Abstract
Incubation of isolated rat liver nuclei with ATP, NAD+, and submicromolar Ca2+ concentrations resulted in extensive DNA hydrolysis. Half-maximal activity occurred with 200 nM Ca2+, and saturation of the process was observed with 1 μM Ca2+. ATP stimulated a calmodulin-dependent nuclear Ca2+ uptake system which apparently mediated endonuclease activation. Ca2+-activated DNA fragmentation was inhibited by the inhibitor of poly(ADP-ribose) synthetase, 3-aminobenzamide, and was associated with poly(ADP-ribosyl)ation of nuclear protein. The characteristics of this endonuclease activity indicate that it may be responsible for the Ca2+-dependent fragmentation of DNA involved in programmed cell death (apoptosis) and in certain forms of chemically induced cell killing.
Original language | English (US) |
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Pages (from-to) | 6398-6403 |
Number of pages | 6 |
Journal | Journal of Biological Chemistry |
Volume | 264 |
Issue number | 11 |
State | Published - 1989 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology