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Neutrophil elastase-dependent cleavage of LTA4H alters its aminopeptidase activity in cystic fibrosis
European Respiratory Journal ( IF 24.3 ) Pub Date : 2024-03-07 , DOI: 10.1183/13993003.01512-2023
Xin Xu , Jin-dong Li , Todd J. Green , Landon Wilson , Kristopher Genschmer , Derek Russell , J. Edwin Blalock , Amit Gaggar

Extract

The enzyme leukotriene A4 hydrolase (LTA4H) is classically known for its epoxide hydrolase activity that converts leukotriene A4 (LTA4) to the neutrophil chemoattractant LTB4 [1]. In 2010, our group published a study in Science that demonstrated that during an influenza model of acute airway inflammation, LTA4H was released from cells to degrade proline-glycine-proline (PGP), a non-canonical CXCR1 and -2 agonist of polymorphonuclear neutrophil (PMN) recruitment and activation [2], thereby attenuating PMN inflammation [3].



中文翻译:

囊性纤维化中中性粒细胞弹性蛋白酶依赖性 LTA4H 裂解改变其氨肽酶活性

提炼

白三烯 A 4水解酶(LTA4H) 因其环氧化物水解酶活性而闻名,可将白三烯 A 4 (LTA 4 ) 转化为中性粒细胞趋化剂 LTB 4 [1]。2010年,我们小组在《科学》杂志上发表了一项研究,证明在急性气道炎症的流感模型中,LTA4H从细胞中释放出来,降解脯氨酸-甘氨酸-脯氨酸(PGP),这是多形核中性粒细胞的非典型CXCR1和-2激动剂(PMN) 募集和激活 [2],从而减轻 PMN 炎症 [3]。

更新日期:2024-03-07
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