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Blood, 1 February 2004, Vol. 103, No. 3, pp. 1131-1136.
Prepublished online as a Blood First Edition Paper on October 9, 2003; DOI 10.1182/blood-2003-04-1331.
Submitted April 29, 2003
Accepted September 24, 2003
Protein 4.2 is critical to the CD47-membrane skeleton attachment in the human red cell
Kris Noel Dahl, Ranganath Parthasarathy, Connie M Westhoff, D Mark Layton, and Dennis E Discher*
Department of Chemical and Biomolecular Engineering, University of Pennsylvania, Philadelphia, PA, USA
Institute for Medicine and Engineering, University of Pennsylvania, Philadelphia, PA, USA; School of Engineering and Applied Science, University of Pennsylvania, Philadelphia, PA, USA
Department of Pathology and Laboratory Medicine, University of Pennsylvania, Philadelphia, PA, USA
Department of Hematology, Imperial College, London, United Kingdom
* Corresponding author; email: discher{at}seas.upenn.edu.
The reduction in expression of the integral membrane protein CD47 in human red cells deficient in protein 4.2 suggests that protein 4.2 may mediate a linkage of CD47 to the membrane skeleton. We compared the fractions of membrane skeleton attached CD47, RhAG, Rh and Band 3 in normal and protein 4.2-deficient cells using fluorescence imaged micro-deformation. We found that CD47 attachment decreases from 55% in normal cells to 25-35% in 4.2-deficient cells. RhAG, which has been shown to have no significant variation in expression among the cells studied, shows a significant decrease in membrane skeleton attachment in 4.2-deficient cells from 60% to 40%. Both Rh and Band 3, which have also been shown to have no change in expression, show a smaller decrease from 75% attached in normal RBCs to 55% attached in 4.2-deficient cells. In normal cells, Rh phenotype influences CD47 expression but not the level of CD47's membrane skeleton attachment. In contrast, the results indicate that protein 4.2 strongly influences CD47 levels as well as the extent of membrane skeleton attachment in the red cell, whereas protein 4.2 affects membrane skeletal attachment of RhAG, Rh and Band 3 to a lesser extent.
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