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• W2023019142 startingPage "1292" @default.
• W2023019142 abstract "The internucleosomal cleavage of genomic DNA is the biochemical hallmark of apoptosis. DNase γ, a Ca2+/Mg2+-dependent endonuclease, has been suggested to be one of the apoptotic endonucleases. We identified here 4-(4,6-dichloro-[1,3,5]-triazin-2-ylamino)-2-(6-hydroxy-3-oxo-3H-xanthen-9-yl)-benzoic acid (DR396) as a novel and potent DNase γ inhibitor using stable HeLa S3 transfectants of DNase γ (HeLa-γ cells). DR396 inhibited apoptotic DNA fragmentation in HeLa-γ cells induced by staurosporine (STS) and in rat splenocytes exposed to γ-ray irradiation in a dose-dependent manner. This compound potently and selectively inhibited DNase γ activity with an IC50 value of 3.2 μM. DR396 did not delay the apoptotic processes as judged by the morphological changes and the cleavage of a death substrate, poly(ADP–ribose) polymerase (PARP). Furthermore, the compound did not prevent apoptotic DNA fragmentation in Jurkat cells induced by anti-Fas antibody (Ab), which is catalyzed by caspase-activated DNase (CAD). These findings clearly indicate that DR396 exerts chemical knockdown effect of DNase γ on cells, suggesting that the compound could be an attractive tool for understanding of the physiological significance of DNase γ." @default.
• W2023019142 created "2016-06-24" @default.
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• W2023019142 date "2004-12-01" @default.
• W2023019142 modified "2023-10-17" @default.
• W2023019142 title "A novel inhibitor that protects apoptotic DNA fragmentation catalyzed by DNase γ" @default.
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• W2023019142 doi "https://doi.org/10.1016/j.bbrc.2004.10.171" @default.
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