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International Immunology, Vol. 11, No. 5, 707-718, May 1999
© 1999 Japanese Society for Immunology

Cell spreading distinguishes the mechanism of augmentation of T cell activation by integrin-associated protein/CD47 and CD28

Martina I. Reinhold, Jennifer M. Green1, Frederik P. Lindberg, Michel Ticchioni2 and Eric J. Brown1

Division of Infectious Diseases, Washington University School of Medicine, Box 8051,660 South Euclid Avenue, St Louis, MO 63110, USA
2 Laboratoire Central d'Immunologie, Centre Hospitalier Universitaire de Nice, Nice, France

Correspondence to: E. J. Brown, Program in Microbial Pathogenesis and Host Defense, HSE 201, Campus Box 0513, University of California, 513 Parnassus Ave., San Francisco, CA 94143

Integrin-associated protein (IAP/CD47) is a 50 kDa transmembrane protein initially defined as a regulator of ß3 integrin-mediated functions in neutrophils. IAP also can synergize with the TCR in T cell activation independent of ß3 integrins. To analyze the mechanism for IAP synergy with TCR, we expressed in Jurkat cells a chimeric molecule, consisting of the CD16 extracellular domain, the CD7 transmembrane domain and the TCR {zeta} chain cytoplasmic tail (CD16-7-{zeta}), which on its own is unable to induce IL-2 production. Ligation of IAP acted in synergy with TCR to induce IL-2 transcription and synthesis, but failed to synergize with the signal generated by CD16-7-{zeta}, while CD28 was a potent co-stimulator with both TCR and CD16-7-{zeta}. The failure of IAP to activate Jurkat together with CD16-7-{zeta} correlated with a lack of c-Jun N-terminal kinase, but not extracellular-signal-regulated kinase activation. Jurkat adhesion to anti-IAP, but not anti-CD28, induced cell spreading and the same domains of IAP required for augmentation of T cell activation were required to induce cell spreading. IAP synergy with TCR signaling likely results from its ability to stimulate adhesion to a ligand-expressing surface or antigen-presenting cell (APC), rather than from initiation of a novel signaling cascade. We conclude that a major role for ligation of IAP in T cell activation is to enhance the efficiency of TCR signaling by causing T cells to spread on an APC or surface.

Keywords: CD28, CD47, integrin-associated protein

1 Current address: Program in Microbial Pathogenesis and Host Defense, HSE 201, Campus Box 0513, University of California, 513 Parnassus Ave., San Francisco, CA 94143

Transmitting editor: D. Fearon


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