Regulation of Gene Expression by Poly(ADP-ribosyl)ation

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Poly(ADP-ribose) syntheate is associated with a chromatin and some nuclear proteins are poly(ADP-ribosyl)ated by the enzyme. However, the physiological role of the modification is still unclear. In order to examine tne effect of poly(ADP-ribosyl)ation on gene expression we first established a method to measure the amount of the enzyme in tissues and cells by the antibody against the enzyme. We determined the change in the amount of the enzyme during the neural differenciation of rat chromafin cells induced by nerve growth factor. The level of the enzyme was decreased during the process. Synthesis of uteroglobin in rabbit uterine epithelial cells during early pregnancy is induced by progesterone. We attempted to determine the change in the amount of. the enzyme during the uteroglobin induction process. However, the level of the enzyme was not large enough to determine by the antibody method. Thus, we isolated a cDNA clone coding for the enzyme. We use the cDNA as a probe to estimate the level of mRNA for the enzyme during the differenciation of murine macrophage tumor cell line. The amount of mRNA for the enzyme decreased to 20% of that for the untreated cells by 2 days after incubation in the presence of <gamma> -interferon, while the Ia antigen. one of the histocompartibility gene products, was markedly induced. We conclude that the enzyme in somehow involved in the gene regulation. especially during differnciation.