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- 저자 : Yoshihiro Ohmiya (검색결과 2 건)
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Polyelectrolyte Hydrogels for Replacement and Regeneration of Biological Tissues
권혁준,Kazunori Yasuda,Jian Ping Gong,Yoshihiro Ohmiya 한국고분자학회 2014 Macromolecular Research Vol.22 No.3
Polyelectrolyte gels are charged polymer networks with macro-ions fixed on the polymer chains. Thesegels have considerable potential for biological applications such as cellular scaffolds and the replacement of variousbiological tissues. Moreover, high strength up to several tens of megapascals can be obtained with polyelectrolytegels by incorporating double network structure in the gel. This article gives a concise review to introduce thefundamental properties of polyelectrolyte gels and biological applications for tissue engineering using theircharacteristic properties. Applications of polyelectrolyte gels have been highlighted in the fields of artificial muscle,artificial corneas, artificial cartilage, scaffolds for in vitro stem cell culture, and scaffolds for in vivo cartilage regeneration. This review suggests that polyelectrolyte gels would be a useful material for the successful replacement and regenerationof damaged or diseased tissues.
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Coactivation of the CLOCK-BMAL1 complex by CBP mediates resetting of the circadian clock.
Lee, Yool,Lee, Jiwon,Kwon, Ilmin,Nakajima, Yoshihiro,Ohmiya, Yoshihiro,Son, Gi Hoon,Lee, Kun Ho,Kim, Kyungjin Cambridge University Press 2010 Journal of cell science Vol.123 No.20
<P>The transcription factor CLOCK-BMAL1 is a core component of the molecular clock machinery that drives circadian gene expression and physiology in mammals. Recently, we reported that this heterodimeric transcription factor functions as a signaling molecule in response to the resetting stimuli via the Ca²+-dependent protein kinase C pathway. Here, we demonstrate that the CREB-binding protein (CBP) plays a key role in rapid activation of the CLOCK-BMAL1 heterodimer that leads to phase resetting of the circadian clock. Under physiological conditions, a bimolecular fluorescence complementation (BiFC) assay revealed that CLOCK and BMAL1 dimerize in the cytoplasm and subsequently translocate into the nucleus in response to serum stimuli (mean time duration was 29.2 minutes and mean velocity 0.7 관m/minute). Concomitantly, BMAL1 rapidly recruited CBP on Per1 promoter E-box, but not p300 (a functional analog of CBP), in the discrete nuclear foci. However, recruitment of CBP by cAMP/Ca²+ response element-binding (CREB) protein on CRE was not markedly increased upon delivery of the resetting stimuli. Furthermore, overexpression of CBP greatly potentiated the CLOCK-BMAL1-mediated Per1 transcription, and this effect was completely abolished by site-directed mutation of E-box elements, but not by the mutation of CRE in the Per1 promoter. Furthermore, molecular knockdown of CBP severely dampened circadian oscillation of clock gene expression triggered by the resetting stimuli. These findings suggest that CBP recruitment by BMAL1 mediates acute transactivation of CLOCK-BMAL1, thereby inducing immediate-early Per1 transcription and phase resetting of the circadian clock.</P>
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