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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. This Article Full Text Full Text (PDF) All Versions of this Article: 2003-04-1331v1 103/3/1131    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 Dahl, K. N. Articles by Discher, D. E. Search for Related Content PubMed PubMed Citation Articles by Dahl, K. N. Articles by Discher, D. E. Related Collections Red Cells Cell Adhesion and Motility Cytoskeleton Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  RED CELLS Protein 4.2 is critical to CD47-membrane skeleton attachment in human red cells Kris Noel Dahl, Ranganath Parthasarathy, Connie M. Westhoff, D. Mark Layton, and Dennis E. Discher From the Department of Chemical and Biomolecular Engineering and School of Engineering and Applied Science, Institute for Medicine and Engineering, University of Pennsylvania, Philadelphia; Department of Pathology and Laboratory Medicine, University of Pennsylvania, Philadelphia; and Department of Hematology, Imperial College, London, United Kingdom. The reduction in expression of the integral membrane protein CD47 in human red blood cells (RBCs) 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, Rh-associated glycoprotein (RhAG), Rh, and band 3 in normal and protein 4.2-deficient cells using fluorescence-imaged microdeformation. We found that CD47 attachment decreases from 55% in normal cells to 25% to 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 membrane skeleton attachment of CD47. In contrast, the results indicate that protein 4.2 strongly influences CD47 levels as well as the extent of membrane skeleton attachment in the RBC, whereas protein 4.2 affects membrane skeletal attachment of RhAG, Rh, and band 3 to a lesser extent. (Blood. 2004;103:1131-1136) CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: S. E. Iismaa, B. M. Mearns, L. Lorand, and R. M. Graham Transglutaminases and Disease: Lessons From Genetically Engineered Mouse Models and Inherited Disorders Physiol Rev, July 1, 2009; 89(3): 991 - 1023. [Abstract] [Full Text] [PDF] R. K. Tsai and D. E. Discher Inhibition of "self" engulfment through deactivation of myosin-II at the phagocytic synapse between human cells J. Cell Biol., March 5, 2008; 180(5): 989 - 1003. [Abstract] [Full Text] [PDF] M. Stefanovic, N. O. Markham, E. M. Parry, L. J. Garrett-Beal, A. P. Cline, P. G. Gallagher, P. S. Low, and D. M. Bodine An 11-amino acid beta-hairpin loop in the cytoplasmic domain of band 3 is responsible for ankyrin binding in mouse erythrocytes PNAS, August 28, 2007; 104(35): 13972 - 13977. [Abstract] [Full Text] [PDF] S. Subramanian, R. Parthasarathy, S. Sen, E. T. Boder, and D. E. Discher Species- and cell type-specific interactions between CD47 and human SIRP{alpha} Blood, March 15, 2006; 107(6): 2548 - 2556. [Abstract] [Full Text] [PDF] Z. S. Bowman, J. D. Morrow, D. J. Jollow, and D. C. McMillan Primaquine-Induced Hemolytic Anemia: Role of Membrane Lipid Peroxidation and Cytoskeletal Protein Alterations in the Hemotoxicity of 5-Hydroxyprimaquine J. Pharmacol. Exp. Ther., August 1, 2005; 314(2): 838 - 845. [Abstract] [Full Text] [PDF]

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