C7 is expressed on endothelial cells as a trap for the assembling terminal complement complex and may exert anti-inflammatory function
C7 is expressed on endothelial cells as a trap for the assembling terminal complement complex and may exert anti-inflammatory function
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DOI：
10.1182/blood-2008-03-146472
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发表时间：
2009-04-09
期刊：
影响因子：
20.3
通讯作者：
Tedesco, Francesco
中科院分区：
文献类型：
--
作者：
Bossi, Fleur;Rizzi, Lucia;Tedesco, Francesco
我们描述了C7作为内皮细胞(ECs)膜结合分子的一种新的定位。经十二烷基硫酸钠-聚丙烯酰胺凝胶电泳法(SDS-PAGE)、Western印迹分析、Northern印迹分析和质谱学分析表明，膜相关C7(MC7)与可溶性C7无明显区别，而与细胞表面的波形蛋白有关。MC7与其他晚期补体成分相互作用形成膜结合型TCC(MTCC)。与可溶性的SC5b-9不同，mTCC不能刺激内皮细胞表达黏附分子，分泌IL-8，也不能通过单层内皮细胞诱导白蛋白渗漏，更重要的是保护内皮细胞免受SC5b-9的促炎作用。我们的数据揭示了mC7作为晚期补体成分的陷阱来控制SC5b-9引起的过度炎症的新角色的可能性。(血。2009；113：3640-3648)
We describe a novel localization of C7 as a membrane-bound molecule on endothelial cells (ECs). Data obtained by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), Western blot analysis, Northern blot analysis, and mass spectrometry revealed that membrane-associated C7 (mC7) was indistinguishable from soluble C7 and was associated with vimentin on the cell surface. mC7 interacted with the other late complement components to form membrane-bound TCC (mTCC). Unlike the soluble SC5b-9, mTCC failed to stimulate ECs to express adhesion molecules, to secrete IL-8, and to induce albumin leakage through a monolayer of ECs, and more importantly protected ECs from the proinflammatory effect of SC5b-9. Our data disclose the possibility of a novel role of mC7 that acts as a trap for the late complement components to control excessive inflammation induced by SC5b-9. (Blood. 2009; 113: 3640-3648)