The activity of poly(ADP-ribose) polymerase (PARP) is activated upon recognition of DNA strand breaks by its DNA-binding domain and the stimulation of this nuclear enzyme seems to be an early response of cells exposed to a variety of different DNA-damaging agents. In the present work we evaluate the
Effects of poly(ADP-ribose) polymerase inhibition on cell death and chromosome damage induced by VP16 and bleomycin
✍ Scribed by I. D'Agnano; A. Antonelli; B. Bucci; L. Marcucci; P. Petrinelli; R. Ambra; G. Zupi; R. Elli
- Publisher
- John Wiley and Sons
- Year
- 1998
- Tongue
- English
- Weight
- 362 KB
- Volume
- 32
- Category
- Article
- ISSN
- 0893-6692
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✦ Synopsis
Poly(ADP-ribose) polymerase (PARP) is a DNA-bind-induced apoptosis. After VP16 treatment with PARP ing protein involved in cellular response to various inhibition, a reduction in the depletion of the prolifgenotoxic agents. To understand the role of PARP erative compartment and a G2/M phase arrest are in the mechanisms which lead from specific DNA observed. Therefore, the increase in cell viability damage to cell death, we studied the effects of PARP and the reduction in chromosome damage may inhibition in human lymphoblasts damaged with both be the result of a prolonged DNA repair time. bleomycin (BLM) and VP16. These agents can in-Hence, PARP appears to play a significant role in duce DNA breakage but through different mecha-VP16-induced apoptosis and not in BLM-induced nisms, enabling the study of the different effects of apoptosis. Since apoptosis is important in tumor PARP in inducing apoptosis in damaged cells. We treatment these findings might be useful when condemonstrate that in lymphoblasts VP16 treatment sidering the combined employment of PARP inhibiinduces apoptosis to a greater extent than BLM treat-tion with antineoplastic drugs. Environ. Mol. Mutament, and that PARP inhibition reduces VP16-in-gen. 32:56 -63, 1998.
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