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- W1968483896 abstract "BACKGROUND: We have shown that hemorrhagic shockactivated NADPH oxidase plays an important role in PMNmediated lung inflammation; however, this role is attenuated in TLR4-mutant C3H/HeJ mice. The mechanism of hemorrhageinduced activation of NADPH oxidase remains unclear. Here, we hypothesized that hemorrhagic shock activates PMN NADPH oxidase through HMGB1, an endogenous ligand of TLR4. METHODS: Wild-type (WT) and C3H/HeJ mice were bled to a MAP of 40 mmHg, maintained for 2h, then resuscitated with shed blood and Ringer's lactate. PMN were then isolated from blood 2 h after resuscitation, and NADPH oxidase activation in the PMN was measured by detecting the formation of gp91phox-p47phox complex using immunoprecipitation and Western blot. In some experiments, anti-HMGB1 Ab (600 μg/mouse) or control IgG was injected i.p. to the mice before hemorrhage to address the role of HMGB1 in mediating NADPH oxidase activation. RESULTS: Hemorrhagic shock markedly increased PMN NADPH oxidase activation in WT mice, whereas in C3H/HeJ mice hemorrhage failed to activate the NADPH oxidase (Fig. A). Anti-HMGB1 Ab significantly attenuated the hemorrhage-induced activation of PMN NADPH oxidase in WT mice (Fig. B).Fig. 1: (HeJ: C3H/HeJ mice; Ab: anti-HMGB1 Ab; p47phox: gp91phox-p47phox complex was immunoprecipitated with anti-gp91phox Ab, and then probed with anti-p47phox Ab.)CONCLUSION: TLR4 signaling activated by HMGB1 is an important determinant of hemorrhagic shock-induced activation of PMN NDAPH oxidase." @default.
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- W1968483896 date "2006-06-01" @default.
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- W1968483896 title "TLR4 MEDIATES HEMORRHAGIC SHOCK-INDUCED NADPH OXIDASE ACTIVATION IN NEUTROPHIL" @default.
- W1968483896 doi "https://doi.org/10.1097/00024382-200606001-00188" @default.
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