...
首页> 外文期刊>The biochemical journal >Surfactant protein D (SP-D) counteracts the inhibitory effect of surfactant protein A (SP-A) on phospholipid secretion by alveolar type II cells. Interaction of native SP-D with SP-A
【24h】

Surfactant protein D (SP-D) counteracts the inhibitory effect of surfactant protein A (SP-A) on phospholipid secretion by alveolar type II cells. Interaction of native SP-D with SP-A

机译:表面活性剂蛋白D(SP-D)抵消了表面活性剂蛋白A(SP-A)对II型肺泡细胞磷脂分泌的抑制作用。本机SP-D与SP-A的交互

获取原文
           

摘要

pThe surfactant proteins SP-A and SP-D were obtained from rats given intratracheal instillation of silica. SP-D was isolated from the 33,000 g supernatant of rat bronchoalveolar lavage fluids, and we examined whether SP-D affects surfactant secretion by alveolar type II cells. Native SP-D affected neither basal secretion nor stimulated secretion by type II cells. However, native SP-D counteracted the inhibitory effect of SP-A on surfactant secretion in a concentration-dependent manner; however, SP-D failed to counteract the inhibitory effect of concanavalin A. The activity of SP-D was unaffected by inclusion of excess methyl alpha-mannoside. Excess native SP-D competed with 125I-SP-A for high-affinity binding to type II cells. Heat treatment of SP-D and antibody against SP-D both decreased SP-D activity. Butanol extraction of native SP-D was most effective at destroying SP-D activity and attenuated the ability of the protein to compete with labelled SP-A for binding to type II cells. The butanol-soluble fraction of SP-D possessed the ability to alter the inhibitory effect of SP-A to the same extent as native SP-D. Direct binding of 125I-SP-A on nitrocellulose sheets demonstrated that SP-A could bind native SP-D, but not butanol-extracted SP-D. We conclude that native SP-D alters SP-A activity in type II cells through interaction with it via SP-D-associated lipids./p
机译:>从经气管内滴注二氧化硅的大鼠获得表面活性剂蛋白SP-A和SP-D。从大鼠支气管肺泡灌洗液的33,000 g上清液中分离出SP-D,我们检查了SP-D是否影响II型肺泡细胞分泌的表面活性剂。天然SP-D既不影响基础分泌,也不影响II型细胞的刺激分泌。然而,天然SP-D以浓度依赖的方式抵消了SP-A对表面活性剂分泌的抑制作用。但是,SP-D无法抵消刀豆球蛋白A的抑制作用。SP-D的活性不受过量甲基α-甘露糖苷的影响。过量的天然SP-D与125I-SP-A竞争与II型细胞的高亲和力结合。 SP-D的热处理和针对SP-D的抗体均会降低SP-D活性。天然SP-D的丁醇萃取最有效地破坏SP-D活性,并减弱了蛋白质与标记SP-A竞争结合II型细胞的能力。 SP-D的丁醇可溶级分具有与天然SP-D相同程度地改变SP-A抑制作用的能力。 125I-SP-A在硝酸纤维素纸上的直接结合表明SP-A可以结合天然SP-D,但不能结合丁醇提取的SP-D。我们得出结论,天然SP-D通过与SP-D相关的脂质相互作用,从而改变II型细胞中SP-A的活性。

著录项

获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号