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Prepublished online as a Blood First Edition Paper on September 5, 2002; DOI 10.1182/blood-2002-04-1285.
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Blood, 1 January 2003, Vol. 101, No. 1, pp. 338-344
RED CELLS
Evidence that the red cell skeleton protein 4.2 interacts with
the Rh membrane complex member CD47
Isabelle Mouro-Chanteloup,
Jean Delaunay,
Pierre Gane,
Virginie Nicolas,
Mette Johansen,
Eric J. Brown,
Luanne L. Peters,
Caroline Le Van Kim,
Jean
Pierre Cartron, and
Yves Colin
From the Institut National de la Santé et de la
Recherche Médicale (INSERM) U76, Institut National de la
Transfusion Sanguine, Paris, France; INSERM U473, Service
d'Hématologie, I, Hopital Bicêtre, AP-HP, Faculté de
Medecine Paris-Sud, Le Kremlin Bicêtre, France; Center for
Host/Pathogen Interactions, University of California, San Francisco;
and The Jackson Laboratory, Bar Harbor, ME.
Rhnull red cells are characteristically
stomato-spherocytic. This and other evidence suggest that the Rh
complex represents a major attachment site between the membrane lipid
bilayer and the erythroid skeleton. As an attempt to identify the
linking protein(s) between the red cell skeleton and the Rh complex, we analyzed the expression of Rh, RhAG, CD47, LW, and glycophorin B
proteins in red cells from patients with hereditary spherocytosis associated with complete protein 4.2 deficiency but normal band 3 (4.2(-)HS). Flow cytometric and immunoblotting analysis
revealed a severe reduction of CD47 (up to 80%) and a slower mobility
of RhAG on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, possibly reflecting an overglycosylation state. Unexpectedly, 4.2 / mice, which are anemic, displayed a normal red
cell expression of CD47 and RhAG. These results suggest that human
protein 4.2, through interaction with CD47, is involved in the skeleton
linkage and/or membrane translocation of the Rh complex. However, these potential role(s) of protein 4.2 might be not conserved across species.
Finally, the absence or low expression of red cell CD47 in
CD47/ mice and in some humans carrying RHCE
gene variants (D--, D.., and RN), respectively, had
no detectable effect on protein 4.2 and RhAG expression. Since these
cells are morphologically normal with no sign of hemolysis, it is
assumed that CD47 deficiency per se is not responsible for the cell
shape abnormalities and for the compensated hemolytic anemia typical of
4.2(-) and Rhnull red cells.
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