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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:28 Percentile:70.52(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; Kuroki, Ryota; Tanizaki, Yuta*; Tahara, Ayaka*; Beppu, Miho*; Nagasawa, Kazumichi*; Kato, Takashi
no journal, ,
no abstracts in English
Meguro, Mizue; Beppu, Miho*; Nagasawa, Kazumichi*; Adachi, Motoyasu; Okazaki, Nobuo; Tamada, Taro; Kuroki, Ryota; Kato, Takashi
no journal, ,
Meguro, Mizue; Adachi, Motoyasu; Nagasawa, Kazumichi*; Beppu, Miho*; Okazaki, Nobuo; Kosaka, Nami*; Tamada, Taro; Kuroki, Ryota; Kato, Takashi
no journal, ,
Meguro, 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.