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Journal of Biochemistry 2005 138(2):167-175; doi:10.1093/jb/mvi113
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© 2005 The Japanese Biochemical Society

Regular Paper

Expression of Erythropoietin Receptor–Like Molecule in Xenopus laevis and Erythrocytopenia upon Administration of Its Recombinant Soluble Form

Youichi Aizawa1, Nami Nogawa1, Nobuyoshi Kosaka1, Yasutaka Maeda1, Takafumi Watanabe1, Hiroshi Miyazaki3 and Takashi Kato1,2,*

1 Major in Integrative Bioscience and Biomedical Engineering, Graduate School of Science and Engineering, and 2 Department of Biology, School of Education, Waseda University, Nishi-waseda 1-6-1, Shinjuku-ku, Tokyo 169-8050; and 3 Pharmaceutical Research Laboratory, Kirin Brewery Co., Ltd., Miyaharacho 3, Takasaki, Gunma 370-1295

* To whom correspondence should be addressed at: Department of Biology, School of Education, Waseda University, 1-6-1, Nishi-waseda, Shinjuku-ku Tokyo, 169-8050. Tel: +81-3-5286-1519; Fax: +81-3-3207-9694, E-mail: tkato{at}waseda.jp

The regulation of hematopoiesis in non-mammalian vertebrates is poorly understood. This is partly because the structures and effects of most hematopoietic regulators have not been identified. As a first step towards studies on the key mechanism of hematopoietic regulation among phyla as well as the diversity of organisms, we have focused on amphibian hematopoiesis. A cDNA sharing the highest degree of homology with mammalian erythropoietin (EPO) receptors, tentatively named xlEPOR, was cloned from a cDNA library of Xenopus laevis immature erythrocytes. The comparative identities of the deduced entire amino acid sequence to mammalian EPO receptors were quite low, although functional domains indispensable for erythropoietic activities were found in the molecule. Northern analysis revealed that xlEPOR were expressed in peripheral blood cells. In the peripheral blood of phenylhydrazine-treated adult Xenopus, immature erythrocytes expressing xlEPOR were identified by in situ hybridization and immunostaining with polyclonal antibodies to xlEPOR. To confirm the biological functions of this molecule, the extracellular domain of xlEPOR (i.e., soluble xlEPOR) was administered to adult Xenopus by consecutive intracardiac injection. The peripheral erythrocyte counts were decreased gradually; meanwhile, immature erythrocytes appeared in the circulation, demonstrating that xlEPOR plays a significant physiological role in erythropoiesis in Xenopus laevis.


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