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Human 8-oxo-G-DNA glycosylase 1 (hOGG1) is a DNA glycosylase to cleave 8-oxo-7,8-dihydroguanine (8-oxo-G), a mutagenic DNA adduct formed by oxidant stresses. Here, we examined hOGG1 protein expression and repair activity to nick a DNA strand at the site of 8-oxo-G during differentiation of hematopoietic cells using HL-60 cells. Overall expression of hOGG1 protein was increased during granulocytic differentiation of HL-60 cells induced by DMSO and monocytic differentiation by vitamine D 3 . Greater level of hOGG1 protein was expressed in DMSO-treated cells. However, change in the DNA nicking activity was not in parallel with the change in hOGG1 protein expression, especially in PMA-treated cells. In PMAtreated cells, the level of hOGG1 protein was lowered, even though the DNA nicking activity was elevated, in a manner similar to the changes in serumdeprived HL-60 cells. These results indicate that hOGG1 expression change during differentiation of hematopoietic stem cells for adaptation to new environments. And the DNA cleaving activity may require additional factor(s) other than expressed hOGG1 protein, especially in apoptotic cell death.

We designed new anthracene-based host material to increase color purity as well as device efficiency. The new blue host, 9,10-bis(2,4-dimethylphenyl)anthracene (BDA), has highly twisted structure and wide band gap due to ortho interaction between anthracene and introduced 2,4-dimethylphenyl substituents. BDA exhibited deep blue fluorescence in solution (λmax = 410 nm) and in solid state (λmax = 429 nm), respectively, with the wide optical band gap (E = 3.12 eV). Blue-light-emitting OLEDs using obtained host and 2% Flu-DPAN as emitter showed 8 cd/A of high efficiency as well as high color purity [CIE coordinates = (0.15, 015)].

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