Signal-regulatory protein is selectively expressed by myeloid and neuronal cells

S Adams, L J van der Laan, E Vernon-Wilson, C Renardel de Lavalette, E A Döpp, C D Dijkstra, D L Simmons, T K van den Berg

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Signal-regulatory proteins (SIRP) are transmembrane glycoproteins with three extracellular Ig-like domains, closely related to Ag receptors Ig, TCR, and MHC, and a cytoplasmic domain with two immunoreceptor with tyrosine-based inhibition motifs that can interact with src homology 2 domain-containing phosphatases. SIRP have previously been shown to inhibit signaling through receptor tyrosine kinases, but their physiologic function is unknown. Here we demonstrate by expression cloning that the mAbs ED9, ED17, and MRC-OX41 recognize rat SIRP. In addition, we show for the first time that rat SIRP is selectively expressed by myeloid cells (macrophages, monocytes, granulocytes, dendritic cells) and neurons. Moreover, SIRP ligation induces nitric oxide production by macrophages. This implicates SIRP as a putative recognition/signaling receptor in both immune and nervous systems.

Original languageEnglish
Pages (from-to)1853-9
Number of pages7
JournalJournal of Immunology
Issue number4
Publication statusPublished - 15 Aug 1998

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