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Prepublished online as a Blood First Edition Paper on September 26, 2002; DOI 10.1182/blood-2002-04-1187. This Article Full Text Full Text (PDF) All Versions of this Article: 2002-04-1187v1 101/3/1194    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 Cytoskeleton Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  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. © 2003 by The American Society of Hematology.   CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: 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] K. N. Dahl, R. Parthasarathy, C. M. Westhoff, D. M. Layton, and D. E. Discher Protein 4.2 is critical to CD47-membrane skeleton attachment in human red cells Blood, February 1, 2004; 103(3): 1131 - 1136. [Abstract] [Full Text] [PDF] V. Nicolas, C. Le Van Kim, P. Gane, C. Birkenmeier, J.-P. Cartron, Y. Colin, and I. Mouro-Chanteloup Rh-RhAG/Ankyrin-R, a New Interaction Site between the Membrane Bilayer and the Red Cell Skeleton, Is Impaired by Rhnull-associated Mutation J. Biol. Chem., July 3, 2003; 278(28): 25526 - 25533. [Abstract] [Full Text] [PDF]

	Copyright © 2003 by American Society of Hematology         Online ISSN: 1528-0020