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Gene Review

TIPARP  -  TCDD-inducible poly(ADP-ribose) polymerase

Homo sapiens

Synonyms: ADP-ribosyltransferase diphtheria toxin-like 14, ARTD14, DDF1, DKFZP434J214, DKFZp686N0351, ...
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Disease relevance of TIPARP

  • It has been reported that an uncharacterized gene, corresponding to a 5'-truncated partial cDNA DKFZp434J214, is amplified and up-regulated together with CCNL in head-and-neck squamous cell carcinoma (HNSCC) [1].
  • At the scene of ischemic brain injury: is PARP a perp [2]?
  • These findings reveal a novel mechanism linking demyelination and progressive neuronal damage, which might represent an underlying insidious process driving disease beyond a primary white matter phenomenon and rendering the microglial PARP-1 a possible antiinflammatory therapeutic target [3].
  • The 46 kDa DBD of human PARP, and several derivatives thereof mutated in its first or second zinc-finger, were overproduced in Escherichia coli, in CV-1 monkey cells or in human fibroblasts to study their DNA-binding properties, the trans-dominant inhibition of resident PARP activity, and the consequences on DNA repair, respectively [4].
  • In a rat model of hypoglycemic brain injury, neuronal PARP-1 activation and subsequent neuronal death were blocked by the ERK1/2 inhibitor 2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one (PD98059) [5].

High impact information on TIPARP

  • When neurons are stimulated by membrane depolarization, calcium signaling mediated by CaMKII induces dissociation of KIF4 from PARP-1, resulting in upregulation of PARP-1 activity, which supports neuron survival [6].
  • The C-terminal domain of KIF4 is a module that suppresses the activity of poly (ADP-ribose) polymerase-1 (PARP-1), a nuclear enzyme known to maintain cell homeostasis by repairing DNA and serving as a transcriptional regulator [6].
  • After dissociation from PARP-1, KIF4 enters into the cytoplasm from the nucleus and moves to the distal part of neurites in a microtubule-dependent manner [6].
  • PARP-1, an enzyme that catalyzes the attachment of ADP ribose units to target proteins, plays at least two important roles in transcription regulation [7].
  • Second, PARP-1 acts as a component of enhancer/promoter regulatory complexes [7].

Chemical compound and disease context of TIPARP


Biological context of TIPARP


Anatomical context of TIPARP


Associations of TIPARP with chemical compounds

  • CONCLUSIONS: In living cells, ANI is about 1000-fold more potent at inhibiting PARP activity compared with 3-aminobenzamide (3-ABA) [19].
  • It was shown by biochemical fractionation procedure that PARP-1 as well as ATM increases at chromatin level after induction of DSB with neocarzinostatin (NCS) [15].
  • Upon binding to DNA breaks, activated PARP cleaves NAD(+) into nicotinamide and ADP-ribose and polymerizes the latter onto nuclear acceptor proteins including histones, transcription factors, and PARP itself [20].
  • A positive correlation was found between the in vitro DNA-binding capacity of the recombinant DBD polypeptides and their inhibitory effect on PARP activity stimulated by the alkylating agent N-methyl-N'-nitro-N-nitrosoguanidine (MNNG) [4].
  • In this paper we show, by metabolic labelling with [3H]fatty acids, that the PARP anchor contains palmitate esterified to inositol, and stearate at sn-1, in a monoacylglycerol moiety, a structure identical to PP1 [21].

Other interactions of TIPARP

  • Human TIPARP showed 27.5% and 26.0% total-amino-acid identity with human FLJ22693 and ZAP, respectively [1].

Analytical, diagnostic and therapeutic context of TIPARP

  • Because inhibitors of PARP are able to potentiate the cell-killing effects of some DNA-damaging agents and to inhibit the repair of induced DNA strand breaks, such compounds may enhance the anti-tumour efficacy of radiotherapy or cytotoxic drug treatment [19].
  • Inhibitors of PARP-1 activity in combination with DNA-binding antitumor drugs may constitute a suitable strategy in cancer chemotherapy [22].
  • Furthermore, intranasal administration of IL-5 restored the impairment of eosinophil recruitment and mucus production in OVA-challenged PARP-1(-/-) mice [23].
  • Since caspase-8, -3 and -7 were not activated and PARP was not cleaved in these cells as judged by western blotting and immunofluorescence studies, it is likely that this is an atypical form of programmed cell death owing to a proteinase(s) independent of caspases [24].
  • Gel retardation assay indicates that PARP augments DNA binding activity of E2 in vitro [25].


  1. Identification and characterization of human TIPARP gene within the CCNL amplicon at human chromosome 3q25.31. Katoh, M., Katoh, M. Int. J. Oncol. (2003) [Pubmed]
  2. At the scene of ischemic brain injury: is PARP a perp? Choi, D.W. Nat. Med. (1997) [Pubmed]
  3. Activation of microglial poly(ADP-ribose)-polymerase-1 by cholesterol breakdown products during neuroinflammation: a link between demyelination and neuronal damage. Diestel, A., Aktas, O., Hackel, D., Hake, I., Meier, S., Raine, C.S., Nitsch, R., Zipp, F., Ullrich, O. J. Exp. Med. (2003) [Pubmed]
  4. Overproduction of the poly(ADP-ribose) polymerase DNA-binding domain blocks alkylation-induced DNA repair synthesis in mammalian cells. Molinete, M., Vermeulen, W., Bürkle, A., Ménissier-de Murcia, J., Küpper, J.H., Hoeijmakers, J.H., de Murcia, G. EMBO J. (1993) [Pubmed]
  5. Direct phosphorylation and regulation of poly(ADP-ribose) polymerase-1 by extracellular signal-regulated kinases 1/2. Kauppinen, T.M., Chan, W.Y., Suh, S.W., Wiggins, A.K., Huang, E.J., Swanson, R.A. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  6. KIF4 motor regulates activity-dependent neuronal survival by suppressing PARP-1 enzymatic activity. Midorikawa, R., Takei, Y., Hirokawa, N. Cell (2006) [Pubmed]
  7. PARP goes transcription. Kraus, W.L., Lis, J.T. Cell (2003) [Pubmed]
  8. Decreased PARP and procaspase-2 protein levels are associated with cellular drug resistance in childhood acute lymphoblastic leukemia. Holleman, A., den Boer, M.L., Kazemier, K.M., Beverloo, H.B., von Bergh, A.R., Janka-Schaub, G.E., Pieters, R. Blood (2005) [Pubmed]
  9. Lovastatin potentiates antitumor activity of doxorubicin in murine melanoma via an apoptosis-dependent mechanism. Feleszko, W., Młynarczuk, I., Olszewska, D., Jalili, A., Grzela, T., Lasek, W., Hoser, G., Korczak-Kowalska, G., Jakóbisiak, M. Int. J. Cancer (2002) [Pubmed]
  10. The role of poly(ADP-ribose)polymerase in the induction of sister chromatid exchanges and micronuclei by mitomycin C in Down's syndrome cells as compared to euploid cells. Caria, H., Quintas, A., Chaveca, T., Rueff, J. Mutat. Res. (1997) [Pubmed]
  11. Brain distribution and efficacy as chemosensitizer of an oral formulation of PARP-1 inhibitor GPI 15427 in experimental models of CNS tumors. Tentori, L., Leonetti, C., Scarsella, M., Vergati, M., Xu, W., Calvin, D., Morgan, L., Tang, Z., Woznizk, K., Alemu, C., Hoover, R., Lapidus, R., Zhang, J., Graziani, G. Int. J. Oncol. (2005) [Pubmed]
  12. Inhibitors of poly (ADP-ribose) polymerase ameliorate myocardial reperfusion injury by modulation of activator protein-1 and neutrophil infiltration. Kaplan, J., O'Connor, M., Hake, P.W., Zingarelli, B. Shock (2005) [Pubmed]
  13. ATM-dependent telomere loss in aging human diploid fibroblasts and DNA damage lead to the post-translational activation of p53 protein involving poly(ADP-ribose) polymerase. Vaziri, H., West, M.D., Allsopp, R.C., Davison, T.S., Wu, Y.S., Arrowsmith, C.H., Poirier, G.G., Benchimol, S. EMBO J. (1997) [Pubmed]
  14. Modulation of apoptosis by mitochondrial uncouplers: apoptosis-delaying features despite intrinsic cytotoxicity. Stoetzer, O.J., Pogrebniak, A., Pelka-Fleischer, R., Hasmann, M., Hiddemann, W., Nuessler, V. Biochem. Pharmacol. (2002) [Pubmed]
  15. Poly(ADP-ribose) polymerase-1 inhibits ATM kinase activity in DNA damage response. Watanabe, F., Fukazawa, H., Masutani, M., Suzuki, H., Teraoka, H., Mizutani, S., Uehara, Y. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  16. Reversal of EBV immortalization precedes apoptosis in IL-6-induced human B cell terminal differentiation. Altmeyer, A., Simmons, R.C., Krajewski, S., Reed, J.C., Bornkamm, G.W., Chen-Kiang, S. Immunity (1997) [Pubmed]
  17. Players in the PARP-1 cell-death pathway: JNK1 joins the cast. Alano, C.C., Swanson, R.A. Trends Biochem. Sci. (2006) [Pubmed]
  18. Selective serotonin reuptake inhibitors directly signal for apoptosis in biopsy-like Burkitt lymphoma cells. Serafeim, A., Holder, M.J., Grafton, G., Chamba, A., Drayson, M.T., Luong, Q.T., Bunce, C.M., Gregory, C.D., Barnes, N.M., Gordon, J. Blood (2003) [Pubmed]
  19. 4-Amino-1,8-naphthalimide: a novel inhibitor of poly(ADP-ribose) polymerase and radiation sensitizer. Schlicker, A., Peschke, P., Bürkle, A., Hahn, E.W., Kim, J.H. Int. J. Radiat. Biol. (1999) [Pubmed]
  20. The therapeutic potential of poly(ADP-ribose) polymerase inhibitors. Virág, L., Szabó, C. Pharmacol. Rev. (2002) [Pubmed]
  21. A glycosylphosphatidylinositol protein anchor from procyclic stage Trypanosoma brucei: lipid structure and biosynthesis. Field, M.C., Menon, A.K., Cross, G.A. EMBO J. (1991) [Pubmed]
  22. Poly(ADP-ribose) polymerases: homology, structural domains and functions. Novel therapeutical applications. Nguewa, P.A., Fuertes, M.A., Valladares, B., Alonso, C., Pérez, J.M. Prog. Biophys. Mol. Biol. (2005) [Pubmed]
  23. Poly(ADP-ribose) Polymerase-1 Inhibition Prevents Eosinophil Recruitment by Modulating Th2 Cytokines in a Murine Model of Allergic Airway Inflammation: A Potential Specific Effect on IL-5. Mustapha, O., Datta, R., Oumouna-Benachour, K., Suzuki, Y., Hans, C., Matthews, K., Fallon, K., Boulares, H. J. Immunol. (2006) [Pubmed]
  24. NuMA and nuclear lamins behave differently in Fas-mediated apoptosis. Taimen, P., Kallajoki, M. J. Cell. Sci. (2003) [Pubmed]
  25. Functional interaction between human papillomavirus type 18 E2 and poly(ADP-ribose) polymerase 1. Lee, D., Kim, J.W., Kim, K., Joe, C.O., Schreiber, V., Ménissier-De Murcia, J., Choe, J. Oncogene (2002) [Pubmed]
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