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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
Times Cited Count：29 Percentile：70.4(Biology)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.
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.
Matsumoto, Fumiko; Adachi, Motoyasu; Shimizu, Rumi; Meguro, Mizue; Tamada, Taro; Kato, Takashi; Kuroki, Ryota
no journal, ,
Thrombopoietin (TPO) is a glycoprotein hormone produced mainly by the liver and the kidney that regulates the production of platelets by the bone marrow. It stimulates the production and differentiation of megakaryocytes, the bone marrow cells that fragment into large numbers of platelets. The extracellular domain consists of 450 amino acid residues of thrombopoietin receptor (soluble TPO-R) contains two repeat of cytokine receptor homologous region, CRH-1 and CRH-2. In this work, we prepare CRH-1domein of TPO-R, and we discover that CRH-1 has binding site of TPO.
Meguro, Mizue; Adachi, Motoyasu; Kuroki, Ryota; Tanizaki, Yuta*; Tahara, Ayaka*; Beppu, Miho*; Nagasawa, Kazumichi*; Kato, Takashi
no journal, ,
no abstracts in English
erythropoietin and evolutionary conservation of its structureMeguro, Mizue; Beppu, Miho*; Nagasawa, Kazumichi*; Adachi, Motoyasu; Okazaki, Nobuo; Tamada, Taro; Kuroki, Ryota; Kato, Takashi
no journal, ,
Tahara, Ayaka*; Tanizaki, Yuta*; Okui, Takehito*; Meguro, Mizue; Kinoshita, Sayaka*; Maekawa, Shun*; Yamauchi, Motoki*; Shimoji, Miyako*; Ishida, Takako*; Nagai, Yutaka*; et al.
no journal, ,
Matsumoto, Fumiko; Adachi, Motoyasu; Shimizu, Rumi; Meguro, Mizue; Arai, Shigeki; Tamada, Taro; Kato, Takashi; Kuroki, Ryota
no journal, ,
Meguro, Mizue; Adachi, Motoyasu; Nagasawa, Kazumichi*; Beppu, Miho*; Okazaki, Nobuo; Kosaka, Nami*; Tamada, Taro; Kuroki, Ryota; Kato, Takashi
no journal, ,
erythropoietinMeguro, Mizue; Nagasawa, Kazumichi*; Kosaka, Nami*; Adachi, Motoyasu; Okazaki, Nobuo; Tamada, Taro; Kuroki, Ryota; Kato, Takashi
no journal, ,
no abstracts in English
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.
