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Blood, 15 March 2006, Vol. 107, No. 6, pp. 2548-2556. Prepublished online as a Blood First Edition Paper on November 15, 2005; DOI 10.1182/blood-2005-04-1463. This Article Full Text Full Text (PDF) Supplemental Figures All Versions of this Article: 2005-04-1463v1 107/6/2548    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 Subramanian, S. Articles by Discher, D. E. Search for Related Content PubMed PubMed Citation Articles by Subramanian, S. Articles by Discher, D. E. Related Collections Red Cells Signal Transduction Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  RED CELLS Species- and cell type-specific interactions between CD47 and human SIRP Shyamsundar Subramanian, Ranganath Parthasarathy, Shamik Sen, Eric T. Boder, and Dennis E. Discher From the School of Engineering and Applied Science, University of Pennsylvania, Philadelphia, PA. CD47 on red blood cells (RBCs) reportedly signals "self" by binding SIRP on phagocytes, at least in mice. Such interactions across and within species, from mouse to human, are not yet clear and neither is the relation to cell adhesion. Using human SIRP1 as a probe, antibody-inhibitable binding to CD47 was found only with human and pig RBCs (not mouse, rat, or cow). In addition, CD47-mediated adhesion of human and pig RBCs to SIRP1 surfaces resists sustained forces in centrifugation (as confirmed by atomic force microscopy) but only at SIRP-coating densities far above those measurable on human neutrophils, monocytes, and THP-1 macrophages. While interactions strengthen with deglycosylation of SIRP1, low copy numbers explain the absence of RBC adhesion to phagocytes under physiologic conditions and imply that the interaction being studied is not responsible for red cell clearance in humans. Evidence of clustering nonetheless suggests mechanisms of avidity enhancement. Finally, using the same CD47 antibodies and soluble SIRP1, bone marrow-derived mesenchymal stem cells were assayed and found to display CD47 but not bind SIRP1 significantly. The results thus demonstrate that SIRP-CD47 interactions, which reportedly define self, exhibit cell type specificity and limited cross-species reactivity. (Blood. 2006;107:2548-2556) CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: W. Y. Lee, D. A. Weber, O. Laur, E. A. Severson, I. McCall, R. P. Jen, A. C. Chin, T. Wu, K. M. Gernet, and C. A. Parkos Novel Structural Determinants on SIRP{alpha} that Mediate Binding to CD47 J. Immunol., December 1, 2007; 179(11): 7741 - 7750. [Abstract] [Full Text] [PDF] K. Ide, H. Wang, H. Tahara, J. Liu, X. Wang, T. Asahara, M. Sykes, Y.-G. Yang, and H. Ohdan Role for CD47-SIRP{alpha} signaling in xenograft rejection by macrophages PNAS, March 20, 2007; 104(12): 5062 - 5066. [Abstract] [Full Text] [PDF] S. Subramanian, E. T. Boder, and D. E. Discher Phylogenetic Divergence of CD47 Interactions with Human Signal Regulatory Protein {alpha} Reveals Locus of Species Specificity: IMPLICATIONS FOR THE BINDING SITE J. Biol. Chem., January 19, 2007; 282(3): 1805 - 1818. [Abstract] [Full Text] [PDF] D. Braun, L. Galibert, T. Nakajima, H. Saito, V. V. Quang, M. Rubio, and M. Sarfati Semimature Stage: A Checkpoint in a Dendritic Cell Maturation Program That Allows for Functional Reversion after Signal-Regulatory Protein-{alpha} Ligation and Maturation Signals J. Immunol., December 15, 2006; 177(12): 8550 - 8559. [Abstract] [Full Text] [PDF]

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