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Prepublished online as a Blood First Edition Paper on January 16, 2003; DOI 10.1182/blood-2002-09-2824. This Article Full Text Full Text (PDF) All Versions of this Article: 2002-09-2824v1 101/10/4180    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map 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 Bruce, L. J. Articles by Tanner, M. J.A. Search for Related Content PubMed PubMed Citation Articles by Bruce, L. J. Articles by Tanner, M. J.A. Related Collections Red Cells Transfusion Medicine Gene Expression Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 15 May 2003, Vol. 101, No. 10, pp. 4180-4188 RED CELLS A band 3-based macrocomplex of integral and peripheral proteins in the RBC membrane Lesley J. Bruce, Roland Beckmann, M. Leticia Ribeiro, Luanne L. Peters, Joel A. Chasis, Jean Delaunay, Narla Mohandas, David J. Anstee, and Michael J.A. Tanner From the Department of Biochemistry, University of Bristol; the Department of Haematology, University of Cambridge; the Bristol Institute for Transfusion Sciences, United Kingdom; Unidade de Hematologia Molecular, Servico de Hematologia, Centro Hospitalar de Coimbra, Portugal; Jackson Laboratory, Bar Harbor, ME; Life Sciences Division, University of California, Lawrence Berkeley National Laboratory; INSERM U473 and Service d'Hématologie, d'Immunologie et de Cytogénétique, Hôpital de Bicêtre, Faculté de Médecine Paris-Sud, Le Kremlin-Bicêtre, France; and the New York Blood Center, New York. We have studied the membrane proteins of band 3 anion exchanger (AE1)-deficient mouse and human red blood cells. It has been shown previously that proteins of the band 3 complex are reduced or absent in these cells. In this study we show that proteins of the Rh complex are also greatly reduced (Rh-associated glycoprotein, Rh polypeptides, CD47, glycophorin B) or absent (LW). These observations suggest that the Rh complex is associated with the band 3 complex in healthy RBCs. Mouse band 3(/) RBCs differed from the human band 3-deficient RBCs in that they retained CD47. Aquaporin 1 was reduced, and its glycosylation was altered in mouse and human band 3-deficient RBCs. Proteins of the glycophorin C complex, and other proteins with independent cytoskeletal interactions, were present in normal or increased amounts. To obtain direct evidence for the association of the band 3 and the Rh protein complexes in the RBC, we examined whether Rh complex proteins were coimmunoprecipitated with band 3 from membranes. RhAG and Rh were found to be efficiently coimmunoprecipitated with band 3 from deoxycholate-solubilized membranes. Results suggest that band 3 forms the core of a macrocomplex of integral and peripheral RBC membrane proteins. The presence of these proteins in a single structural macrocomplex makes it likely that they have linked functional or regulatory roles. We speculate that this macrocomplex may function as an integrated CO2/O2 gas exchange unit (metabolon) in the erythrocyte. © 2003 by The American Society of Hematology.   CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: K. P. Jeremy, Z. E. Plummer, D. J. Head, T. E. Madgett, K. L. Sanders, A. Wallington, J. R. Storry, F. Gilsanz, J. Delaunay, and N. D. Avent 4.1R-deficient human red blood cells have altered phosphatidylserine exposure pathways and are deficient in CD44 and CD47 glycoproteins Haematologica, October 1, 2009; 94(10): 1354 - 1361. [Abstract] [Full Text] [PDF] K. Hsu, N. Chi, M. Gucek, J. E. Van Eyk, R. N. Cole, M. Lin, and D. B. 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