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Prepublished online as a Blood First Edition Paper on September 26, 2002; DOI 10.1182/blood-2002-04-1187.
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Blood, 1 February 2003, Vol. 101, No. 3, pp. 1194-1199
RED CELLS
Fractional attachment of CD47 (IAP) to the erythrocyte
cytoskeleton and visual colocalization with Rh protein
complexes
Kris Noel Dahl,
Connie M. Westhoff, and
Dennis
E. Discher
From the School of Engineering and Applied Science,
Institute for Medicine and Engineering, and Department of Pathology and
Laboratory Medicine, University of Pennsylvania, PA.
Interactions of CD47 and RhAG and the Rh proteins are visualized
between one another and with the cytoskeleton of intact erythrocytes. In a first study, CD47 is labeled with a phycoerythrin (PhE)- tagged
antibody, which generates discrete spots that reflect induced clusters
of CD47. Rh and RhAG colocalize with each other and to these induced
clusters, whereas Band 3 and glycophorin C remain more homogeneously
dispersed on the cell periphery. In a second study, red cells are
aspirated into a micropipette, and immunofluorescent maps of the
surface gradients that develop for CD47 and RhAG determine cytoskeletal
connectivity. CD47 and RhAG gradients on normal red cells prove to be
nearly identical and also appear intermediate to those found for the
fluid bilayer and network-linked glycophorin C. Similar gradients are
obtained for CD47 on Rhnull cells, suggesting that linkage
of CD47 to the spectrin-actin skeleton is independent of Rh or RhAG and
is not affected by CD47's reduced surface expression on these cells.
The results show that CD47 colocalizes with Rh and RhAG but is
fractionally attached to the red cell membrane skeleton independent of
these and other major integral membrane proteins involved in
cytoskeletal attachment. The results imply a homogeneous base
distribution of CD47, restrained by cytoskeleton linkages, plus a
smaller fraction of CD47, which is able to diffuse in the membrane.
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