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Category:Linux-only softwareNAD(P)H oxidase-derived superoxide is critical for the activation of hematopoietic stem cells by the stromal cell-derived factor 1 (SDF-1).
Stromal cell-derived factor-1 (SDF-1) is expressed by bone marrow stromal cells (BMSCs) and acts on hematopoietic stem cells (HSCs) by binding to the CXCR4 receptor. The functional consequences of this interaction are controversial: some authors have demonstrated that SDF-1 increases HSC migration through activation of NAD(P)H oxidase, whereas others have reported that SDF-1 does not influence the migration and homing of HSCs to bone marrow. In this study, we have shown that superoxide, produced by the Nox2 NAD(P)H oxidase, is critical for SDF-1-mediated activation of HSCs. As expected, SDF-1 induced migration of HSCs and subsequent differentiation to the monocytic lineage, which was blocked by GKT137831, a novel potent and selective inhibitor of Nox2. This effect was mediated by the increased expression of CXCR4. Furthermore, SDF-1 induced the NAD(P)H oxidase-dependent production of superoxide, which was not related to cell migration, as was the case for Nox2-derived superoxide. Moreover, SDF-1 stimulated the chemotaxis of cultured monocytes. All of these responses were blocked by the Nox2-specific inhibitors, GKT137831 and APO866, or by genetic ablation of Nox2 in bone marrow-derived macrophages. Taken together, these findings demonstrate that Nox2-derived superoxide is an important mediator of SDF-1-mediated activation of hematopoietic cells.Q:
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