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The Inhibitory Receptor PIR-B Negatively Regulates Neutrophil and Macrophage Integrin Signaling¹

Shalini Pereira^*, Hong Zhang^*, Toshiyuki Takai and Clifford A. Lowell^2,*

^* Department of Laboratory Medicine, University of California, San Francisco, CA 94143; and Department of Experimental Immunology, Institute of Development, Aging and Cancer, Tohoku University, Sendai, Japan

The Ig-like receptor family member, PIR-B, has been shown to play an inhibitory role in receptor signaling within B cells, mast cells, and dendritic cells. As it has been implicated in integrin-mediated responses, we investigated the effect of loss of the PIR-B protein on integrin-mediated signaling in primary murine myeloid cells. The pir-b^–/– neutrophils displayed enhanced respiratory burst, secondary granule release, and a hyperadhesive phenotype when plated on surfaces coated with either extracellular matrix proteins or cellular adhesion molecules in the presence or absence of the soluble inflammatory agonist TNF-. The pir-b^–/– and wild-type cells responded equivalently when stimulated with TNF- in suspension, indicating that the hyperresponsive phenotype of the pir-b^–/– cells during adhesion was due to enhanced integrin signaling. Both wild-type and pir-b^–/– neutrophils expressed similar levels of integrin subunits. Primary bone marrow-derived macrophages from pir-b^–/– mice were also hyperadhesive and spread more rapidly than wild-type cells following plating on surfaces that cross-linked cellular ₂ integrins. Biochemical analysis of macrophages from pir-b^–/– mice revealed enhanced phosphorylation and activation of proteins involved in integrin signaling. These observations point to a nonredundant role for PIR-B in the regulation of leukocyte integrin signaling.

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