| First Author | Pereira S | Year | 2004 |
| Journal | J Immunol | Volume | 173 |
| Issue | 9 | Pages | 5757-65 |
| PubMed ID | 15494528 | Mgi Jnum | J:93766 |
| Mgi Id | MGI:3505662 | Doi | 10.4049/jimmunol.173.9.5757 |
| Citation | Pereira S, et al. (2004) The inhibitory receptor PIR-B negatively regulates neutrophil and macrophage integrin signaling. J Immunol 173(9):5757-65 |
| abstractText | 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-alpha. The pir-b-/- and wild-type cells responded equivalently when stimulated with TNF-alpha 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 beta2 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. |
