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 Blood, 15 March 2005, Vol. 105, No. 6, pp. 2421-2427.
Prepublished online as a Blood First Edition Paper on September 21, 2004; DOI 10.1182/blood-2004-07-2823.

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IMMUNOBIOLOGY

Adhesion of human T cells to antigen-presenting cells through SIRP{beta}2-CD47 interaction costimulates T-cell proliferation

Laura Piccio, William Vermi, Kent S. Boles, Anja Fuchs, Carey A. Strader, Fabio Facchetti, Marina Cella, and Marco Colonna

From the Department of Pathology and Immunology, Washington University School of Medicine, St Louis, MO; Department of Neurological Sciences, Istituto di Ricovero e Cura a Carattere Scientifico (IRCCS) Ospedale Maggiore Policlinico, and "Dino Ferrari" Center, Milano, Italy; and Department of Pathology, University of Brescia, Brescia, Italy.

Signal-regulatory proteins (SIRPs) are transmembrane glycoproteins belonging to the immunoglobulin (Ig) superfamily that are expressed in the immune and central nervous systems. SIRP{alpha} binds CD47 and inhibits the function of macrophages, dendritic cells, and granulocytes, whereas SIRP{beta}1 is an orphan receptor that activates the same cell types. A recently identified third member of the SIRP family, SIRP{beta}2, is as yet uncharacterized in terms of expression, specificity, and function. Here, we show that SIRP{beta}2 is expressed on T cells and activated natural killer (NK) cells and, like SIRP{alpha}, binds CD47, mediating cell-cell adhesion. Consequently, engagement of SIRP{beta}2 on T cells by CD47 on antigen-presenting cells results in enhanced antigen-specific T-cell proliferation.


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CD47 and SIRPs: new openings
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