By binding SIRPα or calreticulin/CD91, lung collectins act as dual function surveillance molecules to suppress or enhance inflammation
By binding SIRPα or calreticulin/CD91, lung collectins act as dual function surveillance molecules to suppress or enhance inflammation
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DOI：
10.1016/s0092-8674(03)00758-x
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发表时间：
2003-10-03
期刊：
影响因子：
64.5
通讯作者：
Henson, PM
中科院分区：
文献类型：
--
作者：
Gardai, SJ;Xiao, YQ;Henson, PM
表面活性剂蛋白A和D （SP-A和SP-D）是由两个区域组成的肺集合，一个结合PAMPs的球形头部结构域和一个启动吞噬的胶原尾部结构域。我们提供的证据表明，SP-A和SP-D以双重方式起作用，根据结合方向增强或抑制炎症介质的产生。SP-A和SP-D通过其球状头结合SIRPalpha，启动阻断促炎介质产生的信号通路。相反，它们的胶原尾通过结合钙调蛋白/CD91刺激促炎介质的产生。SP-A和SP-D通过球形头刺激驻留细胞上的SIRPalpha，从而帮助维持非/抗炎肺环境。然而，这些头部与外源生物或受损细胞上的PAMPs相互作用，以及胶原尾部以聚集状态呈现给钙网蛋白/CD91，会刺激吞噬和促炎反应。
Surfactant proteins A and D (SP-A and SP-D) are lung collectins composed of two regions, a globular head domain that binds PAMPs and a collagenous tail domain that initiates phagocytosis. We provide evidence that SP-A and SP-D act in a dual manner, to enhance or suppress inflammatory mediator production depending on binding orientation. SP-A and SP-D bind SIRPalpha through their globular heads to initiate a signaling pathway that blocks proinflammatory mediator production. In contrast, their collagenous tails stimulate proinflammatory mediator production through binding to calreticulin/CD91. Together a model is implied in which SP-A and SP-D help maintain a non/anti-inflammatory lung environment by stimulating SIRPalpha on resident cells through their globular heads. However, interaction of these heads with PAMPs on foreign organisms or damaged cells and presentation of the collagenous tails in an aggregated state to calreticulin/CD91, stimulates phagocytosis and proinflammatory responses.