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Insect Cell Stimulation by LPS Requires the Activity of Cell-Released Proteases

机译:LPS刺激昆虫细胞需要细胞释放蛋白酶的活性。

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The hemocyte line BTI-EA-1174-Afrom the lepidopteran insect Estigmene acraea responds to bacterial lipopolysaccharide (LPS) by an enhanced phagocytic reaction and a dose-depen- dent increase of lysozyme release [Wittwer et al., Dev Comp [mmunoI21:323 (1997)]. This paper provides evidence for a strong proteolytic activ- ity in cell culture supernatants occuring after addition of LPS (1 mg/ml). The proteolysis is caused by cell-released proteases and seems to be necessary for cell activation. Its inhibition by IX2-macroglobulin results in a dose-dependent reduction in cel- lular response strength. Phagocytic reactions, as well as lysozyme release, are lowered to about half in the presence of [).0001 mg/ml ?2-macroglobulin. A nearly complete abolishment [)f activation was achieved with final concentrations of 1.0 mg/ ml ?2-macroglobulin. The data presented allow us to conclude that the LPS-triggered proteolytic activity is an important part [)f the activation process; it occurs outside of the cells and de- livers immune response activating factors. Arch. Insect Biochem. Physiol. 39:91-97, 1998.
机译:鳞翅目昆虫Est藜的血细胞系BTI-EA-1174-A通过增强的吞噬反应和溶菌酶释放的剂量依赖性反应来响应细菌脂多糖(LPS)[Wittwer等,Dev Comp [mmunoI21:323] (1997)]。本文提供了证据,表明加入LPS(1 mg / ml)后,细胞培养上清液具有很强的蛋白水解活性。蛋白水解是由细胞释放的蛋白酶引起的,似乎是细胞活化所必需的。 IX2-巨球蛋白对其的抑制导致细胞反应强度的剂量依赖性降低。在[] .0001mg /mlβ2-巨球蛋白的存在下,吞噬反应以及溶菌酶的释放降低到大约一半。最终浓度为1.0 mg / ml的β2-巨球蛋白实现了几乎完全的[] f活化。所提供的数据使我们得出结论,LPS触发的蛋白水解活性是激活过程的重要组成部分。它发生在细胞外,并提供免疫反应激活因子。拱。昆虫生化。生理学。 39:91-97,1998。

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