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Prepublished online as a Blood First Edition Paper on January 16, 2003; DOI 10.1182/blood-2002-09-2824.
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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.
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