Activity-based assay for human mono-ADP-ribosyltransferases ARTD7/PARP15 and ARTD10/PARP10 aimed at screening and profiling inhibitors

European Journal of Pharmaceutical Sciences

Volumn 49, Issue 2, 2013, Pages 148-156

  Venkannagari, Harikanth ^a   Fallarero, Adyary ^b   Feijs, Karla L H ^c   Lüscher, Bernhard ^c   Lehtiö, Lari ^a  

^a UNIVERSITY OF OULU   (Finland)

^b ÅBO AKADEMI UNIVERSITY   (Finland)

^c RWTH AACHEN UNIVERSITY   (Germany)

Author keywords

Activity assay; ADP ribosyltransferase; Enzyme; High throughput screening; Inhibitor; Poly(ADP ribose)polymerase

Indexed keywords

NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 10; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 7; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE INHIBITOR; UNCLASSIFIED DRUG;

ARTICLE; COST EFFECTIVENESS ANALYSIS; DRUG SCREENING; ENZYME ACTIVITY; IC 50; PRIORITY JOURNAL;

ADP RIBOSE TRANSFERASES; BIOLOGICAL ASSAY; ENZYME INHIBITORS; ESCHERICHIA COLI; HUMANS; POLY(ADP-RIBOSE) POLYMERASES; PROTO-ONCOGENE PROTEINS;

EID: 84877255023     PISSN: 09280987     EISSN: 18790720     Source Type: Journal    
DOI: 10.1016/j.ejps.2013.02.012     Document Type: Article

References (30)

1. R.C.T. Aguiar, K. Takeyama, C. He, K. Kreinbrink, and M.A. Shipp B-aggressive lymphoma family proteins have unique domains that modulate transcription and exhibit poly(ADP-ribose) polymerase activity J. Biol. Chem. 280 2005 33756 33765
2. S. Bollini, J.J. Herbst, G.T. Gaughan, T.A. Verdoorn, J. Ditta, G.M. Dubowchik, and A. Vinitsky High-throughput fluorescence polarization method for identification of FKBP12 ligands J. Biomol. Screen. 7 2002 526 530
3. A. Chiarugi, E. Meli, M. Calvani, R. Picca, R. Baronti, E. Camaioni, G. Costantino, M. Marinozzi, D.E. Pellegrini-Giampietro, and R. Pellicciari Novel isoquinolinone-derived inhibitors of poly(ADP-ribose) polymerase-1: pharmacological characterization and neuroprotective effects in an in vitro model of cerebral ischemia J. Pharmacol. Exp. Ther. 305 2003 943 949
4. H.-Y.E. Chou, H.T. Chou, and S.-C. Lee CDK-dependent activation of poly(ADP-ribose) polymerase member 10 (PARP10) J. Biol. Chem. 281 2006 15201 15207
5. T. Eltze, R. Boer, T. Wagner, S. Weinbrenner, M.C. McDonald, C. Thiemermann, A. Bürkle, and T. Klein Imidazoquinolinone, imidazopyridine, and isoquinolindione derivatives as novel and potent inhibitors of the poly(ADP-ribose) polymerase (PARP): a comparison with standard PARP inhibitors Mol. Pharmacol. 74 2008 1587 1598
6. K.L.H. Feijs, N. Herzog, A. Braczynski, A.H. Forst, N. Herzog, P. Verheugd, U. Linzen, E. Kremmer, and B. Lüscher ARTD10 substrate identification on protein microarrays: regulation of GSK3β by mono-ADP-ribosylation Cell Commun. Signal 11 2013 5 10.1186/1478-811X-11-5
7. Y. Feng, J. Wu, L. Chen, C. Luo, X. Shen, K. Chen, H. Jiang, and D. Liu A fluorometric assay of SIRT1 deacetylation activity through quantification of nicotinamide adenine dinucleotide Anal. Biochem. 395 2009 205 210
8. A. Forst, T. Karlberg, N. Herzog, A.-G. Thorsell, A. Gross, K.L.H. Feijs, P. Verheugd, P. Kursula, B. Nijmeijer, and E. Kremmer Recognition of mono-ADP-ribosylated ARTD10 substrates by ARTD8 macrodomains Structure 21 2013 462 475
9. W. Han, X. Li, and X. Fu The macrodomain protein family: structure, functions, and their potential therapeutic implications Mutat. Res. 727 2011 86 103
10. P.O. Hassa, and M.O. Hottiger The diverse biological roles of mammalian PARPS, a small but powerful family of poly-ADP-ribose polymerases Front. Biosci. 13 2008 3046 3082
11. P.O. Hassa, S.S. Haenni, M. Elser, and M.O. Hottiger Nuclear ADP-ribosylation reactions in mammalian cells: where are we today and where are we going? Microbiol. Mol. Biol. Rev. 70 2006 789 829
12. N. Herzog, J.D.H. Hartkamp, P. Verheugd, F. Treude, A.H. Forst, K.L.H. Feijs, B. Lippok, E. Kremmer, H. Kleine, and B. Lüscher Caspase-dependent cleavage of the mono-ADP-ribosyltransferase ARTD10 interferes with its pro-apoptotic function FEBS J. 280 2013 1330 1343
13. M.O. Hottiger, P.O. Hassa, B. Lüscher, H. Schüler, and F. Koch-Nolte Toward a unified nomenclature for mammalian ADP-ribosyltransferases Trends Biochem. Sci. 35 2010 208 219
14. P. Jagtap, and C. Szabó Poly(ADP-ribose) polymerase and the therapeutic effects of its inhibitors Nat. Rev. Drug Discov. 4 2005 421 440
15. P.G. Jagtap, G.J. Southan, E. Baloglu, S. Ram, J.G. Mabley, A. Marton, A. Salzman, and C. Szabó The discovery and synthesis of novel adenosine substituted 2,3-dihydro-1H-isoindol-1-ones: potent inhibitors of poly(ADP-ribose) polymerase-1 (PARP-1) Bioorg. Med. Chem. Lett. 14 2004 81 85
16. H. Kleine, and B. Lüscher Learning how to read ADP-ribosylation Cell 139 2009 17 19
17. H. Kleine, E. Poreba, K. Lesniewicz, P.O. Hassa, M.O. Hottiger, D.W. Litchfield, B.H. Shilton, and B. Lüscher Substrate-assisted catalysis by PARP10 limits its activity to mono-ADP-ribosylation Mol. Cell 32 2008 57 69
18. H. Kleine, A. Herrmann, T. Lamark, A.H. Forst, P. Verheugd, J. Lüscher-Firzlaff, B. Lippok, K.L. Feijs, N. Herzog, and E. Kremmer Dynamic subcellular localization of the mono-ADP-ribosyltransferase ARTD10 and interaction with the ubiquitin receptor p62 Cell Commun. Signal. 10 2012 28
19. S. Kummar, A. Chen, R.E. Parchment, R.J. Kinders, J. Ji, J.E. Tomaszewski, and J.H. Doroshow Advances in using PARP inhibitors to treat cancer BMC Med. 10 2012 25
20. C.J. Lord, and A. Ashworth Targeted therapy for cancer using PARP inhibitors Curr. Opin. Pharmacol. 8 2008 363 369
21. B. Maurer, U. Mathias, P. Papatheodorou, S. Shekfeh, J. Orth, T. Jank, C. Schwan, W. Sippl, K. Aktories, and M. Jung From cosubstrate similarity to inhibitor diversity-inhibitors of ADP-ribosyltransferases from kinase inhibitor screening Mol. Biosyst. 7 2011 799 808
22. K.A. Menear, C. Adcock, R. Boulter, X. Cockcroft, L. Copsey, A. Cranston, K.J. Dillon, J. Drzewiecki, S. Garman, and S. Gomez 4-[3-(4- cyclopropanecarbonylpiperazine-1-carbonyl)-4-fluorobenzyl]-2H-phthalazin-1-one: a novel bioavailable inhibitor of poly(ADP-ribose) polymerase-1 J. Med. Chem. 51 2008 6581 6591
23. M. Narwal, A. Fallarero, P. Vuorela, and L. Lehtiö Homogeneous screening assay for human tankyrase J. Biomol. Screen. 17 2012 593 604
24. M. Narwal, H. Venkannagari, and L. Lehtiö Structural basis of selective inhibition of human tankyrases J. Med. Chem. 55 2012 1360 1367
25. K.S. Putt, and P.J. Hergenrother An enzymatic assay for poly(ADP-ribose) polymerase-1 (PARP-1) via the chemical quantitation of NAD(+): application to the high-throughput screening of small molecules as potential inhibitors Anal. Biochem. 326 2004 78 86
26. V. Schreiber, F. Dantzer, J.-C. Ame, and G. de Murcia Poly(ADP-ribose): novel functions for an old molecule Nat. Rev. Mol. Cell Biol. 7 2006 517 528
27. E. Wahlberg, T. Karlberg, E. Kouznetsova, N. Markova, A. Macchiarulo, A.-G. Thorsell, E. Pol, Å. Frostell, T. Ekblad, and D. Öncü Family-wide chemical profiling and structural analysis of PARP and tankyrase inhibitors Nat. Biotechnol. 30 2012 283 288
28. I. Welsby, D. Hutin, and O. Leo Complex roles of members of the ADP-ribosyl transferase super family in immune defences: looking beyond PARP1 Biochem. Pharmacol. 84 2012 11 20
29. M. Yu, S. Schreek, C. Cerni, C. Schamberger, K. Lesniewicz, E. Poreba, J. Vervoorts, G. Walsemann, J. Grtzinger, and E. Kremmer PARP-10, a novel Myc-interacting protein with poly(ADP-ribose) polymerase activity, inhibits transformation Oncogene 24 2005 1982 1993
30. Zhang, Chung, and Oldenburg A simple statistical parameter for use in evaluation and validation of high throughput screening assays J. Biomol. Screen. 4 1999 67 73