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首页> 外文期刊>Infection and immunity >Lactoferrin Inhibits the Lipopolysaccharide-Induced Expression and Proteoglycan-Binding Ability of Interleukin-8 in Human Endothelial Cells
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Lactoferrin Inhibits the Lipopolysaccharide-Induced Expression and Proteoglycan-Binding Ability of Interleukin-8 in Human Endothelial Cells

机译：乳铁蛋白抑制脂多糖诱导的人内皮细胞中白细胞介素8的表达和蛋白聚糖结合能力。

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Interleukin-8 (IL-8), a C-X-C chemokine bound to endothelium proteoglycans, initiates the activation and selective recruitment of leukocytes at inflammatory foci. We demonstrate that human lactoferrin, an antimicrobial lipopolysaccharide (LPS)-binding protein, decreases both IL-8 mRNA and protein expression induced by the complex Escherichia coli 055:B5 LPS/sCD14 in human umbilical vein endothelial cells. The use of recombinant lactoferrins mutated in the LPS-binding sites indicates that this inhibitory effect is mediated by an interaction of lactoferrin with LPS and CD14s that suppresses the endotoxin biological activity. Furthermore, since dimeric IL-8 and lactoferrin are both proteoglycan-binding molecules, the competition between these proteins for heparin binding was investigated. Lactoferrin strongly inhibited the interaction of radiolabeled IL-8 to immobilized heparin, whereas a lactoferrin variant lacking the amino acid residues essential for heparin binding was not inhibitory. Moreover, this process is specific, since serum transferrin, a glycoprotein whose structure is close to that of lactoferrin, did not prevent the interaction of IL-8 with heparin. These results suggest that the anti-inflammatory properties of lactoferrin during septicemia are related, at least in part, to the regulation of IL-8 production and also to the ability of lactoferrin to compete with chemokines for their binding to proteoglycans.
机译：白细胞介素8（IL-8）是一种与内皮蛋白聚糖结合的C-X-C趋化因子，可在炎症灶处启动白细胞的激活和选择性募集。我们证明，人乳铁蛋白，一种抗微生物脂多糖（LPS）结合蛋白，可降低人脐静脉内皮细胞复合物 Escherichia coli 055：B5 LPS / sCD14诱导的IL-8 mRNA和蛋白表达。 。在LPS结合位点突变的重组乳铁蛋白的使用表明，这种抑制作用是由乳铁蛋白与LPS和抑制内毒素生物学活性的CD14s相互作用介导的。此外，由于二聚体IL-8和乳铁蛋白都是蛋白聚糖结合分子，因此研究了这些蛋白之间对肝素结合的竞争。乳铁蛋白强烈抑制放射标记的IL-8与固定化肝素的相互作用，而缺乏肝素结合所必需的氨基酸残基的乳铁蛋白变体则不受抑制。此外，该过程是特异性的，因为血清转铁蛋白是一种结构接近乳铁蛋白的糖蛋白，并未阻止IL-8与肝素的相互作用。这些结果表明，败血症期间乳铁蛋白的抗炎特性至少部分与IL-8产生的调节有关，也与乳铁蛋白与趋化因子竞争结合蛋白多糖的能力有关。

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