A highly conserved host lipase deacylates oxidized phospholipids and ameliorates acute lung injury in mice

Oxidized phospholipids have diverse biological activities, many of which can be pathological, yet how they are inactivated in vivo is not fully understood. Here, we present evidence that a highly conserved host lipase, acyloxyacyl hydrolase (AOAH), can play a significant role in reducing the pro-inf...

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Bibliographic Details
Main Authors: Benkun Zou, Michael Goodwin, Danial Saleem, Wei Jiang, Jianguo Tang, Yiwei Chu, Robert S Munford, Mingfang Lu
Format: article
Language:EN
Published: eLife Sciences Publications Ltd 2021
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Online Access:https://doaj.org/article/8336c58698cd4c66a2824f8ee4b95e13
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Summary:Oxidized phospholipids have diverse biological activities, many of which can be pathological, yet how they are inactivated in vivo is not fully understood. Here, we present evidence that a highly conserved host lipase, acyloxyacyl hydrolase (AOAH), can play a significant role in reducing the pro-inflammatory activities of two prominent products of phospholipid oxidation, 1-palmitoyl-2-glutaryl-sn-glycero-3-phosphocholine and 1-palmitoyl-2-(5-oxovaleroyl)-sn-glycero-3-phosphocholine. AOAH removed the sn-2 and sn-1 acyl chains from both lipids and reduced their ability to induce macrophage inflammasome activation and cell death in vitro and acute lung injury in mice. In addition to transforming Gram-negative bacterial lipopolysaccharide from stimulus to inhibitor, its most studied activity, AOAH can inactivate these important danger-associated molecular pattern molecules and reduce tissue inflammation and injury.