PSTEP: Project for solar-terrestrial environment prediction

Kusano, Kanya*; Ichimoto, Kiyoshi*; Ishii, Mamoru*; Miyoshi, Yoshizumi*; Yoden, Shigeo*; Akiyoshi, Hideharu*; Asai, Ayumi*; Ebihara, Yusuke*; Fujiwara, Hitoshi*; Goto, Tadanori*; et al.

Earth, Planets and Space (Internet), 73(1), p.159_1 - 159_29, 2021/12

https://doi.org/10.1186/s40623-021-01486-1

The PSTEP is a nationwide research collaboration in Japan and was conducted from April 2015 to March 2020, supported by a Grant-in-Aid for Scientific Research on Innovative Areas from the Ministry of Education, Culture, Sports, Science and Technology of Japan. It has made a significant progress in space weather research and operational forecasts, publishing over 500 refereed journal papers and organizing four international symposiums, various workshops and seminars, and summer school for graduate students at Rikubetsu in 2017. This paper is a summary report of the PSTEP and describes the major research achievements it produced.

Identification of erythroid progenitors induced by erythropoietic activity in

Kosaka, Nami*; Sugai, Tatsuhisa*; Nagasawa, Kazumichi*; Tanizaki, Yuta*; Meguro, Mizue; Aizawa, Yoichi*; Maekawa, Shun*; Adachi, Motoyasu; Kuroki, Ryota; Kato, Takashi

Journal of Experimental Biology, 214(6), p.921 - 927, 2011/03

https://doi.org/10.1242/jeb.050286

Oxygen is essential for the survival of animals. Red blood cells are responsible for transporting oxygen to tissues. We established a semi-solid colony forming assay, and showed that recombinant xlEPO induces erythroid colony formation in vitro and detected an increased level of erythropoietin activity in blood serum during acute anemic stress. In addition, the study demonstrated the possible presence of multiple, non-xlEPO, factors in anemic serum supportive of erythroid colony formation. These results indicate that erythropoiesis mediated by erythropoietin is present in amphibian species and, furthermore, that the regulatory mechanisms controlling peripheral erythrocyte number may vary among vertebrates.

Advanced fusion technologies developed for JT-60 superconducting Tokamak

Sakasai, Akira; Ishida, Shinichi; Matsukawa, Makoto; Akino, Noboru; Ando, Toshinari*; Arai, Takashi; Ezato, Koichiro; Hamada, Kazuya; Ichige, Hisashi; Isono, Takaaki; et al.

Nuclear Fusion, 44(2), p.329 - 334, 2004/02

https://doi.org/10.1088/0029-5515/44/2/015

no abstracts in English

Engineering design study of JT-60 superconducting modification

Sakasai, Akira; Ishida, Shinichi; Matsukawa, Makoto; Kurita, Genichi; Akino, Noboru; Ando, Toshinari*; Arai, Takashi; Ichige, Hisashi; Kaminaga, Atsushi; Kato, Takashi; et al.

Proceedings of 19th IEEE/NPSS Symposium on Fusion Engineering (SOFE), p.221 - 225, 2002/00

no abstracts in English

Crystal structure of Xenopus laevis erythropoietin

Meguro, Mizue; Adachi, Motoyasu; Okazaki, Nobuo; Tamada, Taro; Kuroki, Ryota; Kato, Takashi

no journal, , 

Erythropoietin (EPO) is a glycoprotein regulating the level of erythrocytes. We have first identified EPO from Xenopus laevis. The proliferation assay of xlEPO prepared using E. coli expression system showed that xlEPO stimulates proliferation of cells expressing xlEPO receptors and the cells expressing huEPO receptors. Cross activity between xlEPO and huEPO against corresponding receptors suggests that receptor recognition scheme of xlEPO is conserved with that of huEPO. Further, we have succeeded in crystallization of recombinant EPO from Xenopus laevis by sitting drop vapor diffusion method. The X-ray diffraction data at 2.9 was obtained. The phase was determined molecular replacement method.

Effect of the C-terminal mutation cytokine expression levels in

Meguro, Mizue; Adachi, Motoyasu; Kuroki, Ryota; Tanizaki, Yuta*; Tahara, Ayaka*; Beppu, Miho*; Nagasawa, Kazumichi*; Kato, Takashi

no journal, , 

no abstracts in English

Characterization of Xenopus laevis thrombocytic cells stimulated by thrombopoietin in liquid culture

Tahara, Ayaka*; Tanizaki, Yuta*; Okui, Takehito*; Meguro, Mizue; Kinoshita, Sayaka*; Maekawa, Shun*; Yamauchi, Motoki*; Shimoji, Miyako*; Ishida, Takako*; Nagai, Yutaka*; et al.

no journal, , 

Implication of molecular diversity and functional conservation of erythropoietin based on a comparison of tertiary structures of humans and frogs

Meguro, Mizue; Adachi, Motoyasu; Nagasawa, Kazumichi*; Beppu, Miho*; Okazaki, Nobuo; Kosaka, Nami*; Tamada, Taro; Kuroki, Ryota; Kato, Takashi

no journal, , 

Structural determinations of four helical vertebrate cytokines that stimulate the production of blood cells

Adachi, Motoyasu; Meguro, Mizue*; Maekawa, Shun*; Okazaki, Nobuo*; Beppu, Miho*; Nagasawa, Kazumichi*; Hirano, Ayumi*; Tamada, Taro; Kato, Takashi; Kuroki, Ryota

no journal, , 

The crystal structures of human EPO and human TPO have been determined both as a receptor bound form and a monoclonal antibody bound form, but isolated structures have not been determined. To determine how much structural and functional differences in hematopoietic cell growth factors exist, we are investigating structure and function of EPO and TPO homologues derived from other vertebrates such as amphibian and fish. Recently, we succeeded in preparations of recombinant EPOs from Xenopus laevis (xl-EPO) and Oryzias latipes (ol-EPO) using E. coli expression and Brevibacillus secretion systems, respectively, and both EPOs were successfully crystallized. The structure determinations of xl-EPO and ol-EPO will contribute to further understanding of the structure-function relationships of EPO including the structural change upon receptor binding.