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Blood, 15 February 2006, Vol. 107, No. 4, pp. 1352-1356. Prepublished online as a Blood First Edition Paper on October 6, 2005; DOI 10.1182/blood-2005-08-3166. This Article Full Text (PDF) All Versions of this Article: 2005-08-3166v1 107/4/1352    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Shima, Y. Articles by Tamai, I. Search for Related Content PubMed PubMed Citation Articles by Shima, Y. Articles by Tamai, I. Social Bookmarking                   What's this?  Previous Article  |  Next Article  Submitted August 8, 2005 Accepted September 21, 2005 L-Arginine import via cationic amino acid transporter CAT1 is essential for both differentiation and proliferation of erythrocytes Yoichiro Shima, Tomoji Maeda, Shin Aizawa, Isao Tsuboi, Daisuke Kobayashi, Ryo Kato, and Ikumi Tamai* Department of Molecular Biopharmaceutics, Faculty of Pharmaceutical Sciences, Tokyo University of Science, Noda, Japan Department of Anatomy, Nihon University School of Medicine, Tokyo, Japan * Corresponding author; email: tamai{at}rs.noda.tus.ac.jp. In the present study, we examined the role in hematopoiesis of cationic amino acid transporter 1 (CAT1), which transports L-arginine, L-lysine, L-ornithine and L-histidine. The expression level of human CAT1 (hCAT1) mRNA in mononuclear cells (MNC) fractionated according to lineage-selective markers was examined by RT-PCR. The expression of CAT1 in glycophorin A-positive erythroid cells was 8 times higher than in non-fractionated MNC (control) cells. Characteristics of L-arginine uptake by K562 cells, an established leukemic cell line used as an erythroid model, were similar to those of CAT1 as regards saturation kinetics, sodium independence and substantial inhibition of L-arginine uptake by N-ethylmaleimide, which is a specific inhibitor of system y+ amino acid transporter. Removal of L-arginine from the culture medium prevented both proliferation and differentiation of K562 cells, while removal of L-lysine or L-histidine had little effect on differentiation, though proliferation was blocked. Hematopoetic stem cells obtained from human cord blood failed to develop into erythroid cells in the absence of L-arginine in the culture medium. These findings indicate that hCAT1 is involved in erythroid hematopoiesis through its role in importing L-arginine, which appears to be essential for the differentiation of red blood cells. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: C. C. Huang, C.-B. Chiribau, M. Majumder, C.-M. Chiang, R. C. Wek, R. J. Kelm Jr., K. Khalili, M. D. Snider, and M. Hatzoglou A Bifunctional Intronic Element Regulates the Expression of the Arginine/Lysine Transporter Cat-1 via Mechanisms Involving the Purine-rich Element Binding Protein A (Pur{alpha}) J. Biol. Chem., November 20, 2009; 284(47): 32312 - 32320. [Abstract] [Full Text] [PDF]

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