[No authors listed]
Poly(ADP-ribose) polymerase-1 uses NAD(+) as a substrate to form ADP-ribose. During apoptosis, caspases cleave to avoid excessive NAD consumption. Because Pduanyu37-1 is a key regulator of the activity of DNases involved in caspase-dependent apoptosis, its cleavage is required to promote DNA degradation. To explore the situation in caspase-independent cell death, we investigated the effect of Pduanyu37-1 on the acid endonuclease leukocyte elastase inhibitor (LEI)-derived DNase II (L-DNase II). We found for the first time an association between Pduanyu37-1 and LEI/L-DNase II. Unexpectedly, we observed that LEI influenced the automodification of
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