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Physiology and pathophysiology of poly(ADP‐ribosyl)ation *
Abstract
One of the immediate eukaryotic cellular responses to DNA breakage is the covalent post‐translational modification of nuclear proteins with poly(ADP‐ribose) from NAD+ as precursor, mostly catalysed by poly(ADP‐ribose) polymerase‐1 (PARP‐1). Recently several other polypeptides have been shown to catalyse poly(ADP‐ribose) formation. Poly(ADP‐ribosyl)ation is involved in a variety of physiological and pathophysiological phenomena. Physiological functions include its participation in DNA‐base excision repair, DNA‐damage signalling, regulation of genomic stability, and regulation of transcription and proteasomal function, supporting the previously observed correlation of cellular poly(ADP‐ribosyl)ation capacity with mammalian life. The pathophysiology effects are mediated through PARP‐1 overactivity, which can cause cell suicide by NAD+ depletion. It is apparent that the latter effect underlies the pathogenesis of a wide range of disease states including type‐1 diabetes, ischaemic infarcts in various organs, and septic or haemorrhagic shock. Therefore pharmacological modulation of poly(ADP‐ribosyl)ation may prove to be an exciting option for various highly prevalent, disabling and even lethal diseases. BioEssays 23:795–806, 2001. © 2001 John Wiley & Sons, Inc.
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Cites
Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions
d'AMOURS, D., DESNOYERS, S., d'SILVA, I., & POIRIER, G. G. (1999) · Biochemical Journal · doi:10.1042/bj3420249 · Cited by 1,815
Chambon, P., Weill, J. D., & Mandel, P. (1963) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(63)90024-x · Cited by 654
Diabetic endothelial dysfunction: the role of poly(ADP-ribose) polymerase activation
Garcia Soriano, F., Virág, L., Jagtap, P., Szabó, É., Mabley, J. G., Liaudet, L., Marton, A., Hoyt, D. G., Murthy, K. G. K., Salzman, A. L., et al. (2001) · Nature Medicine · doi:10.1038/83241 · Cited by 603
Mitotic Misregulation and Human Aging
Ly, D. H., Lockhart, D. J., Lerner, R. A., & Schultz, P. G. (2000) · Science · doi:10.1126/science.287.5462.2486 · Cited by 599
Poly(ADP-ribose) Binds to Specific Domains in DNA Damage Checkpoint Proteins
Pleschke, J. M., Kleczkowska, H. E., Strohm, M., & Althaus, F. R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006520200 · Cited by 541
Poly(ADP-ribose) polymerase-1: what have we learned from the deficient mouse model?
Shall, S., & de Murcia, G. (2000) · Mutation Research/DNA Repair · doi:10.1016/s0921-8777(00)00016-1 · Cited by 534
Tankyrase promotes telomere elongation in human cells
Smith, S., & de Lange, T. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00752-1 · Cited by 418
Smith, S. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01780-1 · Cited by 314
Poly(ADP-ribose) Polymerase Null Mouse Cells Synthesize ADP-ribose Polymers
Shieh, W. M., Amé, J.-C., Wilson, M. V., Wang, Z.-Q., Koh, D. W., Jacobson, M. K., & Jacobson, E. L. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.46.30069 · Cited by 303
Grube, K., & Bürkle, A. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.24.11759 · Cited by 301
Self-citationWhite, A. W., Almassy, R., Calvert, A. H., Curtin, N. J., Griffin, R. J., Hostomsky, Z., Maegley, K., Newell, D. R., Srinivasan, S., & Golding, B. T. (2000) · Journal of Medicinal Chemistry · doi:10.1021/jm000950v · Cited by 288
Chi, N.-W., & Lodish, H. F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m007635200 · Cited by 277
Functions of poly(ADP-ribose) polymerase in controlling telomere length and chromosomal stability
Fagagna, F. D. D., Hande, M. P., Tong, W.-M., Lansdorp, P. M., Wang, Z.-Q., & Jackson, S. P. (1999) · Nature Genetics · doi:10.1038/12680 · Cited by 255
Structure of the catalytic fragment of poly(AD-ribose) polymerase from chicken.
Ruf, A., Mennissier de Murcia, J., de Murcia, G., & Schulz, G. E. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.15.7481 · Cited by 241
Poly-ADP ribose polymerase activates nuclear proteasome to degrade oxidatively damaged histones
Ullrich, O., Reinheckel, T., Sitte, N., Hass, R., Grune, T., & Davies, K. J. A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.11.6223 · Cited by 229
Mendoza-Alvarez, H., & Alvarez-Gonzalez, R. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41568-2 · Cited by 227
NMDA But Not Non-NMDA Excitotoxicity is Mediated by Poly(ADP-Ribose) Polymerase
Mandir, A. S., Poitras, M. F., Berliner, A. R., Herring, W. J., Guastella, D. B., Feldman, A., Poirier, G. G., Wang, Z.-Q., Dawson, T. M., & Dawson, V. L. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-21-08005.2000 · Cited by 213
Delaney, C. A., Wang, L. Z., Kyle, S., White, A. W., Calvert, A. H., Curtin, N. J., Durkacz, B. W., Hostomský, Z., & Newell, D. R. (2000) · PubMed · doi:10.25405/ncl.34597155 · Cited by 205
Poly(ADP-ribose) Polymerase-1 in the Nervous System
Ha, H. C., & Snyder, S. H. (2000) · Neurobiology of Disease · doi:10.1006/nbdi.2000.0324 · Cited by 193
Mammalian Meiotic Telomeres: Protein Composition and Redistribution in Relation to Nuclear Pores
Scherthan, H., Jerratsch, M., Li, B., Smith, S. H., Hultén, M. A., Lock, T., & de Lange, T. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.12.4189 · Cited by 157
Myocardial Postischemic Injury Is Reduced by PolyADPribose Polymerase-1 Gene Disruption
Pieper, A. A., Walles, T., Wei, G., Clements, E. E., Verma, A. M., Snyder, S. H., & Zweier, J. L. (2000) · Molecular Medicine · doi:10.1007/bf03401936 · Cited by 156
ATP for the DNA Ligation Step in Base Excision Repair Is Generated from Poly(ADP-ribose)
Oei, S. L., & Ziegler, M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002429200 · Cited by 147
Bowman, K. J., Newell, D. R., Calvert, H., & Curtin, N. J. (2001) · British Journal of Cancer · doi:10.1054/bjoc.2000.1555 · Cited by 144
Inhibition of poly(ADP-ribose) polymerase attenuates inflammation in a model of chronic colitis
Jijon, H. B., Churchill, T. A., Malfair, D., Wessler, A., Jewell, L. D., Parsons, H. G., & Madsen, K. L. (2000) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.2000.279.3.g641 · Cited by 135
Yakovlev, A. G., Wang, G., Stoica, B. A., Boulares, H. A., Spoonde, A. Y., Yoshihara, K., & Smulson, M. E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001087200 · Cited by 131
The response of Parp knockout mice against DNA damaging agents
Masutani, M., Nozaki, T., Nakamoto, K., Nakagama, H., Suzuki, H. I., Kusuoka, O., Tsutsumi, M., & Sugimura, T. (2000) · Mutation Research/Reviews in Mutation Research · doi:10.1016/s1383-5742(00)00033-8 · Cited by 130
Misregulation of gene expression in primary fibroblasts lacking poly(ADP-ribose) polymerase
Simbulan-Rosenthal, C. M., Ly, D. H., Rosenthal, D. S., Konopka, G., Luo, R., Wang, Z., Schultz, P. G., & Smulson, M. E. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.200285797 · Cited by 130
Poly(ADP-ribose) Polymerase Is a B-MYB Coactivator
Cervellera, M. N., & Sala, A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.14.10692 · Cited by 127
Smulson, M. E., Simbulan-Rosenthal, C. M., Boulares, A. H., Yakovlev, A., Stoica, B. A., Iyer, S., Luo, R., Haddad, B. R., Wang, Z., Pang, T.-L., et al. (2000) · Advances in Enzyme Regulation · doi:10.1016/s0065-2571(99)00024-2 · Cited by 124
Caspase-3-mediated Processing of Poly(ADP-ribose) Glycohydrolase during Apoptosis
Affar, E. B., Germain, M., Winstall, É., Vodenicharov, M. D., Shah, R. G., Salvesen, G. S., & Poirier, G. G. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007269200 · Cited by 120
Evidence for regulation of NF-κB by poly(ADP-ribose) polymerase
Kameoka, M., Ota, K., Tetsuka, T., Tanaka, Y., Itaya, A., Okamoto, T., & Yoshihara, K. (2000) · Biochemical Journal · doi:10.1042/bj3460641 · Cited by 116
Inhibition of poly(ADP-ribose) polymerase attenuates ischemic renal injury in rats
Martin, D. R., Lewington, A. J. P., Hammerman, M. R., & Padanilam, B. J. (2000) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.2000.279.5.r1834 · Cited by 111
Nagayama, T., Simon, R. P., Chen, D., et al. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0741636.x · Cited by 104
Discovering new ADP-ribose polymer cycles: protecting the genome and more
Jacobson, M. K., & Jacobson, E. L. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01481-4 · Cited by 100
Bürkle, A. (2001) · Cancer Letters · doi:10.1016/s0304-3835(00)00694-7 · Cited by 94
Self-citationPoly(ADP‐Ribose) Synthase Inhibition Reduces Ischemic Injury and Inflammation in Neonatal Rat Brain
Ducrocq, S., Benjelloun, N., Plotkine, M., Ben‐Ari, Y., & Charriaut‐Marlangue, C. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0742504.x · Cited by 93
Nirodi, C. S., Nagdas, S. K., Gygi, S. P., Olson, G. E., Aebersold, R. H., & Richmond, A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009897200 · Cited by 90
Regulation of the human poly(ADP-ribose) polymerase promoter by the ETS transcription factor
Soldatenkov, V. A., Albor, A., Patel, B. K. R., Dreszer, R., Dritschilo, A., & Notario, V. (1999) · Oncogene · doi:10.1038/sj.onc.1202778 · Cited by 90
McDonald, M. C., Mota‐Filipe, H., Wright, J., Abdelrahman, M. S. I., Threadgill, M. D., Thompson, A. S., & Thiemermann, C. (2000) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0703391 · Cited by 89
Histone carbonylation in vivo and in vitro
Wondrak, G. T., Cervantes-Laurean, D., Jacobson, E. L., & Jacobson, M. K. (2000) · Biochemical Journal · doi:10.1042/bj3510769 · Cited by 88
Liaudet, L., Szabó, A., Soriano, F. G., Zingarelli, B., Szabó, C., & Salzman, A. L. (2000) · Shock · doi:10.1097/00024382-200014020-00010 · Cited by 84
Vispé, S., Yung, T. M. C., Ritchot, J., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.170280397 · Cited by 82
Sallmann, F. R., Vodenicharov, M. D., Wang, Z., & Poirier, G. G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.20.15504 · Cited by 79
Anderson, M. G., Scoggin, K. E. S., Simbulan-Rosenthal, C. M., & Steadman, J. A. (2000) · Journal of Virology · doi:10.1128/jvi.74.5.2169-2177.2000 · Cited by 76
Beneke, R., Geisen, C., Zevnik, B., Bauch, T., Müller, W., Küpper, J., & Möröy, T. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.18.6695-6703.2000 · Cited by 71
Cottet, F., Blanché, H., Verasdonck, P., Gall, I. L., Schächter, F., Bürkle, A., & Muiras, M.-L. (2000) · Journal of Molecular Medicine · doi:10.1007/s001090000132 · Cited by 61
Self-citationBeneke, S., Álvarez-González, R., & Bürkle, A. (2000) · Experimental Gerontology · doi:10.1016/s0531-5565(00)00134-0 · Cited by 60
Self-citationPlaschke, K., Kopitz, J., Weigand, M. A., et al. (2000) · Neuroscience Letters · doi:10.1016/s0304-3940(00)00988-5 · Cited by 58
GPI 6150 Prevents H2O2 Cytotoxicity by Inhibiting Poly(ADP-ribose) Polymerase
Zhang, J., Lautar, S. L., Huang, S. H., Ramsey, C., Cheung, A., & Li, J.-H. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3816 · Cited by 44
Chiang, S. K. S., & Lam, T. T. (2000) · PubMed · Cited by 43
Ullrich, O., Ciftci, Ö., & Hass, R. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00399-3 · Cited by 42
Kim, J. W., Kim, K., Kang, K.-W., & Joe, C. O. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.11.8121 · Cited by 40
Wurzer, G., Herceg, Z., & Węsierska‐Gądek, J. (2000) · PubMed · Cited by 38
Albertini, M., Clement, M. G., Lafortuna, C. L., Caniatti, M., Magder, S. A., Abdulmalek, K., & Hussain, S. N. A. (2000) · Journal of Critical Care · doi:10.1053/jcrc.2000.7903 · Cited by 37
Functional Interaction of Poly(ADP-ribose) with the 20S Proteasome in Vitro
Mayer‐Kuckuk, P., Ullrich, O., Ziegler, M., Grune, T., & Schweiger, M. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0824 · Cited by 36
Inhibition of poly(ADP-ribose) polymerase activity is insufficient to induce tetraploidy
Rosenthal, D. S. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.3.841 · Cited by 30
Liu, J., Ying, W., Massa, S. M., Duriez, P. J., Swanson, R. A., Poirier, G. G., & Sharp, F. R. (2000) · Molecular Brain Research · doi:10.1016/s0169-328x(00)00122-4 · Cited by 24
Age-related alteration of poly(ADP-ribose) polymerase activity in different parts of the brain.
Strosznajder, J. B., Jęśko, H. M., & Strosznajder, R. P. (2000) · Acta Biochimica Polonica · doi:10.18388/abp.2000_4012 · Cited by 24
Nucci, C., Piccirilli, S., Rodinò, P., Nisticò, R., Grandinetti, M., Cerulli, L., Leist, M., Nicotera, P., & Bagetta, G. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3811 · Cited by 20
Defending genomic stability over life span:a proposed role for PARP-1
Muiras, M.-L., & Bürkle, A. (2000) · Experimental Gerontology · doi:10.1016/s0531-5565(00)00144-3 · Cited by 15
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Virág, L., & Szabó, C. (2002) · Pharmacological Reviews · doi:10.1124/pr.54.3.375 · Cited by 1,373
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Metadata
- Authors
- Bürkle, A.
- Venue
- BioEssays
- Publisher
- Wiley
- Published
- 2001-08-27
- Volume
- 23
- Issue
- 9
- Pages
- 795-806
- ISSN
- 0265-9247 (ISSN-L)
- 1521-1878
- OpenAlex
- W1844286590
- Cited by
- 335
- References
- 60
- FWCI
- 2.30
- Type
- journal article
- Language
- en
- Open access
- closed
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