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The emerging role of poly(ADP-ribose) polymerase-1 in longevity

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2005

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Brabeck, Christine
Diefenbach, Jörg

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https://doi.org/10.1016/j.biocel.2004.10.006
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The International Journal of Biochemistry & Cell Biology. Elsevier. 2005, 37(5), pp. 1043-1053. ISSN 1357-2725. eISSN 1878-5875. Available under: doi: 10.1016/j.biocel.2004.10.006

Zusammenfassung

In the present paper, the involvement of the family of poly(ADP-ribose) polymerases (PARPs), and especially of PARP-1, in mammalian longevity is reviewed. PARPs catalyse poly(ADP-ribosyl)ation, a covalent post-translational protein modification in eukaryotic cells. PARP-1 and PARP-2 are activated by DNA strand breaks, play a role in DNA base-excision repair (BER) and are survival factors for cells exposed to low doses of ionising radiation or alkylating agents. PARP-1 is the main catalyst of poly(ADP-ribosyl)ation in living cells under conditions of DNA breakage, accounting for about 90% of cellular poly(ADP-ribose). DNA-damage-induced poly(ADP-ribosyl)ation also functions as a negative regulator of DNA damage-induced genomic instability. Cellular poly(ADP-ribosyl)ation capacity in permeabilised mononuclear blood cells (MNC) is positively correlated with life span of mammalian species. Furthermore PARP-1 physically interacts with WRN, the protein deficient in Werner syndrome, a human progeroid disorder, and PARP-1 and WRN functionally cooperate in preventing carcinogenesis in vivo. Some of the other members of the PARP family have also been revealed as important regulators of cellular functions relating to ageing/longevity. In particular, tankyrase-1, tankyrase-2, PARP-2 as well as PARP-1 have been found in association with telomeric DNA and are able to poly(ADP-ribosyl)ate the telomere-binding proteins TRF-1 and TRF-2, thus blocking their DNA-binding activity and controlling telomere extension by telomerase.

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570 Biowissenschaften, Biologie

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Aging, Longevity, DNA repair, Poly(ADP-ribose), Genomic instability

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ISO 690BÜRKLE, Alexander, Christine BRABECK, Jörg DIEFENBACH, Sascha BENEKE, 2005. The emerging role of poly(ADP-ribose) polymerase-1 in longevity. In: The International Journal of Biochemistry & Cell Biology. Elsevier. 2005, 37(5), pp. 1043-1053. ISSN 1357-2725. eISSN 1878-5875. Available under: doi: 10.1016/j.biocel.2004.10.006
BibTex
@article{Burkle2005-05emerg-52112,
  year={2005},
  doi={10.1016/j.biocel.2004.10.006},
  title={The emerging role of poly(ADP-ribose) polymerase-1 in longevity},
  number={5},
  volume={37},
  issn={1357-2725},
  journal={The International Journal of Biochemistry & Cell Biology},
  pages={1043--1053},
  author={Bürkle, Alexander and Brabeck, Christine and Diefenbach, Jörg and Beneke, Sascha}
}
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    <dcterms:abstract xml:lang="eng">In the present paper, the involvement of the family of poly(ADP-ribose) polymerases (PARPs), and especially of PARP-1, in mammalian longevity is reviewed. PARPs catalyse poly(ADP-ribosyl)ation, a covalent post-translational protein modification in eukaryotic cells. PARP-1 and PARP-2 are activated by DNA strand breaks, play a role in DNA base-excision repair (BER) and are survival factors for cells exposed to low doses of ionising radiation or alkylating agents. PARP-1 is the main catalyst of poly(ADP-ribosyl)ation in living cells under conditions of DNA breakage, accounting for about 90% of cellular poly(ADP-ribose). DNA-damage-induced poly(ADP-ribosyl)ation also functions as a negative regulator of DNA damage-induced genomic instability. Cellular poly(ADP-ribosyl)ation capacity in permeabilised mononuclear blood cells (MNC) is positively correlated with life span of mammalian species. Furthermore PARP-1 physically interacts with WRN, the protein deficient in Werner syndrome, a human progeroid disorder, and PARP-1 and WRN functionally cooperate in preventing carcinogenesis in vivo. Some of the other members of the PARP family have also been revealed as important regulators of cellular functions relating to ageing/longevity. In particular, tankyrase-1, tankyrase-2, PARP-2 as well as PARP-1 have been found in association with telomeric DNA and are able to poly(ADP-ribosyl)ate the telomere-binding proteins TRF-1 and TRF-2, thus blocking their DNA-binding activity and controlling telomere extension by telomerase.</dcterms:abstract>
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