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J Biol Chem, Vol. 274, Issue 45, 32493-32499, November 5, 1999

Signal Regulatory Proteins Negatively Regulate Immunoreceptor-dependent Cell Activation

From the Laboratoire d'Immunologie Cellulaire et Clinique, INSERM U.255, Institut Curie, 75005 Paris, France

Signal regulatory proteins of the  subtype (SIRP) are ubiquitous molecules of the immunoglobulin superfamily that negatively regulate protein tyrosine kinase receptor-dependent cell proliferation. Their intracytoplasmic domain contains four motifs that resemble immunoreceptor tyrosine-based inhibition motifs (ITIMs) and that, when tyrosyl-phosphorylated, recruit cytoplasmic SH2 domain-bearing protein tyrosine phosphatases (SHPs). ITIMs are borne by molecules that negatively regulate cell activation induced by receptors bearing immunoreceptor tyrosine-based activation motifs (ITAMs). Because SIRP are coexpressed with ITAM-bearing receptors in hematopoietic cells, we investigated whether SIRP could negatively regulate ITAM-dependent cell activation. We found SIRP transcripts in human mast cells, and we show that a chimeric molecule having the transmembrane and intracytoplasmic domains of SIRP could inhibit IgE-induced mediator secretion and cytokine synthesis by mast cells. Inhibition required that the SIRP chimera was coaggregated with ITAM-bearing high affinity IgE receptors (FcRI). It was correlated with the tyrosyl phosphorylation of the SIRP chimera and the recruitment of SHP-1 and SHP-2. The phosphorylation of FcRI ITAMs was decreased; the mobilization of intracellular Ca²⁺ and the influx of extracellular Ca²⁺ were reduced, and the activation of the mitogen-activated protein kinases Erk1 and Erk2 was abolished. SIRP can therefore negatively regulate not only receptor tyrosine kinase-dependent cell proliferation but also ITAM-dependent cell activation.

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