Ayako Nakajima

Hyper-stable organo-Eu(III) luminophore under high temperature for photo-industrial application.

Novel organo-EuIII luminophores, Eu(hfa)x(CPO)y and Eu(hfa)x(TCPO)y (hfa: hexafluoroacetylacetonate, CPO: 4-carboxyphenyl diphenyl phosphine oxide, TCPO: 4,4′,4″-tricarboxyphenyl phosphine oxide), were synthesized by the complexation of EuIII ions with hfa moieties and CPO or TCPO ligands. The thermal and luminescent stabilities of the luminophores are extremely high. The decomposition temperature of Eu(hfa)x(CPO)y and Eu(hfa)x(TCPO)y were determined as 200 and 450 °C, respectively. The luminescence of Eu(hfa)x(TCPO)y under UV light irradiation was observed even at a high temperature, 400 °C. The luminescent properties of Eu(hfa)x(CPO)y and Eu(hfa)x(TCPO)y were estimated from emission spectra, quantum yields and lifetime measurements. The energy transfer efficiency from hfa moieties to EuIII ions in Eu(hfa)x(TCPO)y was 59%. The photosensitized luminescence of hyper-stable Eu(hfa)x(TCPO)y at 400 °C is demonstrated for future photonic applications.

Characterization of binding between SF-1 and Sp1: Predominant interaction of SF-1 with the N-terminal region of Sp1

The transcription factor specificity protein 1 (Sp1) binds to GC boxes and interacts with many transcription factors to regulate gene expression. Steroidogenic factor-1 (SF-1) is an orphan nuclear receptor and plays a major role in regulation of the human steroidogenic acute regulatory (StAR) gene. We demonstrated that there is interaction between SF-1 and Sp1 on the human StAR promoter. In the present study, we examined the mechanism of the interaction between Sp1 and SF-1 on the human StAR gene promoter. Results of glutathione S-transferase (GST) pull-down assays and a mammalian twohybrid assay showed that SF-1 interacted with Sp1 through the N-terminal domains of Sp1. Results of electrophoretic mobility shift assays using nuclear extracts showed that Sp1 is associated with SF-1-DNA complex formation. The density of SF-1-DNA complex was much greater when recombinant Sp1 was added to the incubation mixture. These results suggest that Sp1 interacts with SF-1 and that Sp1 enhances SF-1- DNA complex formation to regulate human StAR transcription.