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Intracellular and extracellular enzymatic deacylation of bacterial endotoxin during localized inflammation induced by Escherichia coli.

机译:大肠杆菌诱导的局部炎症过程中细菌内毒素的细胞内和细胞外酶促脱酰作用。

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Acyloxyacyl hydrolase (AOAH), an enzyme that removes the secondary acyl chains of gram-negative bacterial lipid A (endotoxin), has been identified previously in human neutrophils and mouse macrophages. We report here that bovine leukocytes also contain AOAH activity. Although bovine AOAH deacylates bacterial lipopolysaccharide in a manner similar to human AOAH, it is active in vitro over a broader pH range, from 4.0 to 7.0. By using Escherichia coli infection of the bovine mammary gland as a model of localized gram-negative bacterial disease and associated tissue inflammation, AOAH activity per leukocyte increased. In addition, AOAH activity increased in the cell-free portion of infected mammary secretions. These data indicate that AOAH activity increases in leukocytes associated with inflammation induced by gram-negative bacteria and provide additional evidence of its potential involvement in the defense against the effects of bacterial endotoxin.
机译:乙酰氧酰水解酶(AOAH)是一种去除革兰氏阴性细菌脂质A(内毒素)的次级酰基链的酶,先前已在人嗜中性粒细胞和小鼠巨噬细胞中得到鉴定。我们在这里报告牛白细胞也含有AOAH活性。尽管牛AOAH以类似于人AOAH的方式使细菌脂多糖脱酰,但它在4.0至7.0的较宽pH范围内具有体外活性。通过使用牛乳腺的大肠杆菌感染作为局部革兰氏阴性细菌疾病和相关组织炎症的模型,每个白细胞的AOAH活性增加。另外,在感染的乳腺分泌物的无细胞部分中,AOAH活性增加。这些数据表明,与革兰氏阴性细菌引起的炎症相关的白细胞中的AOAH活性增加,并提供了其潜在参与防御细菌内毒素作用的其他证据。

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