Heat shock protein 70B' (HSP70B') expression and release in response to human oxidized low density lipoprotein immune complexes in macrophages.

摘要: Heat shock proteins (HSPs) have been implicated in the activation and survival of macrophages. This study examined role HSP70B′, a poorly characterized member HSP70 family, response to oxidatively modified LDL (oxLDL) immune complexes prepared with human oxLDL purified antibodies (oxLDL-IC) monocytic macrophage cell lines. Immunoblot analysis lysates conditioned medium from U937 cells treated alone revealed an increase intracellular HSP70B′ protein levels accompanied by concomitant extracellular levels. Fluorescence immunohistochemistry confocal microscopy, however, demonstrated that oxLDL-IC stimulated release which co-localized cell-associated oxLDL-IC. In HSP70B′-green fluorescent protein-transfected mouse RAW 264.7 cells, oxLDL-IC-induced membrane-associated as well lipid moiety internalized Furthermore, data is involved survival, this effect could be mediated sphingosine kinase 1 (SK1) activation. An examination regularly cytokines significant relationship between anti-inflammatory cytokine interleukin-10 (IL-10). Small interfering RNA knockdown resulted corresponding decrease SK1 mRNA phosphorylation increased IL-10. conclusion, these findings suggest induce synthesis once stimulated, binds The also implicate key cellular functions, such regulation activity IL-10, influence survival.