchia, C. Brain Res. (2005) [Pubmed]
  13. Cytoprotective effects of Glycyrrhizae radix extract and its active component liquiritigenin against cadmium-induced toxicity (effects on bad translocation and cytochrome c-mediated PARP cleavage). Kim, S.C., Byun, S.H., Yang, C.H., Kim, C.Y., Kim, J.W., Kim, S.G. Toxicology (2004) [Pubmed]
  14. Early molecular changes in irradiated aortic endothelium. Gajdusek, C., Onoda, K., London, S., Johnson, M., Morrison, R., Mayberg, M. J. Cell. Physiol. (2001) [Pubmed]
  15. Ontogeny of poly(ADP-ribose) polymerase-1 in lung and developmental implications. Ertsey, R., Chapin, C.J., Kitterman, J.A., Scavo, L.M. Am. J. Respir. Cell Mol. Biol. (2004) [Pubmed]
  16. Attenuation of neointima formation through the inhibition of DNA repair enzyme PARP-1 in balloon-injured rat carotid artery. Zhang, C., Yang, J., Jennings, L.K. Am. J. Physiol. Heart Circ. Physiol. (2004) [Pubmed]
  17. Co-localization of poly(ADPR)polymerase 1 (PARP-1) poly(ADPR)polymerase 2 (PARP-2) and related proteins in rat testis nuclear matrix defined by chemical cross-linking. Tramontano, F., Di Meglio, S., Quesada, P. J. Cell. Biochem. (2005) [Pubmed]
  18. Aging splenocyte and thymocyte apoptosis is associated with enhanced expression of p53, bax, and caspase-3. Kapasi, A.A., Singhal, P.C. Mol. Cell Biol. Res. Commun. (1999) [Pubmed]
  19. Dual role for poly(ADP-ribose)polymerase-1 and -2 and poly(ADP-ribose)glycohydrolase as DNA-repair and pro-apoptotic factors in rat germinal cells exposed to nitric oxide donors. Di Meglio, S., Tramontano, F., Cimmino, G., Jones, R., Quesada, P. Biochim. Biophys. Acta (2004) [Pubmed]
  20. Caspase inhibition switches the mode of cell death induced by cyanide by enhancing reactive oxygen species generation and PARP-1 activation. Prabhakaran, K., Li, L., Borowitz, J.L., Isom, G.E. Toxicol. Appl. Pharmacol. (2004) [Pubmed]
  21. Mitochondrial mechanism of microvascular endothelial cells apoptosis in hyperhomocysteinemia. Tyagi, N., Ovechkin, A.V., Lominadze, D., Moshal, K.S., Tyagi, S.C. J. Cell. Biochem. (2006) [Pubmed]
  22. Apoptotic genes expression in the lumbar dorsal horn in a model neuropathic pain in rat. Maione, S., Siniscalco, D., Galderisi, U., de Novellis, V., Uliano, R., Di Bernardo, G., Berrino, L., Cascino, A., Rossi, F. Neuroreport (2002) [Pubmed]
  23. Intra-mitochondrial poly(ADP-ribosylation) contributes to NAD+ depletion and cell death induced by oxidative stress. Du, L., Zhang, X., Han, Y.Y., Burke, N.A., Kochanek, P.M., Watkins, S.C., Graham, S.H., Carcillo, J.A., Szabó, C., Clark, R.S. J. Biol. Chem. (2003) [Pubmed]
  24. Apoptotic cell death progression after photothrombotic focal cerebral ischaemia: effects of the lipophilic iron chelator 2,2'-dipyridyl. Van Hoecke, M., Prigent-Tessier, A., Bertrand, N., Prevotat, L., Marie, C., Beley, A. Eur. J. Neurosci. (2005) [Pubmed]
  25. Transgenic expression of human FGF-1 protects against hypoxic-ischemic injury in perinatal brain by intervening at caspase-XIAP signaling cascades. Russell, J.C., Szuflita, N., Khatri, R., Laterra, J., Hossain, M.A. Neurobiol. Dis. (2006) [Pubmed]
  26. Effect of poly(ADP-ribose) polymerase inhibitors on the ischemia-reperfusion-induced oxidative cell damage and mitochondrial metabolism in Langendorff heart perfusion system. Halmosi, R., Berente, Z., Osz, E., Toth, K., Literati-Nagy, P., Sumegi, B. Mol. Pharmacol. (2001) [Pubmed]
  27. Poly(ADPribosyl)ation system in rat germinal cells at different stages of differentiation. Quesada, P., Atorino, L., Cardone, A., Ciarcia, G., Farina, B. Exp. Cell Res. (1996) [Pubmed]
  28. Induction of DNA synthesis by ligation of the CD53 tetraspanin antigen in primary cultures of mesangial cells. Yunta, M., Rodríguez-Barbero, A., Arévalo, M.A., López-Novoa, J.M., Lazo, P.A. Kidney Int. (2003) [Pubmed]
 
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