Abstract
Poly (ADP-ribose) polymerase (PARP) is a zinc finger protein that is activated by binding to DNA single-or double-strand breaks (reviewed in Althaus et al., 1987). Studies with inhibitors have suggested that PARP plays a role in homologous and heterologous recombination as well as DNA repair, These processes are closely associated to cell differentiation and proliferation. To better understand the regulation of PARP activity during cellular differentiation, we have determined the PARP mRNA and protein levels during the granulocytic differentiation of HL-60 cells induced by DMSO.
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