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-sheet-rich prion protein in scrapie-infected neuroblastoma cells with human IgG1 antibody specific for -form prion proteinKubota, Toshiya*; Hamazoe, Yuta*; Hashiguchi, Shuhei*; Ishibashi, Daisuke*; Akasaka, Kazuyuki*; Nishida, Noriyuki*; Katamine, Shigeru*; Sakaguchi, Suehiro*; Kuroki, Ryota; Nakashima, Toshihiro*; et al.
Journal of Biological Chemistry, 287(17), p.14023 - 14039, 2012/04
Times Cited Count：5 Percentile：11.64(Biochemistry & Molecular Biology)We prepared -sheet-rich recombinant full-length prion protein (-form PrP) (Jackson, G. S., Hosszu, L. L., Power, A., Hill, A. F., Kenney, J., Saibil, H., Craven, C. J., Waltho, J. P., Clarke, A. R., and Collinge, J. (1999) Science 283, 1935-1937). Using this -form PrP and a human single chain Fv-displaying phage library, we have established a human IgG1 antibody specific to -form but not 
-form PrP, PRB7 IgG. When prion-infected ScN2a cells were cultured with PRB7 IgG, they generated and accumulated PRB7-binding granules in the cytoplasm with time, consequently becoming apoptotic cells bearing very large PRB7-bound aggregates. The SAF32 antibody recognizing the N-terminal octarepeat region of full-length PrP stained distinct granules in these cells as determined by confocal laser microscopy observation. When the accumulation of proteinase K-resistant PrP was examined in prion-infected ScN2a cells cultured in the presence of PRB7 IgG or SAF32, it was strongly inhibited by SAF32 but not at all by PRB7 IgG. Thus, we demonstrated direct evidence of the generation and accumulation of -sheet-rich PrP in ScN2a cells de novo. These results suggest first that PRB7-bound PrP is not responsible for the accumulation of -form PrP aggregates, which are rather an end product resulting in the triggering of apoptotic cell death, and second that SAF32-bound PrP lacking the PRB7-recognizing -form may represent so-called PrPSc with prion propagation activity. PRB7 is the first human antibody specific to -form PrP and has become a powerful tool for the characterization of the biochemical nature of prion and its pathology.
Mochizuki, Masahito*; Higuchi, Ryota*; Katsuyama, Jinya; Toyoda, Masao*
Proceedings of 2007 ASME Pressure Vessels and Piping Division Conference/8th International Conference on Creep and Fatigue at Elevated Temperatures (PVP 2007/CREEP-8) (CD-ROM), 8 Pages, 2007/07
The strength properties of structural steels or their weld zone are influenced by the microscopic heterogeneity. It is important to investigate the stress distribution for clarification of the mechanism of fracture and the material design by considering a grain boundary or its neighborhood because either can be a zone where the stress concentration is likely to occur due to a mismatch of the displacement. For this purpose, FEM-MD coupling method is one of the useful methods because it can treat the mismatch of the displacement caused by the microscopic heterogeneity. In this study, FEM-MD coupling method is proposed and the influence of the microscopic heterogeneity of steels is investigated by using FEM-MD coupling method.
-H)Ru complex derived from H
Ogo, Seiji*; Kabe, Ryota*; Uehara, Keiji*; Kure, Bunsho*; Nishimura, Takashi*; Menon, S. C.*; Harada, Ryosuke*; Fukuzumi, Shunichi*; Higuchi, Yoshiki*; Ohara, Takashi; et al.
Science, 316(5824), p.585 - 587, 2007/04
Times Cited Count：228 Percentile：99.49(Multidisciplinary Sciences)A novel dinuclear nickel-ruthenium complex with a bridging hydrido ligand, a Ni(-H)Ru complex, was obtained from the reaction of a dinuclear NiRu aqua complex with dihydrogen (H) in water under ambient conditions. The structure of the Ni(-H)Ru complex was unequivocally determined by neutron analysis. This is the first crystal structure of (six-coordinated Ni)(-H)M (M=transition metal atoms) that is similar to the core structure of the proposed active form of the [NiFe]hydrogenase.
