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Negative regulation of alkylation-induced sister-chromatid exchange by poly(ADP-ribose) polymerase-1 activity

Lookup NU author(s): Professor Alexander Burkle


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One of the earliest responses to DNA damage in eukaryotic cells is activation of poly(ADP-ribose) polymerase-1 (PARP-1), a DNA strand break-dependent nuclear enzyme which covalently modifies proteins with poly(ADP-ribose). Here, we show that conditional over-expression of PARP-1 in stably transfected hamster cells, which causes cellular over-accumulation of poly(ADP-ribose) by several-fold, strongly suppresses alkylation-induced sister-chromatid exchange (SCE), while cytotoxicity of alkylation treatment is slightly enhanced. Viewed together with the known potentiation of SCE by abrogation of PARP-1 activity, our results provide evidence that PARP-1 activity is an important regulator of alkylation-induced SCE formation, imposing a control that is strictly negative and commensurate with the level of enzyme activity. (C) 2000 Wiley-Liss, Inc.

Publication metadata

Author(s): Meyer R, Muller M, Beneke S, Kupper J-H, Burkle A

Publication type: Article

Publication status: Published

Journal: International Journal of Cancer

Year: 2000

Volume: 88

Issue: 3

Pages: 351-355

ISSN (print): 0020-7136

ISSN (electronic): 1097-0215

Publisher: John Wiley & Sons


DOI: 10.1002/1097-0215(20001101)88:3<351::AID-IJC5>3.0.CO;2-H

PubMed id: 11054662


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